AT2A1_RABIT
ID AT2A1_RABIT Reviewed; 1001 AA.
AC P04191; P11719;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 1;
DE Short=SERCA1;
DE Short=SR Ca(2+)-ATPase 1;
DE EC=7.2.2.10 {ECO:0000269|PubMed:10914677, ECO:0000269|PubMed:11438520, ECO:0000269|PubMed:15189864, ECO:0000269|PubMed:18075584, ECO:0000269|PubMed:23996003, ECO:0000269|PubMed:29081402, ECO:0000269|PubMed:8117720};
DE AltName: Full=Calcium pump 1;
DE AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform;
DE AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase;
GN Name=ATP2A1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA1B), AND TISSUE SPECIFICITY.
RX PubMed=2936465; DOI=10.1016/0092-8674(86)90269-2;
RA Brandl C.J., Green N.M., Korczak B., McLennan D.H.;
RT "Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced
RT amino acid sequences.";
RL Cell 44:597-607(1986).
RN [2]
RP PROTEIN SEQUENCE OF 134-140 AND 490-495.
RX PubMed=8761469; DOI=10.1042/bj3180179;
RA Corbalan-Garcia S., Teruel J.A., Gomez-Fernandez J.C.;
RT "Involvement of an arginyl residue in the nucleotide-binding site of
RT Ca(2+)-ATPase from sarcoplasmic reticulum as seen by reaction with
RT phenylglyoxal.";
RL Biochem. J. 318:179-185(1996).
RN [3]
RP PROTEIN SEQUENCE OF 199-212; 335-348 AND 506-519.
RX PubMed=2948019; DOI=10.1007/bf01871021;
RA Andersen J.P., Vilsen B., Collins J.H., Jorgensen P.L.;
RT "Localization of E1-E2 conformational transitions of sarcoplasmic reticulum
RT Ca-ATPase by tryptic cleavage and hydrophobic labeling.";
RL J. Membr. Biol. 93:85-92(1986).
RN [4]
RP PROTEIN SEQUENCE OF 335-365; 468-476; 493-502; 513-529; 606-615; 630-637
RP AND 668-671.
RX PubMed=8218393; DOI=10.1016/0167-4838(93)90036-q;
RA Wawrzynow A., Collins J.H.;
RT "Chemical modification of the Ca(2+)-ATPase of rabbit skeletal muscle
RT sarcoplasmic reticulum: identification of sites labeled with aryl
RT isothiocyanates and thiol-directed conformational probes.";
RL Biochim. Biophys. Acta 1203:60-70(1993).
RN [5]
RP PROTEIN SEQUENCE OF 506-513 AND 584-591, SUBCELLULAR LOCATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=8117720; DOI=10.1021/bi00175a030;
RA Lacapere J.J., Garin J.;
RT "Interaction of 4-azido-2-nitrophenyl phosphate, a pseudosubstrate, with
RT the sarcoplasmic reticulum Ca-ATPase.";
RL Biochemistry 33:2586-2593(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 973-1001 (ISOFORMS SERCA1A AND SERCA1B),
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=3029125; DOI=10.1016/s0021-9258(18)61421-8;
RA Brandl C.J., Deleon S., Martin D.R., McLennan D.H.;
RT "Adult forms of the Ca2+ATPase of sarcoplasmic reticulum. Expression in
RT developing skeletal muscle.";
RL J. Biol. Chem. 262:3768-3774(1987).
RN [7]
RP INTERACTION WITH PHOSPHOLAMBAN, AND ACTIVITY REGULATION.
RX PubMed=8428955; DOI=10.1016/s0021-9258(18)53845-x;
RA Toyofuku T., Kurzydlowski K., Tada M., McLennan D.H.;
RT "Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum
RT that affect functional association with phospholamban.";
RL J. Biol. Chem. 268:2809-2815(1993).
RN [8]
RP INTERACTION WITH PHOSPHOLAMBAN, AND ACTIVITY REGULATION.
RX PubMed=10551848; DOI=10.1074/jbc.274.46.32855;
RA Asahi M., Kimura Y., Kurzydlowski K., Tada M., McLennan D.H.;
RT "Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms
RT a functional interaction site with phospholamban. Evidence for physical
RT interactions at other sites.";
RL J. Biol. Chem. 274:32855-32862(1999).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PRO-789.
RX PubMed=10914677; DOI=10.1007/s004390000297;
RA Odermatt A., Barton K., Khanna V.K., Mathieu J., Escolar D., Kuntzer T.,
RA Karpati G., MacLennan D.H.;
RT "The mutation of Pro(789) to Leu reduces the activity of the fast-twitch
RT skeletal muscle sarco(endo)plasmic reticulum Ca(2+) ATPase (SERCA1) and is
RT associated with Brody disease.";
RL Hum. Genet. 106:482-491(2000).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF CYS-876 AND CYS-888, AND DISULFIDE
RP BOND.
RX PubMed=11438520; DOI=10.1074/jbc.m101229200;
RA Daiho T., Yamasaki K., Saino T., Kamidochi M., Satoh K., Iizuka H.,
RA Suzuki H.;
RT "Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic
RT reticulum Ca2+-ATPase result in a complete loss of Ca2+ transport activity
RT without a loss of Ca2+-dependent ATPase activity. Role of the Cys876-Cys888
RT disulfide bond.";
RL J. Biol. Chem. 276:32771-32778(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=12585965; DOI=10.1042/bj20021477;
RA Newton T., Black J.P., Butler J., Lee A.G., Chad J., East J.M.;
RT "Sarco/endoplasmic-reticulum calcium ATPase SERCA1 is maintained in the
RT endoplasmic reticulum by a retrieval signal located between residues 1 and
RT 211.";
RL Biochem. J. 371:775-782(2003).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=15189864; DOI=10.1529/biophysj.103.036608;
RA Tadini Buoninsegni F., Bartolommei G., Moncelli M.R., Inesi G.,
RA Guidelli R.;
RT "Time-resolved charge translocation by sarcoplasmic reticulum Ca-ATPase
RT measured on a solid supported membrane.";
RL Biophys. J. 86:3671-3686(2004).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PLN AND SLN, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=29081402; DOI=10.1074/jbc.m117.794453;
RA Smeazzetto S., Armanious G.P., Moncelli M.R., Bak J.J., Lemieux M.J.,
RA Young H.S., Tadini-Buoninsegni F.;
RT "Conformational memory in the association of the transmembrane protein
RT phospholamban with the sarcoplasmic reticulum calcium pump SERCA.";
RL J. Biol. Chem. 292:21330-21339(2017).
