1. Beta-Alanyl-L-histidine
2. Carnosine
3. Ignotine
4. Karnozin
5. Karnozzn
6. L-Carnosine
7. N-(3-Aminopropanoyl)histidine
8. N-(b-Alanyl)-L-histidine
9. N-b-alanyl-L-Histidine
10. N-beta-alanyl-L-Histidine
11. b-Alanyl-L-histidine
12. b-Alanylhistidine
13. beta-Alanylhistidine
14. Sevitin

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• Cytoplasm

• Blood
• Urine

• 104300 (Alzheimer's disease)
• 212200 (Carnosinuria)

1. Park YJ, Volpe SL, Decker EA: Quantitation of carnosine in humans plasma after dietary consumption of beef. J Agric Food Chem. 2005 Jun 15;53(12):4736-9. [PubMed ]
2. Guiotto A, Calderan A, Ruzza P, Borin G: Carnosine and carnosine-related antioxidants: a review. Curr Med Chem. 2005;12(20):2293-315. [PubMed ]
3. Hipkiss AR, Preston JE, Himsworth DT, Worthington VC, Keown M, Michaelis J, Lawrence J, Mateen A, Allende L, Eagles PA, Abbott NJ: Pluripotent protective effects of carnosine, a naturally occurring dipeptide. Ann N Y Acad Sci. 1998 Nov 20;854:37-53. [PubMed ]
4. Guiotto A, Calderan A, Ruzza P, Osler A, Rubini C, Jo DG, Mattson MP, Borin G: Synthesis and evaluation of neuroprotective alpha,beta-unsaturated aldehyde scavenger histidyl-containing analogues of carnosine. J Med Chem. 2005 Sep 22;48(19):6156-61. [PubMed ]
5. Hipkiss AR, Brownson C: Carnosine reacts with protein carbonyl groups: another possible role for the anti-ageing peptide? Biogerontology. 2000;1(3):217-23. [PubMed ]
6. Furst P: Amino acid metabolism in uremia. J Am Coll Nutr. 1989 Aug;8(4):310-23. [PubMed ]
7. Lee YT, Hsu CC, Lin MH, Liu KS, Yin MC: Histidine and carnosine delay diabetic deterioration in mice and protect human low density lipoprotein against oxidation and glycation. Eur J Pharmacol. 2005 Apr 18;513(1-2):145-50. Epub 2005 Apr 2. [PubMed ]
8. Hipkiss AR, Brownson C, Bertani MF, Ruiz E, Ferro A: Reaction of carnosine with aged proteins: another protective process? Ann N Y Acad Sci. 2002 Apr;959:285-94. [PubMed ]
9. Mannion AF, Jakeman PM, Dunnett M, Harris RC, Willan PL: Carnosine and anserine concentrations in the quadriceps femoris muscle of healthy humans. Eur J Appl Physiol Occup Physiol. 1992;64(1):47-50. [PubMed ]
10. Hipkiss AR, Brownson C, Carrier MJ: Carnosine, the anti-ageing, anti-oxidant dipeptide, may react with protein carbonyl groups. Mech Ageing Dev. 2001 Sep 15;122(13):1431-45. [PubMed ]
11. Suzuki Y, Ito O, Mukai N, Takahashi H, Takamatsu K: High level of skeletal muscle carnosine contributes to the latter half of exercise performance during 30-s maximal cycle ergometer sprinting. Jpn J Physiol. 2002 Apr;52(2):199-205. [PubMed ]
12. Kang JH, Kim KS, Choi SY, Kwon HY, Won MH, Kang TC: Protection by carnosine-related dipeptides against hydrogen peroxide-mediated ceruloplasmin modification. Mol Cells. 2002 Feb 28;13(1):107-12. [PubMed ]
13. Willi SM, Zhang Y, Hill JB, Phelan MC, Michaelis RC, Holden KR: A deletion in the long arm of chromosome 18 in a child with serum carnosinase deficiency. Pediatr Res. 1997 Feb;41(2):210-3. [PubMed ]
14. Tallon MJ, Harris RC, Boobis LH, Fallowfield JL, Wise JA: The carnosine content of vastus lateralis is elevated in resistance-trained bodybuilders. J Strength Cond Res. 2005 Nov;19(4):725-9. [PubMed ]
15. Mozdzan M, Szemraj J, Rysz J, Nowak D: Antioxidant properties of carnosine re-evaluated with oxidizing systems involving iron and copper ions. Basic Clin Pharmacol Toxicol. 2005 May;96(5):352-60. [PubMed ]
16. Jackson MC, Lenney JF: The distribution of carnosine and related dipeptides in rat and human tissues. Inflamm Res. 1996 Mar;45(3):132-5. [PubMed ]
17. Wikipedia

1. Myeloperoxidase precursor
2. Beta-Ala-His dipeptidase precursor
3. Histidine decarboxylase
4. Vimentin
5. Heat shock 70 kDa protein 1
6. Oligopeptide transporter, kidney isoform

1. MPO[Contains: 89 kDa myeloperoxidase
2. 84 kDa myeloperoxidase
3. Myeloperoxidase light chain
4. Myeloperoxidase heavy chain]

MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTS
LVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLH
VALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMC
NNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTD
QLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPND
PRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQL
GLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLL
REHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYR
SYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLE
GGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYN
AWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPL
LACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMS
NSYPRDFVNCSTLPALNLASWREAS

• Arachidonic acid metabolism (map00590 )
• Methane metabolism (map00680 )
• Phenylalanine Metabolism (map00360 )
• Stilbene, coumarine and lignin biosynthesis (map00940 )

• donor + H2O2 = oxidized donor + 2 H2O

• An_peroxidase (PF03098 )

