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Showing Protein Coagulation factor XII (HMDBP02054)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP02054
Secondary Accession Numbers
  • 7533
Name Coagulation factor XII
Synonyms
  1. Beta-factor XIIa part 1
  2. Beta-factor XIIa part 2
  3. Coagulation factor XIIa heavy chain
  4. Coagulation factor XIIa light chain
  5. HAF
  6. Hageman factor
Gene Name F12
Protein Type Enzyme
Biological Properties
General Function Involved in serine-type endopeptidase activity
Specific Function Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta- factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa
Pathways
  • Acenocoumarol Action Pathway
  • Alteplase Action Pathway
  • Aminocaproic Acid Action Pathway
  • Anistreplase Action Pathway
  • Aprotinin Action Pathway
  • Ardeparin Action Pathway
  • Argatroban Action Pathway
  • Bivalirudin Action Pathway
  • Coagulation
  • Dicoumarol Action Pathway
  • Dicumarol Action Pathway
  • Enoxaparin Action Pathway
  • Fondaparinux Action Pathway
  • Heparin Action Pathway
  • Lepirudin Action Pathway
  • Phenindione Action Pathway
  • Phenprocoumon Action Pathway
  • Reteplase Action Pathway
  • Streptokinase Action Pathway
  • Tenecteplase Action Pathway
  • Tranexamic Acid Action Pathway
  • Urokinase Action Pathway
  • Warfarin Action Pathway
  • Ximelagatran Action Pathway
Reactions Not Available
GO Classification
Component
extracellular region part
extracellular space
extracellular region
Function
endopeptidase activity
serine-type endopeptidase activity
catalytic activity
hydrolase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Chromosome:5
Locus 5q33-qter
SNPs F12
Gene Sequence 
>1848 bp
ATGAGGGCTCTGCTGCTCCTGGGGTTCCTGCTGGTGAGCTTGGAGTCAACACTTTCGATT
CCACCTTGGGAAGCCCCCAAGGAGCATAAGTACAAAGCTGAAGAGCACACAGTCGTTCTC
ACTGTCACCGGGGAGCCCTGCCACTTCCCCTTCCAGTACCACCGGCAGCTGTACCACAAA
TGTACCCACAAGGGCCGGCCAGGCCCTCAGCCCTGGTGTGCTACCACCCCCAACTTTGAT
CAGGACCAGCGATGGGGATACTGTTTGGAGCCCAAGAAAGTGAAAGACCACTGCAGCAAA
CACAGCCCCTGCCAGAAAGGAGGGACCTGTGTGAACATGCCAAGCGGCCCCCACTGTCTC
TGTCCACAACACCTCACTGGAAACCACTGCCAGAAAGAGAAGTGCTTTGAGCCTCAGCTT
CTCCGGTTTTTCCACAAGAATGAGATATGGTATAGAACTGAGCAAGCAGCTGTGGCCAGA
TGCCAGTGCAAGGGTCCTGATGCCCACTGCCAGCGGCTGGCCAGCCAGGCCTGCCGCACC
AACCCGTGCCTCCATGGGGGTCGCTGCCTAGAGGTGGAGGGCCACCGCCTGTGCCACTGC
CCGGTGGGCTACACCGGACCCTTCTGCGACGTGGACACCAAGGCAAGCTGCTATGATGGC
CGCGGGCTCAGCTACCGCGGCCTGGCCAGGACCACGCTCTCGGGTGCGCCCTGTCAGCCG
TGGGCCTCGGAGGCCACCTACCGGAACGTGACTGCCGAGCAAGCGCGGAACTGGGGACTG
GGCGGCCACGCCTTCTGCCGGAACCCGGACAACGACATCCGCCCGTGGTGCTTCGTGCTG
AACCGCGACCGGCTGAGCTGGGAGTACTGCGACCTGGCACAGTGCCAGACCCCAACCCAG
GCGGCGCCTCCGACCCCGGTGTCCCCTAGGCTTCATGTCCCACTCATGCCCGCGCAGCCG
GCACCGCCGAAGCCTCAGCCCACGACCCGGACCCCGCCTCAGTCCCAGACCCCGGGAGCC
TTGCCGGCGAAGCGGGAGCAGCCGCCTTCCCTGACCAGGAACGGCCCACTGAGCTGCGGG
CAGCGGCTCCGCAAGAGTCTGTCTTCGATGACCCGCGTCGTTGGCGGGCTGGTGGCGCTA
CGCGGGGCGCACCCCTACATCGCCGCGCTGTACTGGGGCCACAGTTTCTGCGCCGGCAGC