RN [14] {ECO:0007744|PDB:1SU4}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-993 IN COMPLEXES WITH CALCIUM
RP AND ATP ANALOG, TOPOLOGY, DISULFIDE BONDS, ACTIVE SITE, AND TISSUE
RP SPECIFICITY.
RX PubMed=10864315; DOI=10.1038/35015017;
RA Toyoshima C., Nakasako M., Nomura H., Ogawa H.;
RT "Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A
RT resolution.";
RL Nature 405:647-655(2000).
RN [15] {ECO:0007744|PDB:1IWO}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-993, TOPOLOGY, DOMAIN, AND
RP DISULFIDE BONDS.
RX PubMed=12167852; DOI=10.1038/nature00944;
RA Toyoshima C., Nomura H.;
RT "Structural changes in the calcium pump accompanying the dissociation of
RT calcium.";
RL Nature 418:605-611(2002).
RN [16] {ECO:0007744|PDB:1VFP}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-993 IN COMPLEX WITH ATP ANALOG;
RP CALCIUM AND MAGNESIUM, DOMAIN, TOPOLOGY, AND DISULFIDE BONDS.
RX PubMed=15229613; DOI=10.1038/nature02680;
RA Toyoshima C., Mizutani T.;
RT "Crystal structure of the calcium pump with a bound ATP analogue.";
RL Nature 430:529-535(2004).
RN [17] {ECO:0007744|PDB:1WPG, ECO:0007744|PDB:2ZBD}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-993 IN COMPLEX WITH ADP;
RP CALCIUM AND MAGNESIUM, DOMAIN, AND DISULFIDE BONDS.
RX PubMed=15448704; DOI=10.1038/nature02981;
RA Toyoshima C., Nomura H., Tsuda T.;
RT "Lumenal gating mechanism revealed in calcium pump crystal structures with
RT phosphate analogues.";
RL Nature 432:361-368(2004).
RN [18] {ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-993 IN COMPLEX WITH ADP; ATP
RP ANALOG; CALCIUM AND MAGNESIUM, TOPOLOGY, AND DOMAIN.
RX PubMed=15192230; DOI=10.1126/science.1099366;
RA Sorensen T.L., Moller J.V., Nissen P.;
RT "Phosphoryl transfer and calcium ion occlusion in the calcium pump.";
RL Science 304:1672-1675(2004).
RN [19] {ECO:0007744|PDB:1XP5}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-993 IN COMPLEX WITH MAGNESIUM
RP AND TRANSITION STATE ANALOG, AND DOMAIN.
RX PubMed=15618517; DOI=10.1126/science.1106289;
RA Olesen C., Sorensen T.L., Nielsen R.C., Moller J.V., Nissen P.;
RT "Dephosphorylation of the calcium pump coupled to counterion occlusion.";
RL Science 306:2251-2255(2004).
RN [20] {ECO:0007744|PDB:2C88, ECO:0007744|PDB:2C8K, ECO:0007744|PDB:2C8L, ECO:0007744|PDB:2C9M}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-993 IN COMPLEX WITH ATP ANALOG
RP AND CALCIUM, DOMAIN, AND DISULFIDE BONDS.
RX PubMed=16710301; DOI=10.1038/sj.emboj.7601135;
RA Jensen A.M., Sorensen T.L., Olesen C., Moller J.V., Nissen P.;
RT "Modulatory and catalytic modes of ATP binding by the calcium pump.";
RL EMBO J. 25:2305-2314(2006).
RN [21] {ECO:0007744|PDB:3B9B, ECO:0007744|PDB:3B9R, ECO:0007744|PDB:3BA6}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-993 IN COMPLEX WITH ATP ANALOG;
RP CALCIUM AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, ACTIVE SITE, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, TISSUE
RP SPECIFICITY, AND DISULFIDE BONDS.
RX PubMed=18075584; DOI=10.1038/nature06418;
RA Olesen C., Picard M., Winther A.M., Gyrup C., Morth J.P., Oxvig C.,
RA Moller J.V., Nissen P.;
RT "The structural basis of calcium transport by the calcium pump.";
RL Nature 450:1036-1042(2007).
RN [22] {ECO:0007744|PDB:4NAB}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-993 OF MUTANT GLN-309 IN
RP COMPLEX WITH CALCIUM, FUNCTION, DOMAIN, DISULFIDE BONDS, AND MUTAGENESIS OF
RP GLU-309.
RX PubMed=24270570; DOI=10.1038/emboj.2013.250;
RA Clausen J.D., Bublitz M., Arnou B., Montigny C., Jaxel C., Moller J.V.,
RA Nissen P., Andersen J.P., le Maire M.;
RT "SERCA mutant E309Q binds two Ca(2+) ions but adopts a catalytically
RT incompetent conformation.";
RL EMBO J. 32:3231-3243(2013).
RN [23] {ECO:0007744|PDB:4KYT, ECO:0007744|PDB:4Y3U}
RP X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 1-993 IN COMPLEX WITH PLN,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DISULFIDE BONDS, AND DOMAIN.