• None

• None

ATGGGGGTTCCCTTCTTCTCTTCTCTCAGATGCATGGTGGACTTAGGACCTTGCTGGGCT
GGGGGTCTCACTGCAGAGATGAAGCTGCTTCTGGCCCTAGCAGGGCTCCTGGCCATTCTG
GCCACGCCCCAGCCCTCTGAAGGTGCTGCTCCAGCTGTCCTGGGGGAGGTGGACACCTCG
TTGGTGCTGAGCTCCATGGAGGAGGCCAAGCAGCTGGTGGACAAGGCCTACAAGGAGCGG
CGGGAAAGCATCAAGCAGCGGCTTCGCAGCGGCTCAGCCAGCCCCATGGAACTCCTATCC
TACTTCAAGCAGCCGGTGGCAGCCACCAGGACGGCGGTGAGGGCCGCTGACTACCTGCAC
GTGGCTCTAGACCTGCTGGAGAGGAAGCTGCGGTCCCTGTGGCGAAGGCCATTCAATGTC
ACTGATGTGCTGACGCCCGCCCAGCTGAATGTGTTGTCCAAGTCAAGCGGCTGCGCCTAC
CAGGACGTGGGGGTGACTTGCCCGGAGCAGGACAAATACCGCACCATCACCGGGATGTGC
AACAACAGACGCAGCCCCACGCTGGGGGCCTCCAACCGTGCCTTTGTGCGCTGGCTGCCG
GCGGAGTATGAGGACGGCTTCTCTCTTCCCTACGGCTGGACGCCCGGGGTCAAGCGCAAC
GGCTTCCCGGTGGCTCTGGCTCGCGCGGTCTCCAACGAGATCGTGCGCTTCCCCACTGAT
CAGCTGACTCCGGACCAGGAGCGCTCACTCATGTTCATGCAATGGGGCCAGCTGTTGGAC
CACGACCTCGACTTCACCCCTGAGCCGGCCGCCCGGGCCTCCTTCGTCACTGGCGTCAAC
TGCGAGACCAGCTGCGTTCAGCAGCCGCCCTGCTTCCCGCTCAAGATCCCGCCCAATGAC
CCCCGCATCAAGAACCAAGCCGACTGCATCCCGTTCTTCCGCTCCTGCCCGGCTTGCCCC
GGGAGCAACATCACCATCCGCAACCAGATCAACGCGCTCACTTCCTTCGTGGACGCCAGC
ATGGTGTACGGCAGCGAGGAGCCCCTGGCCAGGAACCTGCGCAACATGTCCAACCAGCTG
GGGCTGCTGGCCGTCAACCAGCGCTTCCAAGACAACGGCCGGGCCCTGCTGCCCTTTGAC
AACCTGCACGATGACCCCTGTCTCCTCACCAACCGCTCAGCGCGCATCCCCTGCTTCCTG
GCAGGGGACACCCGTTCCAGTGAGATGCCCGAGCTCACCTCCATGCACACCCTCTTACTT
CGGGAGCACAACCGGCTGGCCACAGAGCTCAAGAGCCTGAACCCTAGGTGGGATGGGGAG
AGGCTCTACCAGGAAGCCCGGAAGATCGTGGGGGCCATGGTCCAGATCATCACTTACCGG
GACTACCTGCCCCTGGTGCTGGGGCCAACGGCCATGAGGAAGTACCTGCCCACGTACCGT
TCCTACAATGACTCAGTGGACCCACGCATCGCCAACGTCTTCACCAATGCCTTCCGCTAC
GGCCACACCCTCATCCAACCCTTCATGTTCCGCCTGGACAATCGGTACCAGCCCATGGAA
CCCAACCCCCGTGTCCCCCTCAGCAGGGTCTTTTTTGCCTCCTGGAGGGTCGTGCTGGAA
GGTGGCATTGACCCCATCCTCCGGGGCCTCATGGCCACCCCTGCCAAGCTGAATCGTCAG
AACCAAATTGCAGTGGATGAGATCCGGGAGCGATTGTTTGAGCAGGTCATGAGGATTGGG
CTGGACCTGCCTGCTCTGAACATGCAGCGCAGCAGGGACCACGGCCTCCCAGGATACAAT
GCCTGGAGGCGCTTCTGTGGGCTCCCGCAGCCTGAAACTGTGGGCCAGCTGGGCACGGTG
CTGAGGAACCTGAAATTGGCGAGGAAACTGATGGAGCAGTATGGCACGCCCAACAACATC
GACATCTGGATGGGCGGCGTGTCCGAGCCTCTGAAGCGCAAAGGCCGCGTGGGCCCACTC
CTCGCCTGCATCATCGGTACCCAGTTCAGGAAGCTCCGGGATGGTGATCGGTTTTGGTGG
GAGAACGAGGGTGTGTTCAGCATGCAGCAGCGACAGGCCCTGGCCCAGATCTCATTGCCC
CGGATCATCTGCGACAACACAGGCATCACCACCGTGTCTAAGAACAACATCTTCATGTCC
AACTCATATCCCCGGGACTTTGTCAACTGCAGTACACTTCCTGCATTGAACCTGGCTTCC
TGGAGGGAAGCCTCCTAG