CTCATCGCCCCCTGCTGGGTGCTGACGGCCGCTCACTGCCTGCAGGACCGGCCCGCACCC
GAGGATCTGACGGTGGTGCTCGGCCAGGAACGCCGTAACCACAGCTGTGAGCCGTGCCAG
ACGTTGGCCGTGCGCTCCTACCGCTTGCACGAGGCCTTCTCGCCCGTCAGCTACCAGCAC
GACCTGGCTCTGTTGCGCCTTCAGGAGGATGCGGACGGCAGCTGCGCGCTCCTGTCGCCT
TACGTTCAGCCGGTGTGCCTGCCAAGCGGCGCCGCGCGACCCTCCGAGACCACGCTCTGC
CAGGTGGCCGGCTGGGGCCACCAGTTCGAGGGGGCGGAGGAATATGCCAGCTTCCTGCAG
GAGGCGCAGGTACCGTTCCTCTCCCTGGAGCGCTGCTCAGCCCCGGACGTGCACGGATCC
TCCATCCTCCCCGGCATGCTCTGCGCAGGGTTCCTCGAGGGCGGCACCGATGCGTGCCAG
GGTGATTCCGGAGGCCCGCTGGTGTGTGAGGACCAAGCTGCAGAGCGCCGGCTCACCCTG
CAAGGCATCATCAGCTGGGGATCGGGCTGTGGTGACCGCAACAAGCCAGGCGTCTACACC
GATGTGGCCTACTACCTGGCCTGGATCCGGGAGCACACCGTTTCCTGA
Protein Properties
Number of Residues 615
Molecular Weight 67817.6
Theoretical pI 7.76
Pfam Domain Function
Signals
  • 1-19
Transmembrane Regions
  • None
Protein Sequence 
>Coagulation factor XII
MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHK
CTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCL
CPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRT
NPCLHGGRCLEVEGHRLCHCPVGYTGPFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQP
WASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQ
AAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCG
QRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAP
EDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSP
YVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGS
SILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYT
DVAYYLAWIREHTVS
GenBank ID Protein 22532477
UniProtKB/Swiss-Prot ID P00748
UniProtKB/Swiss-Prot Entry Name FA12_HUMAN
PDB IDs Not Available
GenBank Gene ID AF538691
GeneCard ID F12
GenAtlas ID F12
HGNC ID HGNC:3530
References
General References
  1. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed:16335952 ]
  2. Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [PubMed:14760718 ]
  3. Harris RJ, Ling VT, Spellman MW: O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. J Biol Chem. 1992 Mar 15;267(8):5102-7. [PubMed:1544894 ]
  4. Cool DE, MacGillivray RT: Characterization of the human blood coagulation factor XII gene. Intron/exon gene organization and analysis of the 5'-flanking region. J Biol Chem. 1987 Oct 5;262(28):13662-73. [PubMed:2888762 ]
  5. Tripodi M, Citarella F, Guida S, Galeffi P, Fantoni A, Cortese R: cDNA sequence coding for human coagulation factor XII (Hageman). Nucleic Acids Res. 1986 Apr 11;14(7):3146. [PubMed:3754331 ]
  6. Cool DE, Edgell CJ, Louie GV, Zoller MJ, Brayer GD, MacGillivray RT: Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa. J Biol Chem. 1985 Nov 5;260(25):13666-76. [PubMed:3877053 ]
  7. Que BG, Davie EW: Characterization of a cDNA coding for human factor XII (Hageman factor). Biochemistry. 1986 Apr 8;25(7):1525-8. [PubMed:3011063 ]
  8. McMullen BA, Fujikawa K: Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor). J Biol Chem. 1985 May 10;260(9):5328-41. [PubMed:3886654 ]
  9. Fujikawa K, McMullen BA: Amino acid sequence of human beta-factor XIIa. J Biol Chem. 1983 Sep 25;258(18):10924-33. [PubMed:6604055 ]