RX PubMed=23996003; DOI=10.1074/jbc.m113.501585;
RA Akin B.L., Hurley T.D., Chen Z., Jones L.R.;
RT "The structural basis for phospholamban inhibition of the calcium pump in
RT sarcoplasmic reticulum.";
RL J. Biol. Chem. 288:30181-30191(2013).
RN [24] {ECO:0007744|PDB:3W5A, ECO:0007744|PDB:3W5B, ECO:0007744|PDB:3W5C, ECO:0007744|PDB:3W5D}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-993 IN COMPLEX WITH SLN AND
RP MAGNESIUM, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOPOLOGY, DOMAIN, AND
RP DISULFIDE BONDS.
RX PubMed=23455422; DOI=10.1038/nature11899;
RA Toyoshima C., Iwasawa S., Ogawa H., Hirata A., Tsueda J., Inesi G.;
RT "Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1
RT state.";
RL Nature 495:260-264(2013).
RN [25] {ECO:0007744|PDB:4H1W}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-993 IN COMPLEX WITH SLN; ATP
RP ANALOG AND MAGNESIUM, AND DOMAIN.
RX PubMed=23455424; DOI=10.1038/nature11900;
RA Winther A.M., Bublitz M., Karlsen J.L., Moller J.V., Hansen J.B.,
RA Nissen P., Buch-Pedersen M.J.;
RT "The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the
RT cytoplasm.";
RL Nature 495:265-269(2013).
RN [26] {ECO:0007744|PDB:4XOU}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-993 IN COMPLEX WITH ATP ANALOG
RP AND CALCIUM, AND TOPOLOGY.
RX PubMed=26175901; DOI=10.1107/s2052252515008969;
RA Bublitz M., Nass K., Drachmann N.D., Markvardsen A.J., Gutmann M.J.,
RA Barends T.R., Mattle D., Shoeman R.L., Doak R.B., Boutet S.,
RA Messerschmidt M., Seibert M.M., Williams G.J., Foucar L., Reinhard L.,
RA Sitsel O., Gregersen J.L., Clausen J.D., Boesen T., Gotfryd K., Wang K.T.,
RA Olesen C., Moller J.V., Nissen P., Schlichting I.;
RT "Structural studies of P-type ATPase-ligand complexes using an X-ray free-
RT electron laser.";
RL IUCrJ 2:409-420(2015).
RN [27] {ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8, ECO:0007744|PDB:5XA9, ECO:0007744|PDB:5XAA, ECO:0007744|PDB:5XAB}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-993 IN COMPLEX WITH ADP AND
RP CALCIUM, TOPOLOGY, DISULFIDE BONDS, AND DOMAIN.
RX PubMed=28467821; DOI=10.1038/nature22357;
RA Norimatsu Y., Hasegawa K., Shimizu N., Toyoshima C.;
RT "Protein-phospholipid interplay revealed with crystals of a calcium pump.";
RL Nature 545:193-198(2017).
RN [28] {ECO:0007744|PDB:5ZMV}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-993 OF MUTANTS ALA/GLN-309,
RP DOMAIN, DISULFIDE BONDS, AND MUTAGENESIS OF GLU-309.
RX PubMed=30482857; DOI=10.1073/pnas.1815472115;
RA Tsunekawa N., Ogawa H., Tsueda J., Akiba T., Toyoshima C.;
RT "Mechanism of the E2 to E1 transition in Ca2+ pump revealed by crystal
RT structures of gating residue mutants.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:12722-12727(2018).
CC -!- FUNCTION: Key regulator of striated muscle performance by acting as the
CC major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+)
CC into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP
CC coupled with the translocation of calcium from the cytosol to the
CC sarcoplasmic reticulum lumen (PubMed:10914677, PubMed:11438520,
CC PubMed:15189864, PubMed:29081402, PubMed:18075584, PubMed:24270570,
CC PubMed:23996003). Contributes to calcium sequestration involved in
CC muscular excitation/contraction. {ECO:0000250|UniProtKB:Q8R429,
CC ECO:0000269|PubMed:10914677, ECO:0000269|PubMed:11438520,
CC ECO:0000269|PubMed:15189864, ECO:0000269|PubMed:18075584,
CC ECO:0000269|PubMed:23996003, ECO:0000269|PubMed:24270570,
CC ECO:0000269|PubMed:29081402}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000269|PubMed:10914677, ECO:0000269|PubMed:11438520,
CC ECO:0000269|PubMed:15189864, ECO:0000269|PubMed:18075584,
CC ECO:0000269|PubMed:23996003, ECO:0000269|PubMed:29081402,
CC ECO:0000269|PubMed:8117720};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000305|PubMed:10914677};
CC -!- ACTIVITY REGULATION: Inhibited by sarcolipin (SLN) and myoregulin
CC (MRLN) (PubMed:10551848, PubMed:8428955, PubMed:29081402). Inhibited by
CC phospholamban (PLN) (PubMed:10551848, PubMed:8428955, PubMed:29081402,
CC PubMed:23996003). Reversibly inhibited by phospholamban (PLN) at low
CC calcium concentrations (PubMed:10551848, PubMed:8428955,
CC PubMed:29081402, PubMed:23996003). Dephosphorylated PLN decreases the
CC apparent affinity of the ATPase for calcium (PubMed:10551848,
CC PubMed:8428955). This inhibition is regulated by the phosphorylation of
CC PLN (PubMed:10551848, PubMed:8428955). Enhanced by DWORF; DWORF
CC increases activity by displacing sarcolipin (SLN), phospholamban (PLN)
CC and myoregulin (MRLN) (By similarity). {ECO:0000250|UniProtKB:Q8R429,
CC ECO:0000269|PubMed:10551848, ECO:0000269|PubMed:23996003,
CC ECO:0000269|PubMed:29081402, ECO:0000269|PubMed:8428955}.