1. Morishita K, Kubota N, Asano S, Kaziro Y, Nagata S: Molecular cloning and characterization of cDNA for human myeloperoxidase. J Biol Chem. 1987 Mar 15;262(8):3844-51. [PubMed ]
2. Morishita K, Tsuchiya M, Asano S, Kaziro Y, Nagata S: Chromosomal gene structure of human myeloperoxidase and regulation of its expression by granulocyte colony-stimulating factor. J Biol Chem. 1987 Nov 5;262(31):15208-13. [PubMed ]
3. Johnson KR, Nauseef WM, Care A, Wheelock MJ, Shane S, Hudson S, Koeffler HP, Selsted M, Miller C, Rovera G: Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species. Nucleic Acids Res. 1987 Mar 11;15(5):2013-28. [PubMed ]
4. Johnson K, Gemperlein I, Hudson S, Shane S, Rovera G: Complete nucleotide sequence of the human myeloperoxidase gene. Nucleic Acids Res. 1989 Oct 11;17(19):7985-6. [PubMed ]
5. Seto P, Hirayu H, Magnusson RP, Gestautas J, Portmann L, DeGroot LJ, Rapoport B: Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase. J Clin Invest. 1987 Oct;80(4):1205-8. [PubMed ]
6. Hashinaka K, Nishio C, Hur SJ, Sakiyama F, Tsunasawa S, Yamada M: Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation. Biochemistry. 1988 Aug 9;27(16):5906-14. [PubMed ]
7. Hosokawa Y, Kawaguchi R, Hikiji K, Yamada M, Suzuki K, Nakagawa T, Yoshihara T, Yamaguchi K: Cloning and characterization of four types of cDNA encoding myeloperoxidase from human monocytic leukemia cell line, SKM-1. Leukemia. 1993 Mar;7(3):441-5. [PubMed ]
8. Yamada M, Yoshida M, Hashinaka K: Identification of transcriptional cis-elements in introns 7 and 9 of the myeloperoxidase gene. J Biol Chem. 1993 Jun 25;268(18):13479-85. [PubMed ]
9. Yamada M, Hur SJ, Hashinaka K, Tsuneoka K, Saeki T, Nishio C, Sakiyama F, Tsunasawa S: Isolation and characterization of a cDNA coding for human myeloperoxidase. Arch Biochem Biophys. 1987 May 15;255(1):147-55. [PubMed ]
10. Yamada M, Hur SJ, Toda H: Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures. Biochem Biophys Res Commun. 1990 Jan 30;166(2):852-9. [PubMed ]
11. Fiedler TJ, Davey CA, Fenna RE: X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. J Biol Chem. 2000 Apr 21;275(16):11964-71. [PubMed ]
12. Fenna R, Zeng J, Davey C: Structure of the green heme in myeloperoxidase. Arch Biochem Biophys. 1995 Jan 10;316(1):653-6. [PubMed ]
13. Blair-Johnson M, Fiedler T, Fenna R: Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution. Biochemistry. 2001 Nov 20;40(46):13990-7. [PubMed ]
14. Kizaki M, Miller CW, Selsted ME, Koeffler HP: Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency. Blood. 1994 Apr 1;83(7):1935-40. [PubMed ]
15. Nauseef WM, Brigham S, Cogley M: Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan. J Biol Chem. 1994 Jan 14;269(2):1212-6. [PubMed ]
16. Nauseef WM, Cogley M, McCormick S: Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase. J Biol Chem. 1996 Apr 19;271(16):9546-9. [PubMed ]
17. DeLeo FR, Goedken M, McCormick SJ, Nauseef WM: A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation. J Clin Invest. 1998 Jun 15;101(12):2900-9. [PubMed ]
18. Romano M, Dri P, Dadalt L, Patriarca P, Baralle FE: Biochemical and molecular characterization of hereditary myeloperoxidase deficiency. Blood. 1997 Nov 15;90(10):4126-34. [PubMed ]

1. Boldyrev A, Abe H, Stvolinsky S, Tyulina O: Effects of carnosine and related compounds on generation of free oxygen species: a comparative study. Comp Biochem Physiol B Biochem Mol Biol. 1995 Nov;112(3):481-5. [PubMed ]

1. Carnosine dipeptidase 1
2. CNDP dipeptidase 1
3. Serum carnosinase
4. Glutamate carboxypeptidase-like protein 2

MDPKLGRMAASLLAVLLLLLERGMFSSPSPPPALLEKVFQYIDLHQDEFVQTLKEWVAIE
SDSVQPVPRFRQELFRMMAVAADTLQRLGARVASVDMGPQQLPDGQSLPIPPVILAELGS
DPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAF
RALEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLWISQRKPAIT
YGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGHILVPGIYDEVV
PLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGIEGAFDEPG
TKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIA
NIDDTQYLAAKRAIRTVFGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQ
NEKINRWNYIEGTKLFAAFFLEMAQLH

• Beta Alanine Metabolism (map00410 )
• Histidine Metabolism (map00340 )

• Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine

• M20_dimer (PF07687 )
• Peptidase_M20 (PF01546 )

