ID   AT2A_CHIOP              Reviewed;         143 AA.
AC   P86911;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase {ECO:0000303|PubMed:21059421};
DE            Short=SERCA {ECO:0000303|PubMed:21059421};
DE            EC=7.2.2.10 {ECO:0000250|UniProtKB:Q93084};
DE   Flags: Fragments;
OS   Chionoecetes opilio (Crab-beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Majoidea; Majidae; Chionoecetes.
OX   NCBI_TaxID=41210;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND IGE-BINDING.
RC   TISSUE=Muscle {ECO:0000269|PubMed:21059421};
RX   PubMed=21059421; DOI=10.1016/j.jprot.2010.10.010;
RA   Abdel Rahman A.M., Kamath S.D., Lopata A.L., Robinson J.J., Helleur R.J.;
RT   "Biomolecular characterization of allergenic proteins in snow crab
RT   (Chionoecetes opilio) and de novo sequencing of the second allergen
RT   arginine kinase using tandem mass spectrometry.";
RL   J. Proteomics 74:231-241(2011).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the transport of calcium. Transports calcium ions from
CC       the cytosol into the sarcoplasmic/endoplasmic reticulum lumen.
CC       Contributes to calcium sequestration involved in muscular
CC       excitation/contraction (By similarity). {ECO:0000250|UniProtKB:Q93084}.
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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P04191}. Sarcoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P04191}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:21059421}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIA subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P86911; -.
DR   SMR; P86911; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   SUPFAM; SSF81653; SSF81653; 1.
PE   1: Evidence at protein level;
KW   Allergen; Calcium; Calcium transport; Direct protein sequencing;
KW   Endoplasmic reticulum; Ion transport; Membrane; Metal-binding;
KW   Sarcoplasmic reticulum; Translocase; Transmembrane; Transport.
FT   CHAIN           <1..>143
FT                   /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase"
FT                   /id="PRO_0000410432"
FT   NON_CONS        12..13
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_CONS        30..31
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_CONS        51..52
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_CONS        66..67
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_CONS        79..80
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_CONS        95..96
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_CONS        110..111
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_CONS        118..119
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_CONS        127..128
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:21059421"
FT   NON_TER         143
FT                   /evidence="ECO:0000303|PubMed:21059421"
SQ   SEQUENCE   143 AA;  15161 MW;  899161BBAF723953 CRC64;
     YGPNELPAEE GKNAESAIEA LKEYEPEMGK EIVPGDLVEI SVGDKIPADL RIDQSILTGE
     SVSVIKNILF SGTNVAAGKT QMAETEEIKT PLQQKVGEAT ETALIVLGEK EFTLEFSRVI
     VITGDNKKAE IGIAMGSGTA VAK