CC -!- SUBUNIT: Interacts with sarcolipin (SLN) (PubMed:29081402,
CC PubMed:23455422, PubMed:23455424). Interacts with phospholamban (PLN)
CC (PubMed:8428955, PubMed:10551848, PubMed:29081402, PubMed:23996003).
CC Interacts with myoregulin (MRLN) (By similarity). Interacts with DWORF
CC (By similarity). Interacts VMP1 (By similarity).
CC {ECO:0000250|UniProtKB:O14983, ECO:0000250|UniProtKB:Q8R429,
CC ECO:0000269|PubMed:10551848, ECO:0000269|PubMed:23455422,
CC ECO:0000269|PubMed:23455424, ECO:0000269|PubMed:23996003,
CC ECO:0000269|PubMed:29081402, ECO:0000269|PubMed:8428955}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12585965}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:12167852,
CC ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
CC ECO:0000269|PubMed:15448704, ECO:0000269|PubMed:15618517,
CC ECO:0000269|PubMed:16710301, ECO:0000269|PubMed:18075584,
CC ECO:0000269|PubMed:23455422, ECO:0000269|PubMed:23455424,
CC ECO:0000269|PubMed:23996003, ECO:0000269|PubMed:24270570,
CC ECO:0000269|PubMed:26175901, ECO:0000269|PubMed:28467821,
CC ECO:0000269|PubMed:30482857}. Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11438520, ECO:0000269|PubMed:15189864,
CC ECO:0000269|PubMed:18075584, ECO:0000269|PubMed:23455422,
CC ECO:0000269|PubMed:23996003, ECO:0000269|PubMed:29081402,
CC ECO:0000269|PubMed:8117720}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:12167852,
CC ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
CC ECO:0000269|PubMed:15448704, ECO:0000269|PubMed:15618517,
CC ECO:0000269|PubMed:16710301, ECO:0000269|PubMed:18075584,
CC ECO:0000269|PubMed:23455422, ECO:0000269|PubMed:23455424,
CC ECO:0000269|PubMed:23996003, ECO:0000269|PubMed:24270570,
CC ECO:0000269|PubMed:26175901, ECO:0000269|PubMed:28467821,
CC ECO:0000269|PubMed:30482857}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=SERCA1B; Synonyms=Neonatal;
CC IsoId=P04191-1; Sequence=Displayed;
CC Name=SERCA1A; Synonyms=Adult;
CC IsoId=P04191-2; Sequence=VSP_000356;
CC -!- TISSUE SPECIFICITY: Skeletal muscle (at protein level)
CC (PubMed:11438520, PubMed:15189864, PubMed:29081402, PubMed:10864315,
CC PubMed:18075584, PubMed:23996003, PubMed:23455422). Skeletal muscle,
CC fast twitch muscle (type II) fibers (PubMed:2936465, PubMed:3029125).
CC {ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:11438520,
CC ECO:0000269|PubMed:15189864, ECO:0000269|PubMed:18075584,
CC ECO:0000269|PubMed:23455422, ECO:0000269|PubMed:23996003,
CC ECO:0000269|PubMed:29081402, ECO:0000269|PubMed:2936465,
CC ECO:0000269|PubMed:3029125}.
CC -!- DEVELOPMENTAL STAGE: Isoform SERCA1A and isoform SERCA1B are
CC predominantly found in adult and neonatal skeletal muscle respectively.
CC {ECO:0000269|PubMed:3029125}.
CC -!- DOMAIN: Ca(2+) and ATP binding cause major rearrangements of the
CC cytoplasmic and transmembrane domains. According to the E1-E2 model,
CC Ca(2+) binding to the cytosolic domain of the pump in the high-affinity
CC E1 conformation is followed by the ATP-dependent phosphorylation of the
CC active site Asp, giving rise to E1P. A conformational change of the
CC phosphoenzyme gives rise to the low-affinity E2P state that exposes the
CC Ca(2+) ions to the lumenal side and promotes Ca(2+) release.
CC Dephosphorylation of the active site Asp mediates the subsequent return
CC to the E1 conformation. {ECO:0000269|PubMed:12167852,
CC ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
CC ECO:0000269|PubMed:15448704, ECO:0000269|PubMed:15618517,
CC ECO:0000269|PubMed:16710301, ECO:0000269|PubMed:18075584,
CC ECO:0000269|PubMed:23455422, ECO:0000269|PubMed:23455424,
CC ECO:0000269|PubMed:24270570, ECO:0000269|PubMed:28467821,
CC ECO:0000269|PubMed:30482857, ECO:0000305}.
CC -!- DOMAIN: PLN and SLN both have a single transmembrane helix; both occupy
CC a similar binding site on ATP2A1 that is situated between the ATP2A1
CC transmembrane helices. {ECO:0000269|PubMed:23455422,
CC ECO:0000269|PubMed:23455424, ECO:0000269|PubMed:23996003}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M12898; AAA31165.1; -; mRNA.
DR EMBL; M15351; AAA31166.1; -; mRNA.
DR EMBL; M15158; AAA31167.1; -; mRNA.
DR PIR; A01075; PWRBFC.
DR RefSeq; NP_001082787.1; NM_001089318.1. [P04191-1]
DR PDB; 1IWO; X-ray; 3.10 A; A/B=1-994.
DR PDB; 1KJU; EM; 6.00 A; A=1-994.
DR PDB; 1SU4; X-ray; 2.40 A; A=1-994.
DR PDB; 1T5S; X-ray; 2.60 A; A=1-993.
DR PDB; 1T5T; X-ray; 2.90 A; A=1-993.
DR PDB; 1VFP; X-ray; 2.90 A; A/B=1-994.