• 1-26

ATGGATCCCAAACTCGGGAGAATGGCTGCGTCCCTGCTGGCTGTGCTGCTGCTGCTGCTG
CTGGAGCGCGGCATGTTCTCCTCACCCTCCCCGCCCCCGGCGCTGTTAGAGAAAGTCTTC
CAGTACATTGACCTCCATCAGGATGAATTTGTGCAGACGCTGAAGGAGTGGGTGGCCATC
GAGAGCGACTCTGTCCAGCCTGTGCCTCGCTTCAGACAAGAGCTCTTCAGAATGATGGCC
GTGGCTGCGGACACGCTGCAGCGCCTGGGGGCCCGTGTGGCCTCGGTGGACATGGGTCCT
CAGCAGCTGCCCGATGGTCAGAGTCTTCCAATACCTCCCGTCATCCTGGCCGAACTGGGG
AGCGATCCCACGAAAGGCACCGTGTGCTTCTACGGCCACTTGGACGTGCAGCCTGCTGAC
CGGGGCGATGGGTGGCTCACGGACCCCTATGTGCTGACGGAGGTAGGCGGGAAACTTTAT
GGACGAGGAGCGACCGACAACAAAGGCCCTGTCTTGGCTTGGATCAATGCTGTGAGCGCC
TTCAGAGCCCTGGAGCAAGATCTTCCTGTGAATATCAAATTCATCATTGAGGGGATGGAA
GAGGCTGGCTCTGTTGCCCTGGAGGAACTTGTGGAAAAAGAAAAGGACCGATTCTTCTCT
GGTGTGGACTACATTGTAATTTCAGATAACCTGTGGATCAGCCAAAGGAAGCTAGCAATC
ACTTACGGAACCCGGGGGAACAGCTACTTCATGGTGGAGGTGAAATGCAGAGACCAGGAT
TTTCACTCAGGAACCTTTGGTGGCATCCTTCATGAACTAATGGCTGATCTGGTTGCTCTT
CTCGGTAGCCTGGTAGACTCGTCTGGTCATATCCTGGTCCCTGGAATCTATGATGAAGTG
GTTCCTCTTACAGAAGAGGAAATAAATACATACAAAGCCATCCATCTAGACCTAGAAGAA
TACCGGAATAGCAGCCGGGTTGAGAAATTTCTGTTCGATACTAAGGAGGAGATTCTAATG
CACCTCTGGAGGTACCCATCTCTTTCTATTCATGGGATCGAGGGCGCGTTTGATGAGCCT
GGAACTAAAACAGTCATACCTGGCCGAGTTATAGGAAAATTTTCAATCCGTCTAGTCCCT
CACATGAATGTGTCTGCGGTGGAAAAACAGGTGACACGACATCTTGAAGATGTGTTCTCC
AAAAGAAATAGTTCCAACAAGATGGTTGTTTCCATGACTCTAGGACTACACCCGTGGATT
GCAAATATTGATGACACTCAGTATCTCGCAGCAAAAAGAGCGATCAGAACAGTGTTTGGA
ACAGAACCAGATATGATCCGGGATGGATCCACCATTCCAATTGCCAAAATGTTCCAGGAG
ATCGTCCACAAGAGCGTGGTGCTAATTCCGCTGGGAGCTGTTGATGATGGAGAACATTCG
CAGAATGAGAAAATCAACAGGTGGAACTACATAGAGGGAACCAAATTATTTGCTGCCTTT
TTCTTAGAGATGGCCCAGCTCCATTAA

1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]

1. HDC

MMEPEEYRERGREMVDYICQYLSTVRERRVTPDVQPGYLRAQLPESAPEDPDSWDSIFGD
IERIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNVM
DWLAKMLGLPEHFLHHHPSSQGGGVLQSTVSESTLIALLAARKNKILEMKTSEPDADESC
LNARLVAYASDQAHSSVEKAGLISLVKMKFLPVDDNFSLRGEALQKAIEEDKQRGLVPVF
VCATLGTTGVCAFDCLSELGPICAREGLWLHIDAAYAGTAFLCPEFRGFLKGIEYADSFT
FNPSKWMMVHFDCTGFWVKDKYKLQQTFSVNPIYLRHANSGVATDFMHWQIPLSRRFRSV
KLWFVIRSFGVKNLQAHVRHGTEMAKYFESLVRNDPSFEIPAKRHLGLVVFRLKGPNCLT
ENVLKEIAKAGRLFLIPATIQDKLIIRFTVTSQFTTRDDILRDWNLIRDAATLILSQHCT
SQPSPRVGNLISQIRGARAWACGTSLQSVSGAGDDPVQARKIIKQPQRVGAGPMKRENGL
HLETLLDPVDDCFSEEAPDATKHKLSSFLFSYLSVQTKKKTVRSLSCNSVPVSAQKPLPT
EASVKNGGSSRVRIFSRFPEDMMMLKKSAFKKLIKFYSVPSFPECSSQCGLQLPCCPLQA
MV

• Histidine Metabolism (map00340 )

• L-histidine = histamine + CO2

• Pyridoxal_deC (PF00282 )