  10. Schloesser M, Hofferbert S, Bartz U, Lutze G, Lammle B, Engel W: The novel acceptor splice site mutation 11396(G-->A) in the factor XII gene causes a truncated transcript in cross-reacting material negative patients. Hum Mol Genet. 1995 Jul;4(7):1235-7. [PubMed:8528215 ]
  11. Bernardi F, Marchetti G, Patracchini P, del Senno L, Tripodi M, Fantoni A, Bartolai S, Vannini F, Felloni L, Rossi L, et al.: Factor XII gene alteration in Hageman trait detected by TaqI restriction enzyme. Blood. 1987 May;69(5):1421-4. [PubMed:2882793 ]
  12. Miyata T, Kawabata S, Iwanaga S, Takahashi I, Alving B, Saito H: Coagulation factor XII (Hageman factor) Washington D.C.: inactive factor XIIa results from Cys-571----Ser substitution. Proc Natl Acad Sci U S A. 1989 Nov;86(21):8319-22. [PubMed:2510163 ]
  13. Hovinga JK, Schaller J, Stricker H, Wuillemin WA, Furlan M, Lammle B: Coagulation factor XII Locarno: the functional defect is caused by the amino acid substitution Arg 353-->Pro leading to loss of a kallikrein cleavage site. Blood. 1994 Aug 15;84(4):1173-81. [PubMed:8049433 ]
  14. Schloesser M, Zeerleder S, Lutze G, Halbmayer WM, Hofferbert S, Hinney B, Koestering H, Lammle B, Pindur G, Thies K, Kohler M, Engel W: Mutations in the human factor XII gene. Blood. 1997 Nov 15;90(10):3967-77. [PubMed:9354665 ]
  15. Kondo S, Tokunaga F, Kawano S, Oono Y, Kumagai S, Koide T: Factor XII Tenri, a novel cross-reacting material negative factor XII deficiency, occurs through a proteasome-mediated degradation. Blood. 1999 Jun 15;93(12):4300-8. [PubMed:10361128 ]
  16. Kanaji T, Kanaji S, Osaki K, Kuroiwa M, Sakaguchi M, Mihara K, Niho Y, Okamura T: Identification and characterization of two novel mutations (Q421 K and R123P) in congenital factor XII deficiency. Thromb Haemost. 2001 Dec;86(6):1409-15. [PubMed:11776307 ]
  17. Ishii K, Oguchi S, Moriki T, Yatabe Y, Takeshita E, Murata M, Ikeda Y, Watanabe K: Genetic analyses and expression studies identified a novel mutation (W486C) as a molecular basis of congenital coagulation factor XII deficiency. Blood Coagul Fibrinolysis. 2004 Jul;15(5):367-73. [PubMed:15205584 ]
  18. Oguchi S, Ishii K, Moriki T, Takeshita E, Murata M, Ikeda Y, Watanabe K: Factor XII Shizuoka, a novel mutation (Ala392Thr) identified and characterized in a patient with congenital coagulation factor XII deficiency. Thromb Res. 2005;115(3):191-7. [PubMed:15617741 ]
  19. Dewald G, Bork K: Missense mutations in the coagulation factor XII (Hageman factor) gene in hereditary angioedema with normal C1 inhibitor. Biochem Biophys Res Commun. 2006 May 19;343(4):1286-9. [PubMed:16638441 ]
  20. Cichon S, Martin L, Hennies HC, Muller F, Van Driessche K, Karpushova A, Stevens W, Colombo R, Renne T, Drouet C, Bork K, Nothen MM: Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III. Am J Hum Genet. 2006 Dec;79(6):1098-104. Epub 2006 Oct 18. [PubMed:17186468 ]