DR PDB; 1WPG; X-ray; 2.30 A; A/B/C/D=1-993.
DR PDB; 1XP5; X-ray; 3.00 A; A=1-993.
DR PDB; 2AGV; X-ray; 2.40 A; A/B=1-993.
DR PDB; 2BY4; X-ray; 3.30 A; A=1-993.
DR PDB; 2C88; X-ray; 3.10 A; A=1-993.
DR PDB; 2C8K; X-ray; 2.80 A; A=1-993.
DR PDB; 2C8L; X-ray; 3.10 A; A=1-993.
DR PDB; 2C9M; X-ray; 3.00 A; A/B=1-993.
DR PDB; 2DQS; X-ray; 2.50 A; A=1-993.
DR PDB; 2EAR; X-ray; 3.10 A; A=1-993.
DR PDB; 2EAT; X-ray; 2.90 A; A=1-993.
DR PDB; 2EAU; X-ray; 2.80 A; A=1-993.
DR PDB; 2O9J; X-ray; 2.65 A; A=1-993.
DR PDB; 2OA0; X-ray; 3.40 A; A=1-993.
DR PDB; 2VOY; EM; 18.00 A; B=36-77, C=967-988, D=832-854, E=86-115, G=243-278, H=289-336, K=749-780, L=789-809.
DR PDB; 2YFY; X-ray; 3.10 A; A=1-993.
DR PDB; 2ZBD; X-ray; 2.40 A; A=1-993.
DR PDB; 2ZBE; X-ray; 3.80 A; A/B=1-993.
DR PDB; 2ZBF; X-ray; 2.40 A; A=1-993.
DR PDB; 2ZBG; X-ray; 2.55 A; A=1-993.
DR PDB; 3AR2; X-ray; 2.50 A; A=1-994.
DR PDB; 3AR3; X-ray; 2.30 A; A=1-994.
DR PDB; 3AR4; X-ray; 2.15 A; A=1-994.
DR PDB; 3AR5; X-ray; 2.20 A; A=1-994.
DR PDB; 3AR6; X-ray; 2.20 A; A=1-994.
DR PDB; 3AR7; X-ray; 2.15 A; A=1-994.
DR PDB; 3AR8; X-ray; 2.60 A; A=1-994.
DR PDB; 3AR9; X-ray; 2.60 A; A=1-994.
DR PDB; 3B9B; X-ray; 2.65 A; A=1-993.
DR PDB; 3B9R; X-ray; 3.00 A; A/B=1-993.
DR PDB; 3BA6; X-ray; 2.80 A; A=1-993.
DR PDB; 3FGO; X-ray; 2.50 A; A/B=1-994.
DR PDB; 3FPB; X-ray; 2.55 A; A=1-994.
DR PDB; 3FPS; X-ray; 3.20 A; A=1-994.
DR PDB; 3J7T; EM; 3.40 A; A=1-994.
DR PDB; 3N5K; X-ray; 2.20 A; A/B=1-994.
DR PDB; 3N8G; X-ray; 2.58 A; A=1-993.
DR PDB; 3W5A; X-ray; 3.01 A; A/B=1-993.
DR PDB; 3W5B; X-ray; 3.20 A; A=1-993.
DR PDB; 3W5C; X-ray; 2.50 A; A=1-993.
DR PDB; 3W5D; X-ray; 2.45 A; A=1-993.
DR PDB; 4BEW; X-ray; 2.50 A; A/B=1-994.
DR PDB; 4H1W; X-ray; 3.10 A; A=1-993.
DR PDB; 4J2T; X-ray; 3.20 A; A=1-993.
DR PDB; 4KYT; X-ray; 2.83 A; A=1-993.
DR PDB; 4NAB; X-ray; 3.50 A; A=1-993.
DR PDB; 4UU0; X-ray; 2.50 A; A=1-993.
DR PDB; 4UU1; X-ray; 2.80 A; A=1-993.
DR PDB; 4XOU; X-ray; 2.80 A; A=1-993.
DR PDB; 4Y3U; X-ray; 3.51 A; A=1-993.
DR PDB; 4YCL; X-ray; 3.25 A; A=1-993.
DR PDB; 4YCM; X-ray; 3.20 A; A=2-993.
DR PDB; 4YCN; X-ray; 3.50 A; A=2-993.
DR PDB; 5A3Q; X-ray; 3.05 A; A=1-993.
DR PDB; 5A3R; X-ray; 3.05 A; A=1-993.
DR PDB; 5A3S; X-ray; 3.30 A; A/B=1-993.
DR PDB; 5NCQ; X-ray; 3.00 A; A=1-993.
DR PDB; 5XA7; X-ray; 3.20 A; A=1-993.
DR PDB; 5XA8; X-ray; 3.20 A; A=1-993.
DR PDB; 5XA9; X-ray; 3.20 A; A=1-993.
DR PDB; 5XAA; X-ray; 3.20 A; A=1-993.
DR PDB; 5XAB; X-ray; 3.20 A; A=1-993.
DR PDB; 5ZMV; X-ray; 3.30 A; A=1-993.
DR PDB; 5ZMW; X-ray; 2.50 A; A=1-993.
DR PDB; 6HEF; X-ray; 3.54 A; A=1-993.
DR PDB; 6RB2; X-ray; 3.20 A; A=1-993.
DR PDB; 6YAA; X-ray; 3.40 A; A=1-993.
DR PDB; 6YSO; X-ray; 3.13 A; A/B=1-993.
DR PDBsum; 1IWO; -.
DR PDBsum; 1KJU; -.
DR PDBsum; 1SU4; -.
DR PDBsum; 1T5S; -.
DR PDBsum; 1T5T; -.
DR PDBsum; 1VFP; -.
DR PDBsum; 1WPG; -.