• None

• None

ATGATGGAGCCTGAGGAGTACAGAGAGAGAGGGAGAGAGATGGTGGATTACATCTGCCAG
TACCTGAGCACTGTGCGGGAGAGACGTGTGACGCCAGACGTGCAGCCTGGCTACCTGCGA
GCCCAGCTGCCTGAGAGTGCTCCTGAGGACCCCGACAGCTGGGACAGCATCTTTGGGGAC
ATTGAACGAATCATCATGCCTGGGGTGGTACATTGGCAGAGCCCCCATATGCACGCCTAC
TACCCAGCCCTCACCTCTTGGCCCTCCCTGCTAGGAGACATGCTGGCTGATGCCATCAAC
TGCTTGGGATTCACCTGGGCATCCAGCCCTGCGTGTACAGAGCTGGAGATGAACGTCATG
GACTGGTTGGCAAAAATGCTGGGACTTCCAGAGCACTTCTTGCACCACCACCCCAGCAGC
CAGGGCGGAGGCGTCCTGCAGCAGACGGTCAGTGAATCCACTTTGATTGCCCTGCTGGCA
GCAAGGAAGAACAAAATCCTGGAAATGAAAACGTCTGAGCCCGATGCTGATGAGTCCTGC
CTAAATGCCCGACTCGTGGCCTATGCCTCTGACCAGGCTCACTCCTCTGTGGAAAAGGCT
GGTTTGATTTCCCTTGTGAAGATGAAATTTCTGCCTGTGGATGACAACTTCTCACTCCGA
GGGGAAGCTCTTCAGAAGGCCATCGAGGAAGACAAGCAGCGGGGCTTGGTGCCCGTCTTT
GTCTGTGCAACACTAGGGACCACTGGGGTCTGTGCATTTGACTGCCTGTCAGAGCTGGGC
CCCATCTGTGCCCGTGAGGGGCTGTGGCTCCACATCGATGCTGCTTATGCAGGCACTGCC
TTCCTGTGCCCCGAGTTCCGGGGGTTTCTGAAGGGGATTGAGTATGCCGACTCCTTCACC
TTTAATCCTTCCAAGTGGATGATGGTGCATTTTGACTGTACTGGGTTCTGGGTCAAGGAC
AAGTACAAGCTGCAGCAGACCTTCAGTGTGAATCCCATCTACCTCAGGCATGCCAACTCA
GGCGTGGCCACCGACTTCATGCACTGGCAGATCCCCCTGAGCCGACGGTTTCGCTCTGTT
AAACTCTGGTTCGTGATTCGGTCCTTCGGGGTGAAGAATCTTCAAGCACATGTCAGACAT
GGTACTGAAATGGCTAAATATTTTGAATCTCTGGTCAGAAACGACCCTTCCTTTGAAATT
CCTGCCAAGAGGCACCTTGGCCTGGTGGTTTTTCGTCTAAAGGGTCCTAATTGTCTCACA
GAAAATGTGTTAAAGGAAATAGCTAAAGCTGGCCGTCTCTTCCTCATCCCGGCCACTATC
CAGGACAAGTTAATCATCCGTTTCACTGTGACATCCCAGTTTACCACTAGGGATGACATC
CTGAGAGACTGGAATCTCATTCGAGATGCTGCCACTCTCATCCTGAGTCAGCACTGTACT
TCCCAACCCAGCCCTCGGGTTGGGAACCTCATCTCCCAAATCAGGGGTGCCAGAGCCTGG
GCCTGTGGAACGTCCCTTCAGTCTGTCAGTGGGGCAGGAGATGATCCAGTCCAGGCCAGG
AAGATCATCAAGCAGCCTCAGCGTGTGGGAGCCGGTCCCATGAAAAGGGAAAATGGCCTC
CATCTTGAAACCCTGCTGGACCCAGTTGATGACTGCTTTTCAGAAGAGGCCCCAGATGCC
ACCAAGCACAAGCTGTCCTCCTTCCTGTTCAGTTACTTGTCTGTGCAGACTAAGAAGAAG
ACGGTGCGCTCCCTCAGTTGCAACAGTGTGCCAGTGAGTGCTCAGAAGCCACTGCCCACA
GAGGCCTCTGTGAAGAATGGGGGCTCCTCCAGGGTCAGAATCTTTTCCAGGTTTCCAGAA
GACATGATGATGCTGAAGAAAAGTGCCTTCAAAAAACTCATCAAATTCTACAGCGTCCCC
AGCTTTCCTGAATGCAGCTCTCAATGTGGACTCCAGCTGCCCTGTTGCCCTCTGCAGGCC
ATGGTTTAG

1. Yamauchi K, Sato R, Tanno Y, Ohkawara Y, Maeyama K, Watanabe T, Satoh K, Yoshizawa M, Shibahara S, Takishima T: Nucleotide sequence of the cDNA encoding L-histidine decarboxylase derived from human basophilic leukemia cell line, KU-812-F. Nucleic Acids Res. 1990 Oct 11;18(19):5891. [PubMed ]
2. Zahnow CA, Yi HF, McBride OW, Joseph DR: Cloning of the cDNA encoding human histidine decarboxylase from an erythroleukemia cell line and mapping of the gene locus to chromosome 15. DNA Seq. 1991;1(6):395-400. [PubMed ]
3. Mamune-Sato R, Yamauchi K, Tanno Y, Ohkawara Y, Ohtsu H, Katayose D, Maeyama K, Watanabe T, Shibahara S, Takishima T: Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells. Eur J Biochem. 1992 Oct 15;209(2):533-9. [PubMed ]
4. Yatsunami K, Ohtsu H, Tsuchikawa M, Higuchi T, Ishibashi K, Shida A, Shima Y, Nakagawa S, Yamauchi K, Yamamoto M, et al.: Structure of the L-histidine decarboxylase gene. J Biol Chem. 1994 Jan 14;269(2):1554-9. [PubMed ]

1. Nagai K, Suda T, Kawasaki K, Mathuura S: Action of carnosine and beta-alanine on wound healing. Surgery. 1986 Nov;100(5):815-21. [PubMed ]

MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGV
YATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDK
VRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAE
DIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEE
EIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSE
AANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQD
TIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSS
LNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE

• Filament (PF00038 )
• Filament_head (PF04732 )

