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Identification
HMDB Protein ID HMDBP01382
Secondary Accession Numbers
  • 6678
Name Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
Synonyms
  1. Calcium pump 1
  2. Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
  3. Endoplasmic reticulum class 1/2 Ca(2+) ATPase
  4. SERCA1
  5. SR Ca(2+)-ATPase 1
Gene Name ATP2A1
Protein Type Unknown
Biological Properties
General Function Involved in ATP binding
Specific Function This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.
Pathways
  • Alzheimer disease
  • Calcium signaling pathway
  • Pancreatic secretion
Reactions Not Available
GO Classification
Biological Process
ATP biosynthetic process
apoptotic mitochondrial changes
blood coagulation
calcium ion import
elevation of endoplasmic reticulum calcium ion concentration
elevation of mitochondrial calcium ion concentration
intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
maintenance of mitochondrion location
positive regulation of fast-twitch skeletal muscle fiber contraction
reduction of endoplasmic reticulum calcium ion concentration
relaxation of skeletal muscle
negative regulation of striated muscle contraction
Cellular Component
endoplasmic reticulum membrane
I band
perinuclear region of cytoplasm
endoplasmic reticulum-Golgi intermediate compartment
calcium channel complex
H zone
platelet dense tubular network membrane
sarcoplasmic reticulum
sarcoplasmic reticulum membrane
Component
membrane
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
di-, tri-valent inorganic cation transmembrane transporter activity
calcium ion transmembrane transporter activity
calcium-transporting atpase activity
binding
catalytic activity
hydrolase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
transmembrane transporter activity
substrate-specific transmembrane transporter activity
ion transmembrane transporter activity
cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
transporter activity
atpase activity, coupled to transmembrane movement of ions
atpase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
hydrolase activity, acting on acid anhydrides
Molecular Function
ATP binding
calcium-transporting ATPase activity
calcium ion binding
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
di-, tri-valent inorganic cation transport
divalent metal ion transport
calcium ion transport
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
establishment of localization
transport
ion transport
atp biosynthetic process
cation transport
Cellular Location
  1. Endoplasmic reticulum membrane
  2. Multi-pass membrane protein
  3. Multi-pass membrane protein
  4. Sarcoplasmic reticulum membrane
Gene Properties
Chromosome Location 16
Locus 16p12.1
SNPs ATP2A1
Gene Sequence
>3006 bp