DR PDBsum; 1XP5; -.
DR PDBsum; 2AGV; -.
DR PDBsum; 2BY4; -.
DR PDBsum; 2C88; -.
DR PDBsum; 2C8K; -.
DR PDBsum; 2C8L; -.
DR PDBsum; 2C9M; -.
DR PDBsum; 2DQS; -.
DR PDBsum; 2EAR; -.
DR PDBsum; 2EAT; -.
DR PDBsum; 2EAU; -.
DR PDBsum; 2O9J; -.
DR PDBsum; 2OA0; -.
DR PDBsum; 2VOY; -.
DR PDBsum; 2YFY; -.
DR PDBsum; 2ZBD; -.
DR PDBsum; 2ZBE; -.
DR PDBsum; 2ZBF; -.
DR PDBsum; 2ZBG; -.
DR PDBsum; 3AR2; -.
DR PDBsum; 3AR3; -.
DR PDBsum; 3AR4; -.
DR PDBsum; 3AR5; -.
DR PDBsum; 3AR6; -.
DR PDBsum; 3AR7; -.
DR PDBsum; 3AR8; -.
DR PDBsum; 3AR9; -.
DR PDBsum; 3B9B; -.
DR PDBsum; 3B9R; -.
DR PDBsum; 3BA6; -.
DR PDBsum; 3FGO; -.
DR PDBsum; 3FPB; -.
DR PDBsum; 3FPS; -.
DR PDBsum; 3J7T; -.
DR PDBsum; 3N5K; -.
DR PDBsum; 3N8G; -.
DR PDBsum; 3W5A; -.
DR PDBsum; 3W5B; -.
DR PDBsum; 3W5C; -.
DR PDBsum; 3W5D; -.
DR PDBsum; 4BEW; -.
DR PDBsum; 4H1W; -.
DR PDBsum; 4J2T; -.
DR PDBsum; 4KYT; -.
DR PDBsum; 4NAB; -.
DR PDBsum; 4UU0; -.
DR PDBsum; 4UU1; -.
DR PDBsum; 4XOU; -.
DR PDBsum; 4Y3U; -.
DR PDBsum; 4YCL; -.
DR PDBsum; 4YCM; -.
DR PDBsum; 4YCN; -.
DR PDBsum; 5A3Q; -.
DR PDBsum; 5A3R; -.
DR PDBsum; 5A3S; -.
DR PDBsum; 5NCQ; -.
DR PDBsum; 5XA7; -.
DR PDBsum; 5XA8; -.
DR PDBsum; 5XA9; -.
DR PDBsum; 5XAA; -.
DR PDBsum; 5XAB; -.
DR PDBsum; 5ZMV; -.
DR PDBsum; 5ZMW; -.
DR PDBsum; 6HEF; -.
DR PDBsum; 6RB2; -.
DR PDBsum; 6YAA; -.
DR PDBsum; 6YSO; -.
DR AlphaFoldDB; P04191; -.
DR BMRB; P04191; -.
DR PCDDB; P04191; -.
DR SMR; P04191; -.
DR IntAct; P04191; 4.
DR MINT; P04191; -.
DR STRING; 9986.ENSOCUP00000002327; -.
DR BindingDB; P04191; -.
DR ChEMBL; CHEMBL4693; -.
DR TCDB; 3.A.3.2.43; the p-type atpase (p-atpase) superfamily.
DR SwissPalm; P04191; -.
DR PRIDE; P04191; -.
DR GeneID; 100037716; -.
DR KEGG; ocu:100037716; -.
DR CTD; 487; -.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; P04191; -.
DR OrthoDB; 100699at2759; -.
DR BRENDA; 7.2.2.10; 1749.
DR SABIO-RK; P04191; -.
DR EvolutionaryTrace; P04191; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0031673; C:H zone; ISS:UniProtKB.
DR GO; GO:0031674; C:I band; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:UniProtKB.
DR GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0045988; P:negative regulation of striated muscle contraction; ISS:UniProtKB.
DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:1902082; P:positive regulation of calcium ion import into sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0106134; P:positive regulation of cardiac muscle cell contraction; ISS:UniProtKB.
DR GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; ISS:UniProtKB.
