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
- FunctionsATP binding / calcium ion binding / calcium-transporting ATPase activity / protein homodimerization activityProcessesapoptotic 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 transportComponentscalcium 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
Resource Link UniProtKB ID O14983 UniProtKB Entry Name AT2A1_HUMAN GenBank Protein ID 158256064 GenBank Gene ID AK291314 HGNC ID HGNC:811 - General References
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB00228 Enflurane approved, investigational, vet_approved unknown inhibitorstimulator Details DB03909 Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate experimental unknown Details DB04444 Tetrafluoroaluminate Ion experimental unknown Details DB04638 2,5-di-tert-butylhydroquinone experimental unknown Details 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-ONE experimental unknown Details DB01189 Desflurane approved yes inhibitor Details DB00867 Ritodrine approved, investigational unknown inhibitor Details DB01236 Sevoflurane approved, vet_approved yes inhibitor Details