• None

• None

ATGTCCACCAGGTCCGTGTCCTCGTCCTCCTACCGCAGGATGTTCGGCGGCCCGGGCACC
GCGAGCCGGCCGAGCTCCAGCCGGAGCTACGTGACTACGTCCACCCGCACCTACAGCCTG
GGCGACGCGCTGCGCCCCAGCACCAGCCGCAGCCTCTACGCCTCGTCCCCGGGCGGCGTG
TATGCCACGCGCTCCTCTGCCGTGCGCCTGCGGAGCAGCGTGCCCGGGGTGCGGCTCCTG
CAGGACTCGGTGGACTTCTCGCTGGCCGACGCCATCAACACCGAGTTCAAGAACACCCGC
ACCAACGAGAAGGTGGAGCTGCAGGAGCTGAATGACCGCTTCGCCAACTACATCGACAAG
GTGCGCTTCCTGGAGCAGCAGAATAAGATCCTGCTGGCCGAGCTCGAGCAGCTCAAGGGC
CAAGGCAAGTCGCGCCTAGGGGACCTCTACGAGGAGGAGATGCGGGAGCTGCGCCGGCAG
GTGGACCAGCTAACCAACGACAAAGCCCGCGTCGAGGTGGAGCGCGACAACCTGGCCGAG
GACATCATGCGCCTCCGGGAAAAATTGCAGGAGGAGATGCTTCAGAGAGAGGAAGCCGAA
AACACCCTGCAATCTTTCAGACAGGATGTTGACAATGCGTCTCTGGCACGTCTTGACCTT
GAACGCAAAGTGGAATCTTTGCAAGAAGAGATTGCCTTTTTGAAGAAACTCCACGAAGAG
GAAATCCAGGAGCTGCAGGCTCAGATTCAGGAACAGCATGTCCAAATCGATGTGGATGTT
TCCAAGCCTGACCTCACGGCTGCCCTGCGTGACGTACGTCAGCAATATGAAAGTGTGGCT
GCCAAGAACCTGCAGGAGGCAGAAGAATGGTACAAATCCAAGTTTGCTGACCTCTCTGAG
GCTGCCAACCGGAACAATGACGCCCTGCGCCAGGCAAAGCAGGAGTCCACTGAGTACCGG
AGACAGGTGCAGTCCCTCACCTGTGAAGTGGATGCCCTTAAAGGAACCAATGAGTCCCTG
GAACGCCAGATGCGTGAAATGGAAGAGAACTTTGCCGTTGAAGCTGCTAACTACCAAGAC
ACTATTGGCCGCCTGCAGGATGAGATTCAGAATATGAAGGAGGAAATGGCTCGTCACCTT
CGTGAATACCAAGACCTGCTCAATGTTAAGATGGCCCTTGACATTGAGATTGCCACCTAC
AGGAAGCTGCTGGAAGGCGAGGAGAGCAGGATTTCTCTGCCTCTTCCAAACTTTTCCTCC
CTGAACCTGAGGGAAACTAATCTGGATTCACTCCCTCTGGTTGATACCCACTCAAAAAGG
ACATTCCTGATTAAGACGGTTGAAACTAGAGATGGACAGGTTATCAACGAAACTTCTCAG
CATCACGATGACCTTGAATAA

1. Ferrari S, Battini R, Kaczmarek L, Rittling S, Calabretta B, de Riel JK, Philiponis V, Wei JF, Baserga R: Coding sequence and growth regulation of the human vimentin gene. Mol Cell Biol. 1986 Nov;6(11):3614-20. [PubMed ]
2. Honore B, Madsen P, Basse B, Andersen A, Walbum E, Celis JE, Leffers H: Nucleotide sequence of cDNA covering the complete coding part of the human vimentin gene. Nucleic Acids Res. 1990 Nov 25;18(22):6692. [PubMed ]
3. Sommers CL, Walker-Jones D, Heckford SE, Worland P, Valverius E, Clark R, McCormick F, Stampfer M, Abularach S, Gelmann EP: Vimentin rather than keratin expression in some hormone-independent breast cancer cell lines and in oncogene-transformed mammary epithelial cells. Cancer Res. 1989 Aug 1;49(15):4258-63. [PubMed ]
4. Perreau J, Lilienbaum A, Vasseur M, Paulin D: Nucleotide sequence of the human vimentin gene and regulation of its transcription in tissues and cultured cells. Gene. 1988;62(1):7-16. [PubMed ]
5. Gupta AK, Aubin JE, Waye MM: Isolation of a human vimentin cDNA with a long 3'-noncoding region from a human osteosarcoma cell line (MG-63). Gene. 1990 Feb 14;86(2):303-4. [PubMed ]
6. Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed ]
7. Strelkov SV, Herrmann H, Geisler N, Lustig A, Ivaninskii S, Zimbelmann R, Burkhard P, Aebi U: Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. J Mol Biol. 2001 Mar 2;306(4):773-81. [PubMed ]
8. Strelkov SV, Herrmann H, Geisler N, Wedig T, Zimbelmann R, Aebi U, Burkhard P: Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 2002 Mar 15;21(6):1255-66. [PubMed ]

1. Hipkiss AR: Could carnosine or related structures suppress Alzheimer's disease? J Alzheimers Dis. 2007 May;11(2):229-40. [PubMed ]

1. HSP70.1
2. HSP70-1/HSP70-2

MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA
LNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEIS
SMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAA
IAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH
FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRA
RFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLN
KSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTI
PTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDI
DANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKN
ALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELE
QVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD

• HSP70 (PF00012 )