DR GO; GO:0006942; P:regulation of striated muscle contraction; ISS:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Calcium;
KW Calcium transport; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1001
FT /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase 1"
FT /id="PRO_0000046189"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 70..89
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 111..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 254..273
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 274..295
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 296..313
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 314..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 758..777
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 778..787
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 788..808
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 809..828
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 829..851
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 852..897
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 898..917
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 918..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 931..949
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 950..964
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TRANSMEM 965..985
FT /note="Helical; Name=10"
FT /evidence="ECO:0000269|PubMed:10864315"
FT TOPO_DOM 986..1001
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10864315"
FT REGION 788..808
FT /note="Interaction with PLN"
FT /evidence="ECO:0000269|PubMed:10551848,
FT ECO:0000269|PubMed:23996003"
FT REGION 932..943
FT /note="Interaction with PLN"
FT /evidence="ECO:0000269|PubMed:23996003"
FT ACT_SITE 351
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:18075584"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1VFP,
FT ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6,
FT ECO:0007744|PDB:3N8G, ECO:0007744|PDB:5XA7,
FT ECO:0007744|PDB:5XA8"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2,
FT ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G,
FT ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2ZBD,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6,
FT ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB,
FT ECO:0007744|PDB:4XOU"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2,
FT ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G,
FT ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7,
FT ECO:0007744|PDB:5XA8"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:15229613, ECO:0007744|PDB:1T5S,
FT ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP,
FT ECO:0007744|PDB:1WPG, ECO:0007744|PDB:1XP5,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:2ZBE,
FT ECO:0007744|PDB:2ZBF, ECO:0007744|PDB:2ZBG,
FT ECO:0007744|PDB:3AR8, ECO:0007744|PDB:3AR9,
FT ECO:0007744|PDB:3B9B, ECO:0007744|PDB:3B9R,
FT ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB,
FT ECO:0007744|PDB:3N5K, ECO:0007744|PDB:4BEW,
FT ECO:0007744|PDB:5A3Q, ECO:0007744|PDB:5A3S"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1VFP,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G,
FT ECO:0007744|PDB:4H1W, ECO:0007744|PDB:4XOU"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:15229613, ECO:0007744|PDB:1T5S,
FT ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP,
FT ECO:0007744|PDB:1WPG, ECO:0007744|PDB:1XP5,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:2ZBE,
FT ECO:0007744|PDB:2ZBF, ECO:0007744|PDB:2ZBG,
FT ECO:0007744|PDB:3AR8, ECO:0007744|PDB:3AR9,
FT ECO:0007744|PDB:3B9B, ECO:0007744|PDB:3B9R,
FT ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB,
FT ECO:0007744|PDB:3N5K, ECO:0007744|PDB:4BEW,
FT ECO:0007744|PDB:5A3Q, ECO:0007744|PDB:5A3S"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C88,
FT ECO:0007744|PDB:2DQS, ECO:0007744|PDB:2ZBD,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3AR3,
FT ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU,
FT ECO:0007744|PDB:5XA8"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:1VFP, ECO:0007744|PDB:1WPG,
FT ECO:0007744|PDB:2DQS, ECO:0007744|PDB:2ZBD,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3B9R,
FT ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB,
FT ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4BEW,
FT ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8"
FT BINDING 515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S,
FT ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C8K,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G,
FT ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU"
FT BINDING 560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1VFP,
FT ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C88,
FT ECO:0007744|PDB:2C8K, ECO:0007744|PDB:2DQS,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3B9R,
FT ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4H1W,
FT ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU"
FT BINDING 625..627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2OA0,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2,
FT ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4UU1,
FT ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8"
FT BINDING 678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S,
FT ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2,
FT ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB,
FT ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4BEW,
FT ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8"
FT BINDING 684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G,
FT ECO:0007744|PDB:4XOU"
FT BINDING 703
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:15229613, ECO:0007744|PDB:1T5S,
FT ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP,
FT ECO:0007744|PDB:1WPG, ECO:0007744|PDB:1XP5,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:2ZBE,
FT ECO:0007744|PDB:2ZBF, ECO:0007744|PDB:2ZBG,
FT ECO:0007744|PDB:3AR8, ECO:0007744|PDB:3AR9,
FT ECO:0007744|PDB:3B9B, ECO:0007744|PDB:3B9R,
FT ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB,
FT ECO:0007744|PDB:3N5K, ECO:0007744|PDB:4BEW,
FT ECO:0007744|PDB:5A3Q, ECO:0007744|PDB:5A3S"
FT BINDING 706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S,
FT ECO:0007744|PDB:1VFP, ECO:0007744|PDB:3AR2,
FT ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU"
FT BINDING 768
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2,
FT ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G,
FT ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU,
FT ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8"
FT BINDING 771
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2,
FT ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G,
FT ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8"
FT BINDING 796
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15192230,
FT ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901,
FT ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S,
FT ECO:0007744|PDB:1T5T, ECO:0007744|PDB:2ZBD,
FT ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G,
FT ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7,
FT ECO:0007744|PDB:5XA8"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M,
FT ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2,
FT ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G,
FT ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU,
FT ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T,
FT ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2ZBD,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:4XOU,
FT ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4,
FT ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP,
FT ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6,
FT ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB,
FT ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7,
FT ECO:0007744|PDB:5XA8"
FT BINDING 908
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613,
FT ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4,
FT ECO:0007744|PDB:1T5S, ECO:0007744|PDB:2C9M,
FT ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6,
FT ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64578"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64578"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64578"
FT DISULFID 876..888
FT /evidence="ECO:0000269|PubMed:10864315,
FT ECO:0000269|PubMed:11438520, ECO:0000269|PubMed:12167852,
FT ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:15448704,
FT ECO:0000269|PubMed:16710301, ECO:0000269|PubMed:18075584,
FT ECO:0000269|PubMed:23455422, ECO:0000269|PubMed:23996003,
FT ECO:0000269|PubMed:24270570, ECO:0000269|PubMed:28467821,
FT ECO:0000269|PubMed:30482857, ECO:0007744|PDB:1IWO,
FT ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1VFP,
FT ECO:0007744|PDB:1WPG, ECO:0007744|PDB:2AGV,
FT ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C88,
FT ECO:0007744|PDB:2C8K, ECO:0007744|PDB:2C8L,
FT ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2DQS,
FT ECO:0007744|PDB:2EAR, ECO:0007744|PDB:2EAT,
FT ECO:0007744|PDB:2EAU, ECO:0007744|PDB:2O9J,
FT ECO:0007744|PDB:2YFY, ECO:0007744|PDB:2ZBD,
FT ECO:0007744|PDB:2ZBE, ECO:0007744|PDB:2ZBF,
FT ECO:0007744|PDB:2ZBG, ECO:0007744|PDB:3AR2,
FT ECO:0007744|PDB:3AR3, ECO:0007744|PDB:3AR4,
FT ECO:0007744|PDB:3AR5, ECO:0007744|PDB:3AR6,
FT ECO:0007744|PDB:3AR7, ECO:0007744|PDB:3AR8,
FT ECO:0007744|PDB:3AR9, ECO:0007744|PDB:3B9B,
FT ECO:0007744|PDB:3B9R, ECO:0007744|PDB:3FGO,
FT ECO:0007744|PDB:3FPB, ECO:0007744|PDB:3FPS,
FT ECO:0007744|PDB:3J7T, ECO:0007744|PDB:3N5K,
FT ECO:0007744|PDB:3W5A, ECO:0007744|PDB:3W5B,
FT ECO:0007744|PDB:3W5C, ECO:0007744|PDB:3W5D,
FT ECO:0007744|PDB:4BEW, ECO:0007744|PDB:4J2T,
FT ECO:0007744|PDB:4KYT, ECO:0007744|PDB:4NAB,
FT ECO:0007744|PDB:4UU0, ECO:0007744|PDB:4UU1,
FT ECO:0007744|PDB:4Y3U, ECO:0007744|PDB:4YCL,
FT ECO:0007744|PDB:4YCM, ECO:0007744|PDB:4YCN,
FT ECO:0007744|PDB:5A3Q, ECO:0007744|PDB:5A3R,
FT ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5ZMV"
FT VAR_SEQ 994..1001
FT /note="DPEDERRK -> G (in isoform SERCA1A)"
FT /evidence="ECO:0000303|PubMed:3029125"
FT /id="VSP_000356"
FT MUTAGEN 309
FT /note="E->A: Interferes with conformation changes that are
FT essential for ATP-dependent Ca(2+) transport."