ATGGAGGCCGCTCATGCTAAAACCACGGAGGAATGTTTGGCCTATTTTGGGGTGAGTGAG
ACCACGGGCCTCACCCCGGACCAAGTTAAGCGGAATCTGGAGAAATACGGCCTCAATGAG
CTCCCTGCTGAGGAAGGGAAGACCCTGTGGGAGCTGGTGATAGAGCAGTTTGAAGACCTC
CTGGTGCGGATTCTCCTCCTGGCCGCATGCATTTCCTTCGTGCTGGCCTGGTTTGAGGAA
GGTGAAGAGACCATCACTGCCTTTGTTGAACCCTTTGTCATCCTCTTGATCCTCATTGCC
AATGCCATCGTGGGGGTTTGGCAGGAGCGGAACGCAGAGAACGCCATCGAGGCCCTGAAG
GAGTATGAGCCAGAGATGGGGAAGGTCTACCGGGCTGACCGCAAGTCAGTGCAAAGGATC
AAGGCTCGGGACATCGTCCCTGGGGACATCGTGGAGGTGGCTGTGGGGGACAAAGTCCCT
GCAGACATCCGAATCCTCGCCATCAAATCCACCACGCTGCGGGTTGACCAGTCCATCCTG
ACAGGCGAGTCTGTATCTGTCATCAAACACACGGAGCCCGTTCCTGACCCCCGAGCTGTC
AACCAGGACAAGAAGAACATGCTTTTCTCGGGCACCAACATTGCAGCCGGCAAGGCCTTG
GGCATCGTGGCCACCACTGGTGTGGGCACCGAGATTGGGAAGATCCGAGACCAAATGGCT
GCCACAGAACAGGACAAGACCCCCTTGCAGCAGAAGCTGGATGAGTTTGGGGAGCAGCTC
TCCAAGGTCATCTCCCTCATCTGTGTGGCTGTCTGGCTTATCAACATTGGCCACTTCAAC
GACCCCGTCCATGGGGGCTCCTGGTTCCGCGGGGCCATCTACTACTTTAAGATTGCCGTG
GCCTTGGCTGTGGCTGCCATCCCCGAAGGTCTTCCTGCAGTCATCACCACCTGCCTGGCC
CTGGGTACCCGTCGGATGGCAAAGAAGAATGCCATTGTAAGAAGCTTGCCCTCCGTAGAG
ACCCTGGGCTGCACCTCTGTCATCTGTTCCGACAAGACAGGCACCCTCACCACCAACCAG
ATGTCTGTCTGCAAGATGTTTATCATTGACAAGGTGGATGGGGACATCTGCCTCCTGAAT
GAGTTCTCCATCACCGGCTCCACTTACGCTCCAGAGGGAGAGGTCTTGAAGAATGATAAG
CCAGTCCGGCCAGGGCAGTATGACGGGCTGGTGGAGCTGGCCACCATCTGTGCCCTCTGC
AATGACTCCTCCTTGGACTTCAACGAGGCCAAAGGTGTCTATGAGAAGGTCGGCGAGGCC
ACCGAGACAGCACTCACCACCCTGGTGGAGAAGATGAATGTGTTCAACACGGATGTGAGA
AGCCTCTCGAAGGTGGAGAGAGCCAACGCCTGCAACTCGGTGATCCGCCAGCTAATGAAG
AAGGAATTCACCCTGGAGTTCTCCCGAGACAGAAAGTCCATGTCTGTCTATTGCTCCCCA
GCCAAATCTTCCCGGGCTGCTGTGGGCAACAAGATGTTTGTCAAGGGTGCCCCTGAGGGC
GTCATCGACCGCTGTAACTATGTGCGAGTTGGCACCACCCGGGTGCCACTGACGGGGCCG
GTGAAGGAAAAGATCATGGCGGTGATCAAGGAGTGGGGCACTGGCCGGGACACCCTGCGC
TGCTTGGCCCTGGCCACCCGGGACACCCCCCCGAAGCGAGAGGAAATGGTCCTGGATGAC
TCTGCCAGGTTCCTGGAGTATGAGACGGACCTGACATTCGTGGGTGTAGTGGGCATGCTG
GACCCTCCGCGCAAGGAGGTCACGGGCTCCATCCAGCTGTGCCGTGACGCCGGGATCCGG
GTGATCATGATCACTGGGGACAACAAGGGCACAGCCATTGCCATCTGCCGGCGAATTGGC
ATCTTTGGGGAGAACGAGGAGGTGGCCGATCGCGCCTACACGGGCCGAGAGTTCGACGAC
CTGCCCCTGGCTGAACAGCGGGAAGCCTGCCGACGTGCCTGCTGCTTCGCCCGTGTGGAG
CCCTCGCACAAGTCCAAGATTGTGGAGTACCTGCAGTCCTACGATGAGATCACAGCCATG
ACAGGTGATGGCGTCAATGACGCCCCTGCCCTGAAGAAGGCTGAGATTGGCATTGCCATG
GGATCTGGCACTGCCGTGGCCAAGACTGCCTCTGAGATGGTGCTGGCTGACGACAACTTC
TCCACCATCGTAGCTGCTGTGGAGGAGGGCCGCGCCATCTACAACAACATGAAGCAGTTC
ATCCGCTACCTCATTTCCTCCAACGTGGGCGAGGTGGTCTGTATCTTCCTGACCGCTGCC
CTGGGGCTGCCTGAGGCCCTGATCCCGGTGCAGCTGCTATGGGTGAACTTGGTGACCGAC
GGGCTCCCAGCCACAGCCCTGGGCTTCAACCCACCAGACCTGGACATCATGGACCGCCCC
CCCCGGAGCCCCAAGGAGCCCCTCATCAGTGGCTGGCTCTTCTTCCGCTACATGGCAATC
GGGGGCTATGTGGGTGCAGCCACCGTGGGAGCAGCTGCCTGGTGGTTCCTGTACGCTGAG
GATGGGCCTCATGTCAACTACAGCCAGCTGACTCACTTCATGCAGTGCACCGAGGACAAC
ACCCACTTTGAGGGCATAGACTGTGAGGTCTTCGAGGCCCCCGAGCCCATGACCATGGCC
CTGTCCGTGCTGGTGACCATCGAGATGTGCAATGCACTGAACAGCCTGTCCGAGAACCAG
