Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

Details

Name
Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
Synonyms
  • 3.6.3.8
  • Calcium pump 1
  • Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
  • Endoplasmic reticulum class 1/2 Ca(2+) ATPase
  • SERCA1
Gene Name
ATP2A1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0007448|Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
MEAAHAKTTEECLAYFGVSETTGLTPDQVKRNLEKYGLNELPAEEGKTLWELVIEQFEDL
LVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAENAIEALK
EYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILAIKSTTLRVDQSIL
TGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVGTEIGKIRDQMA
ATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWFRGAIYYFKIAV
ALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQ
MSVCKMFIIDKVDGDICLLNEFSITGSTYAPEGEVLKNDKPVRPGQYDGLVELATICALC
NDSSLDFNEAKGVYEKVGEATETALTTLVEKMNVFNTDVRSLSKVERANACNSVIRQLMK
KEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPLTGP
VKEKIMAVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSARFLEYETDLTFVGVVGML
DPPRKEVTGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVADRAYTGREFDD
LPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAM
GSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAA
LGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAI
GGYVGAATVGAAAWWFLYAEDGPHVNYSQLTHFMQCTEDNTHFEGIDCEVFEAPEPMTMA
LSVLVTIEMCNALNSLSENQSLLRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKLR
ALDLTQWLMVLKISLPVIGLDEILKFVARNYLEDPEDERRK
Number of residues
1001
Molecular Weight
110251.36
Theoretical pI
4.8
GO Classification
Functions
ATP binding / calcium ion binding / calcium-transporting ATPase activity / protein homodimerization activity
Processes
apoptotic mitochondrial changes / blood coagulation / calcium ion import / calcium ion transmembrane transport / calcium ion transport / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / ion transmembrane transport / maintenance of mitochondrion location / negative regulation of endoplasmic reticulum calcium ion concentration / negative regulation of striated muscle contraction / positive regulation of endoplasmic reticulum calcium ion concentration / positive regulation of fast-twitch skeletal muscle fiber contraction / positive regulation of mitochondrial calcium ion concentration / regulation of striated muscle contraction / relaxation of skeletal muscle / response to endoplasmic reticulum stress / transmembrane transport
Components
calcium channel complex / endoplasmic reticulum membrane / endoplasmic reticulum-Golgi intermediate compartment / H zone / I band / integral component of membrane / integral component of plasma membrane / membrane / mitochondrion / perinuclear region of cytoplasm / platelet dense tubular network membrane / sarcoplasmic reticulum / sarcoplasmic reticulum membrane
General Function
Protein homodimerization activity
Specific Function
Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. 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.
Pfam Domain Function
Transmembrane Regions
49-69 90-110 254-273 296-313 758-777 788-808 829-851 898-917 931-949 965-985
Cellular Location
Endoplasmic reticulum membrane
Gene sequence
>lcl|BSEQ0012711|Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (ATP2A1)
ATGGGGAAGGTCTACCGGGCTGACCGCAAGTCAGTGCAAAGGATCAAGGCTCGGGACATC
GTCCCTGGGGACATCGTGGAGGTGGCTGTGGGGGACAAAGTCCCTGCAGACATCCGAATC
CTCGCCATCAAATCCACCACGCTGCGGGTTGACCAGTCCATCCTGACAGGCGAGTCTGTA
TCTGTCATCAAACACACGGAGCCCGTTCCTGACCCCCGAGCTGTCAACCAGGACAAGAAG