FT /evidence="ECO:0000269|PubMed:30482857"
FT MUTAGEN 309
FT /note="E->Q: No loss of calcium binding. Strongly decreased
FT rate of phosphorylation of the active site Asp residue.
FT Interferes with conformation changes that are essential for
FT ATP-dependent Ca(2+)transport."
FT /evidence="ECO:0000269|PubMed:24270570,
FT ECO:0000269|PubMed:30482857"
FT MUTAGEN 789
FT /note="P->L: Almost complete loss of Ca(2+) transport
FT activity because of reduced Ca(2+) affinity."
FT /evidence="ECO:0000269|PubMed:10914677"
FT MUTAGEN 876
FT /note="C->A: Loss of ATP-dependent Ca(2+)transport."
FT /evidence="ECO:0000269|PubMed:11438520"
FT MUTAGEN 888
FT /note="C->A: Loss of ATP-dependent Ca(2+)transport."
FT /evidence="ECO:0000269|PubMed:11438520"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5ZMW"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2ZBG"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3AR7"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 89..111
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3J7T"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2EAU"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 248..273
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 288..306
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 362..373
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:4KYT"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 408..419
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:3J7T"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:1WPG"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:3W5C"
FT HELIX 470..478
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 479..488
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 489..492
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 493..502
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 503..508
FT /evidence="ECO:0007829|PDB:1WPG"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 518..523
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 539..554
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:3N5K"
FT STRAND 560..569
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 584..587
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 590..600
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 607..616
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 620..627
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 629..638
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 640..642
FT /evidence="ECO:0007829|PDB:3W5D"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:4YCN"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 655..659
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 663..672
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 683..692
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 693..695
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 698..702
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 708..713
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 716..720
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 725..729
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 732..735
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 740..780
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 789..797
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 798..800
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 801..807
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 816..818
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:2ZBD"
FT HELIX 831..855
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 856..858
FT /evidence="ECO:0007829|PDB:3AR3"
FT STRAND 860..862
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 866..868
FT /evidence="ECO:0007829|PDB:3AR5"
FT HELIX 870..872
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 873..875
FT /evidence="ECO:0007829|PDB:1SU4"
FT STRAND 876..879
FT /evidence="ECO:0007829|PDB:3N5K"
FT TURN 880..882
FT /evidence="ECO:0007829|PDB:3N5K"
FT STRAND 884..886
FT /evidence="ECO:0007829|PDB:3W5D"
FT HELIX 890..892
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 894..913
FT /evidence="ECO:0007829|PDB:3AR4"
FT STRAND 916..919
FT /evidence="ECO:0007829|PDB:1SU4"
FT TURN 922..924
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 927..929
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 931..949
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 952..956
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 964..974
FT /evidence="ECO:0007829|PDB:3AR4"
FT HELIX 976..990
FT /evidence="ECO:0007829|PDB:3AR4"
FT TURN 991..993
FT /evidence="ECO:0007829|PDB:5A3Q"
SQ SEQUENCE 1001 AA; 110459 MW; 1F0D8C36CF975266 CRC64;
MEAAHSKSTE ECLAYFGVSE TTGLTPDQVK RHLEKYGHNE LPAEEGKSLW ELVIEQFEDL
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILIA NAIVGVWQER NAENAIEALK
EYEPEMGKVY RADRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRILSIKS TTLRVDQSIL
TGESVSVIKH TEPVPDPRAV NQDKKNMLFS GTNIAAGKAL GIVATTGVST EIGKIRDQMA
ATEQDKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWIR GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCKMFIID KVDGDFCSLN EFSITGSTYA PEGEVLKNDK PIRSGQFDGL VELATICALC
NDSSLDFNET KGVYEKVGEA TETALTTLVE KMNVFNTEVR NLSKVERANA CNSVIRQLMK
KEFTLEFSRD RKSMSVYCSP AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPMTGP
VKEKILSVIK EWGTGRDTLR CLALATRDTP PKREEMVLDD SSRFMEYETD LTFVGVVGML
DPPRKEVMGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD RAYTGREFDD
LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM TGDGVNDAPA LKKAEIGIAM
GSGTAVAKTA SEMVLADDNF STIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAA
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI
GGYVGAATVG AAAWWFMYAE DGPGVTYHQL THFMQCTEDH PHFEGLDCEI FEAPEPMTMA
LSVLVTIEMC NALNSLSENQ SLMRMPPWVN IWLLGSICLS MSLHFLILYV DPLPMIFKLK
ALDLTQWLMV LKISLPVIGL DEILKFIARN YLEDPEDERR K