TCCCTGCTGCGGATGCCACCCTGGGTGAACATCTGGCTGCTGGGCTCCATCTGCCTCTCC
ATGTCCCTGCACTTCCTCATCCTCTATGTTGACCCCCTGCCGATGATCTTCAAGCTCCGG
GCCCTGGACCTCACCCAGTGGCTCATGGTCCTCAAGATCTCACTGCCAGTCATTGGGCTC
GACGAAATCCTCAAGTTCGTTGCTCGGAACTACCTAGAGGATCCAGAAGATGAAAGAAGG
AAGTGA
Protein Properties
Number of Residues 1001
Molecular Weight 109282.355
Theoretical pI 5.175
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
MEAAHAKTTEECLAYFGVSETTGLTPDQVKRNLEKYGLNELPAEEGKTLWELVIEQFEDL
LVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAENAIEALK
EYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILAIKSTTLRVDQSIL
TGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVGTEIGKIRDQMA
ATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWFRGAIYYFKIAV
ALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQ
MSVCKMFIIDKVDGDICLLNEFSITGSTYAPEGEVLKNDKPVRPGQYDGLVELATICALC
NDSSLDFNEAKGVYEKVGEATETALTTLVEKMNVFNTDVRSLSKVERANACNSVIRQLMK
KEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPLTGP
VKEKIMAVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSARFLEYETDLTFVGVVGML
DPPRKEVTGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVADRAYTGREFDD
LPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAM
GSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAA
LGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAI
GGYVGAATVGAAAWWFLYAEDGPHVNYSQLTHFMQCTEDNTHFEGIDCEVFEAPEPMTMA
LSVLVTIEMCNALNSLSENQSLLRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKLR
ALDLTQWLMVLKISLPVIGLDEILKFVARNYLEDPEDERRK
GenBank ID Protein 27886529
UniProtKB/Swiss-Prot ID O14983
UniProtKB/Swiss-Prot Entry Name AT2A1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_173201.3
GeneCard ID ATP2A1
GenAtlas ID ATP2A1
HGNC ID HGNC:811
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Zhang Y, Fujii J, Phillips MS, Chen HS, Karpati G, Yee WC, Schrank B, Cornblath DR, Boylan KB, MacLennan DH: Characterization of cDNA and genomic DNA encoding SERCA1, the Ca(2+)-ATPase of human fast-twitch skeletal muscle sarcoplasmic reticulum, and its elimination as a candidate gene for Brody disease. Genomics. 1995 Dec 10;30(3):415-24. [PubMed:8825625 ]
  3. Daiho T, Yamasaki K, Saino T, Kamidochi M, Satoh K, Iizuka H, Suzuki H: Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2+-ATPase result in a complete loss of Ca2+ transport activity without a loss of Ca2+-dependent ATPase activity. Role of the CYS876-CYS888 disulfide bond. J Biol Chem. 2001 Aug 31;276(35):32771-8. Epub 2001 Jul 3. [PubMed:11438520 ]
  4. Odermatt A, Barton K, Khanna VK, Mathieu J, Escolar D, Kuntzer T, Karpati G, MacLennan DH: The mutation of Pro789 to Leu reduces the activity of the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA1) and is associated with Brody disease. Hum Genet. 2000 May;106(5):482-91. [PubMed:10914677 ]