AACATGCTTTTCTCGGGCACCAACATTGCAGCCGGCAAGGCCTTGGGCATCGTGGCCACC
ACTGGTGTGGGCACCGAGATTGGGAAGATCCGAGACCAAATGGCTGCCACAGAACAGGAC
AAGACCCCCTTGCAGCAGAAGCTGGATGAGTTTGGGGAGCAGCTCTCCAAGGTCATCTCC
CTCATCTGTGTGGCTGTCTGGCTTATCAACATTGGCCACTTCAACGACCCCGTCCATGGG
GGCTCCTGGTTCCGCGGGGCCATCTACTACTTTAAGATTGCCGTGGCCTTGGCTGTGGCT
GCCATCCCCGAAGGTCTTCCTGCAGTCATCACCACCTGCCTGGCCCTGGGTACCCGTCGG
ATGGCAAAGAAGAATGCCATTGTAAGAAGCTTGCCCTCCGTAGAGACCCTGGGCTGCACC
TCTGTCATCTGTTCCGACAAGACAGGCACCCTCACCACCAACCAGATGTCTGTCTGCAAG
ATGTTTATCATTGACAAGGTGGATGGGGACATCTGCCTCCTGAATGAGTTCTCCATCACC
GGCTCCACTTACGCTCCAGAGGGAGAGGTCTTGAAGAATGATAAGCCAGTCCGGCCAGGG
CAGTATGACGGGCTGGTGGAGCTGGCCACCATCTGTGCCCTCTGCAATGACTCCTCCTTG
GACTTCAACGAGGCCAAAGGTGTCTATGAGAAGGTCGGCGAGGCCACCGAGACAGCACTC
ACCACCCTGGTGGAGAAGATGAATGTGTTCAACACGGATGTGAGAAGCCTCTCGAAGGTG
GAGAGAGCCAACGCCTGCAACTCGGTGATCCGCCAGCTAATGAAGAAGGAATTCACCCTG
GAGTTCTCCCGAGACAGAAAGTCCATGTCTGTCTATTGCTCCCCAGCCAAATCTTCCCGG
GCTGCTGTGGGCAACAAGATGTTTGTCAAGGGTGCCCCTGAGGGCGTCATCGACCGCTGT
AACTATGTGCGAGTTGGCACCACCCGGGTGCCACTGACGGGGCCGGTGAAGGAAAAGATC
ATGGCGGTGATCAAGGAGTGGGGCACTGGCCGGGACACCCTGCGCTGCTTGGCCCTGGCC
ACCCGGGACACCCCCCCGAAGCGAGAGGAAATGGTCCTGGATGACTCTGCCAGGTTCCTG
GAGTATGAGACGGACCTGACATTCGTGGGTGTAGTGGGCATGCTGGACCCTCCGCGCAAG
GAGGTCACGGGCTCCATCCAGCTGTGCCGTGACGCCGGGATCCGGGTGATCATGATCACT
GGGGACAACAAGGGCACAGCCATTGCCATCTGCCGGCGAATTGGCATCTTTGGGGAGAAC
GAGGAGGTGGCCGATCGCGCCTACACGGGCCGAGAGTTCGACGACCTGCCCCTGGCTGAA
CAGCGGGAAGCCTGCCGACGTGCCTGCTGCTTCGCCCGTGTGGAGCCCTCGCACAAGTCC
AAGATTGTGGAGTACCTGCAGTCCTACGATGAGATCACAGCCATGACAGGTGATGGCGTC
AATGACGCCCCTGCCCTGAAGAAGGCTGAGATTGGCATTGCCATGGGATCTGGCACTGCC
GTGGCCAAGACTGCCTCTGAGATGGTGCTGGCTGACGACAACTTCTCCACCATCGTAGCT
GCTGTGGAGGAGGGCCGCGCCATCTACAACAACATGAAGCAGTTCATCCGCTACCTCATT
TCCTCCAACGTGGGCGAGGTGGTCTGTATCTTCCTGACCGCTGCCCTGGGGCTGCCTGAG
GCCCTGATCCCGGTGCAGCTGCTATGGGTGAACTTGGTGACCGACGGGCTCCCAGCCACA
GCCCTGGGCTTCAACCCACCAGACCTGGACATCATGGACCGCCCCCCCCGGAGCCCCAAG
GAGCCCCTCATCAGTGGCTGGCTCTTCTTCCGCTACATGGCAATCGGGGGCTATGTGGGT
GCAGCCACCGTGGGAGCAGCTGCCTGGTGGTTCCTGTACGCTGAGGATGGGCCTCATGTC
AACTACAGCCAGCTGACTCACTTCATGCAGTGCACCGAGGACAACACCCACTTTGAGGGC
ATAGACTGTGAGGTCTTCGAGGCCCCCGAGCCCATGACCATGGCCCTGTCCGTGCTGGTG
ACCATCGAGATGTGCAATGCACTGAACAGCCTGTCCGAGAACCAGTCCCTGCTGCGGATG
CCACCCTGGGTGAACATCTGGCTGCTGGGCTCCATCTGCCTCTCCATGTCCCTGCACTTC
CTCATCCTCTATGTTGACCCCCTGCCGATGATCTTCAAGCTCCGGGCCCTGGACCTCACC
CAGTGGCTCATGGTCCTCAAGATCTCACTGCCAGTCATTGGGCTCGACGAAATCCTCAAG
TTCGTTGCTCGGAACTACCTAGAGGGATAA
Chromosome Location
16
Locus
16p12.1
External Identifiers
ResourceLink
UniProtKB IDO14983
UniProtKB Entry NameAT2A1_HUMAN
GenBank Protein ID158256064
GenBank Gene IDAK291314
HGNC IDHGNC:811
General References
  1. 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. [Article]
  2. 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. [Article]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [Article]
  4. 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. [Article]
  5. 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. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00228Enfluraneapproved, investigational, vet_approvedunknowninhibitorstimulatorDetails
DB03909Adenosine-5'-[Beta, Gamma-Methylene]TriphosphateexperimentalunknownDetails
DB04444Tetrafluoroaluminate IonexperimentalunknownDetails
DB046382,5-di-tert-butylhydroquinoneexperimentalunknownDetails
DB07604(6AR,11AS,11BR)-10-ACETYL-9-HYDROXY-7,7-DIMETHYL-2,6,6A,7,11A,11B-HEXAHYDRO-11H-PYRROLO[1',2':2,3]ISOINDOLO[4,5,6-CD]INDOL-11-ONEexperimentalunknownDetails
DB01189DesfluraneapprovedyesinhibitorDetails