• None

• None

ATGGCCAAAGCCGCGGCGATCGGCATCGACCTGGGCACCACCTACTCCTGCGTGGGGGTG
TTCCAACACGGCAAGGTGGAGATCATCGCCAACGACCAGGGCAACCGCACCACCCCCAGC
TACGTGGCCTTCACGGACACCGAGCGGCTCATCGGGGATGCGGCCAAGAACCAGGTGGCG
CTGAACCCGCAGAACACCGTGTTTGACGCGAAGCGCCTGATTGGCCGCAAGTTCGGCGAC
CCGGTGGTGCAGTCGGACATGAAGCACTGGCCTTTCCAGGTGATCAACGACGGAGACAAG
CCCAAGGTGCAGGTGAGCTACAAGGGGGAGACCAAGGCATTCTACCCCGAGGAGATCTCG
TCCATGGTGCTGACCAAGATGAAGGAGATCGCCGAGGCGTACCTGGGCTACCCGGTGACC
AACGCGGTGATCACCGTGCCGGCCTACTTCAACGACTCGCAGCGCCAGGCCACCAAGGAT
GCGGGTGTGATCGCGGGGCTCAACGTGCTGCGGATCATCAACGAGCCCACGGCCGCCGCC
ATCGCCTACGGCCTGGACAGAACGGGCAAGGGGGAGCGCAACGTGCTCATCTTTGACCTG
GGCGGGGGCACCTTCGACGTGTCCATCCTGACGATCGACGACGGCATCTTCGAGGTGAAG
GCCACGGCCGGGGACACCCACCTGGGTGGGGAGGACTTTGACAACAGGCTGGTGAACCAC
TTCGTGGAGGAGTTCAAGAGAAAACACAAGAAGGACATCAGCCAGAACAAGCGAGCCGTG
AGGCGGCTGCGCACCGCCTGCGAGAGGGCCAAGAGGACCCTGTCGTCCAGCACCCAGGCC
AGCCTGGAGATCGACTCCCTGTTTGAGGGCATCGACTTCTACACGTCCATCACCAGGGCG
AGGTTCGAGGAGCTGTGCTCCGACCTGTTCCGAAGCACCCTGGAGCCCGTGGAGAAGGCT
CTGCGCGACGCCAAGCTGGACAAGGCCCAGATTCACGACCTGGTCCTGGTCGGGGGCTCC
ACCCGCATCCCCAAGGTGCAGAAGCTGCTGCAGGACTTCTTCAACGGGCGCGACCTGAAC
AAGAGCATCAACCCCGACGAGGCTGTGGCCTACGGGGCGGCGGTGCAGGCGGCCATCCTG
ATGGGGGACAAGTCCGAGAACGTGCAGGACCTGCTGCTGCTGGACGTGGCTCCCCTGTCG
CTGGGGCTGGAGACGGCCGGAGGCGTGATGACTGCCCTGATCAAGCGCAACTCCACCATC
CCCACCAAGCAGACGCAGATCTTCACCACCTACTCCGACAACCAACCCGGGGTGCTGATC
CAGGTGTACGAGGGCGAGAGGGCCATGACGAAAGACAACAATCTGTTGGGGCGCTTCGAG
CTGAGCGGCATCCCTCCGGCCCCCAGGGGCGTGCCCCAGATCGAGGTGACCTTCGACATC
GATGCCAACGGCATCCTGAACGTCACGGCCACGGACAAGAGCACCGGCAAGGCCAACAAG
ATCACCATCACCAACGACAAGGGCCGCCTGAGCAAGGAGGAGATCGAGCGCATGGTGCAG
GAGGCGGAGAAGTACAAAGCGGAGGACGAGGTGCAGCGCGAGAGGGTGTCAGCCAAGAAC
GCCCTGGAGTCCTACGCCTTCAACATGAAGAGCGCCGTGGAGGATGAGGGGCTCAAGGGC
AAGATCAGCGAGGCCGACAAGAAGAAGGTGCTGGACAAGTGTCAAGAGGTCATCTCGTGG
CTGGACGCCAACACCTTGGCCGAGAAGGACGAGTTTGAGCACAAGAGGAAGGAGCTGGAG
CAGGTGTGTAACCCCATCATCAGCGGACTGTACCAGGGTGCCGGTGGTCCCGGGCCTGGG
GGCTTCGGGGCTCAGGGTCCCAAGGGAGGGTCTGGGTCAGGCCCCACCATTGAGGAGGTA
GATTAG

1. Milner CM, Campbell RD: Structure and expression of the three MHC-linked HSP70 genes. Immunogenetics. 1990;32(4):242-51. [PubMed ]
2. Hunt C, Morimoto RI: Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6455-9. [PubMed ]
3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
4. Sargent CA, Dunham I, Trowsdale J, Campbell RD: Human major histocompatibility complex contains genes for the major heat shock protein HSP70. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1968-72. [PubMed ]
5. Drabent B, Genthe A, Benecke BJ: In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells. Nucleic Acids Res. 1986 Nov 25;14(22):8933-48. [PubMed ]
6. Osipiuk J, Walsh MA, Freeman BC, Morimoto RI, Joachimiak A: Structure of a new crystal form of human Hsp70 ATPase domain. Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1105-7. [PubMed ]

1. Wada I, Otaka M, Jin M, Odashima M, Komatsu K, Konishi N, Matsuhashi T, Horikawa Y, Ohba R, Itoh H, Watanabe S: Expression of HSP72 in the gastric mucosa is regulated by gastric acid in rats-correlation of HSP72 expression with mucosal protection. Biochem Biophys Res Commun. 2006 Oct 20;349(2):611-8. Epub 2006 Aug 23. [PubMed ]

1. Peptide transporter 2
2. Kidney H(+/peptide cotransporter
3. Solute carrier family 15 member 2

MNPFQKNESKETLFSPVSIEEVPPRPPSPPKKPSPTICGSNYPLSIAFIVVNEFCERFSY
YGMKAVLILYFLYFLHWNEDTSTSIYHAFSSLCYFTPILGAAIADSWLGKFKTIIYLSLV
YVLGHVIKSLGALPILGGQVVHTVLSLIGLSLIALGTGGIKPCVAAFGGDQFEEKHAEER
TRYFSVFYLSINAGSLISTFITPMLRGDVQCFGEDCYALAFGVPGLLMVIALVVFAMGSK
IYNKPPPEGNIVAQVFKCIWFAISNRFKNRSGDIPKRHDWLDWAAEKYPKQLIMDVKALT
RVLFLYIPLPMFWALLDQQGSRWTLQAIRMNRNLGFFVLQPDQMQVLNPLLVLIFIPLFD
FVIYRLVSKCGINFSSLRKMAVGMILACLAFAVAARVEIKINEMAPAQPGPQEVFLQVLN
LADDEVKVTVVGNENNSLLIESIKSFQKTPHYSKLHLKTKSQDFHFHLKYHNLSLYTEHS
VQEKNWYSLVIREDGNSISSMMVKDTESRTTNGMTTVRFVNTLHKDVNISLSTDTSLNVG
EDYGVSAYRTVQRGEYPAVHCRTEDKNFSLNLGLLDFGAAYLFVITNNTNQGLQAWKIED
IPANKMSIRWQLPQYALVTAGEVMFSVTGLEFSYSQAPSSMKSVLQAAWLLTIAVGNIIV
LVVAQFSGLVQWAEFILFSCLLLVICLIFSIMGYYYVPVKTEDMRGPADKHIPHIQGNMI
KLETKKTKL

• PTR2 (PF00854 )

• None

• 58-78 88-108 115-135 140-160 184-204 218-238 296-316 344-364 381-401 568-588 612-632 644-664 675-695

ATGAATCCTTTCCAGAAAAATGAGTCCAAGGAAACTCTTTTTTCACCTGTCTCCATTGAA
GAGGTACCACCTCGACCACCTAGCCCTCCAAAGAAGCCATCTCCGACAATCTGTGGCTCC
AACTATCCACTGAGCATTGCCTTCATTGTGGTGAATGAATTCTGCGAGCGCTTTTCCTAT
TATGGAATGAAAGCTGTGCTGATCCTGTATTTCCTGTATTTCCTGCACTGGAATGAAGAT
ACCTCCACATCTATATACCATGCCTTCAGCAGCCTCTGTTATTTTACTCCCATCCTGGGA
GCAGCCATTGCTGACTCGTGGTTGGGAAAATTCAAGACAATCATCTATCTCTCCTTGGTG
TATGTGCTTGGCCATGTGATCAAGTCCTTGGGTGCCTTACCAATACTGGGAGGACAAGTG
GTACACACAGTCCTATCATTGATCGGCCTGAGTCTAATAGCTTTGGGGACAGGAGGCATC
AAACCCTGTGTGGCAGCTTTTGGTGGAGACCAGTTTGAAGAAAAACATGCAGAGGAACGG
ACTAGATACTTCTCAGTCTTCTACCTGTCCATCAATGCAGGGAGCTTGATTTCTACATTT
ATCACACCCATGCTGAGAGGAGATGTGCAATGTTTTGGAGAAGACTGCTATGCATTGGCT
TTTGGAGTTCCAGGACTGCTCATGGTAATTGCACTTGTTGTGTTTGCAATGGGAAGCAAA
ATATACAATAAACCACCCCCTGAAGGAAACATAGTGGCTCAAGTTTTCAAATGTATCTGG
TTTGCTATTTCCAATCGTTTCAAGAACCGTTCTGGAGACATTCCAAAGCGACACGACTGG
CTAGACTGGGCGGCTGAGAAATATCCAAAGCAGCTCATTATGGATGTAAAGGCACTGACC
AGGGTACTATTCCTTTATATCCCATTGCCCATGTTCTGGGCTCTTTTGGATCAGCAGGGT
TCACGATGGACTTTGCAAGCCATCAGGATGAATAGGAATTTGGGGTTTTTTGTGCTTCAG
CCGGACCAGATGCAGGTTCTAAATCCCCTTCTGGTTCTTATCTTCATCCCGTTGTTTGAC
TTTGTCATTTATCGTCTGGTCTCCAAGTGTGGAATTAACTTCTCATCACTTAGGAAAATG
GCTGTTGGTATGATCCTAGCATGCCTGGCATTTGCAGTTGCGGCACGTGTAGAGATAAAA
ATAAATGAAATGGCCCCAGCCCAGCCAGGTCCCCAGGAGGTTTTCCTACAAGTCTTGAAT
CTGGCAGATGATGAGGTGAAGGTGACAGTGGTGGGAAATGAAAACAATTCTCTGTTGATA
GAGTCCATCAAATCCTTTCAGAAAACACCACACTATTCCAAACTGCACCTGAAAACAAAA
AGCCAGGATTTTCACTTCCACCTGAAATATCACAATTTGTCTCTCTACACTGAGCATTCT
GTGCAGGAGAAGAACTGGTACAGTCTTGTCATTCGTGAAGATGGGAACAGTATCTCCAGC
ATGATGGTAAAGGATACAGAAAGCAGAACAACCAATGGGATGACAACCGTGAGGTTTGTT
AACACTTTGCATAAAGATGTCAACATCTCCCTGAGTACAGATACCTCTCTCAATGTTGGT
GAAGACTATGGTGTGTCTGCTTATAGAACTGTGCAAAGAGGAGAATACCCTGCAGTGCAC
TGTAGAACAGAAGATAAGAACTTTTCTCTGAATTTGGGTCTTCTAGACTTTGGTGCAGCA
TATCTGTTTGTTATTACTAATAACACCAATCAGGGTCTTCAGGCCTGGAAGATTGAAGAC
ATTCCAGCCAACAAAATGTCCATTCGGTGGCAGCTACCACAATATGCCCTGGTTACAGCT
GGGGAGGTCATGTTCTCTGTCACAGGTCTTGAGTTTTCTTATTCTCAGGCTCCCTCTAGC
ATGAAATCTGTGCTCCAGGCAGCTTGGCTATTGACAATTGCAGTTGGGAATATCATCGTG
CTTGTTGTGGCACAGTTCAGTGGCCTGGTACAGTGGGCCGAATTCATTTTGTTTTCCTGC
CTCCTGCTGGTGATCTGCCTGATCTTCTCCATCATGGGCTACTACTATGTTCCTGTAAAG
ACAGAGGATATGCGGGGTCCAGCAGATAAGCACATTCCTCACATCCAGGGGAACATGATC
AAACTAGAGACCAAGAAGACAAAACTCTGA

1. Liu W, Liang R, Ramamoorthy S, Fei YJ, Ganapathy ME, Hediger MA, Ganapathy V, Leibach FH: Molecular cloning of PEPT 2, a new member of the H+/peptide cotransporter family, from human kidney. Biochim Biophys Acta. 1995 May 4;1235(2):461-6. [PubMed ]

1. Teuscher NS, Keep RF, Smith DE: PEPT2-mediated uptake of neuropeptides in rat choroid plexus. Pharm Res. 2001 Jun;18(6):807-13. [PubMed ]