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Database: UniProt
Entry: W5NVR5_SHEEP
LinkDB: W5NVR5_SHEEP
Original site: W5NVR5_SHEEP 
ID   W5NVR5_SHEEP            Unreviewed;      1063 AA.
AC   W5NVR5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   Name=ATP2A1 {ECO:0000313|Ensembl:ENSOARP00000002261.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000002261.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000002261.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000002261.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000002261.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
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:0000256|ARBA:ARBA00024147};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC         Evidence={ECO:0000256|ARBA:ARBA00024147};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004326}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675,
CC       ECO:0000256|RuleBase:RU361146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR   EMBL; AMGL01069010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01069011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01069012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01069013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NVR5; -.
DR   SMR; W5NVR5; -.
DR   STRING; 9940.ENSOARP00000002261; -.
DR   PaxDb; 9940-ENSOARP00000002261; -.
DR   Ensembl; ENSOART00000002312.1; ENSOARP00000002261.1; ENSOARG00000002132.1.
DR   eggNOG; KOG0202; Eukaryota.
DR   OMA; YDPMEKA; -.
DR   Proteomes; UP000002356; Chromosome 24.
DR   Bgee; ENSOARG00000002132; Expressed in longissimus thoracis muscle and 50 other cell types or tissues.
DR   ExpressionAtlas; W5NVR5; baseline.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd02083; P-type_ATPase_SERCA; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF24; SARCOPLASMIC_ENDOPLASMIC RETICULUM CALCIUM ATPASE 1; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361146};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW   Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361146};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        79..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        103..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        311..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        778..799
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        851..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        946..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        982..1005
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          22..96
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1017..1063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1023..1042
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1063 AA;  116772 MW;  ED0E23CDA30F5C61 CRC64;
     CENPPRRKTP PPGPQEGSTM EAAHSKTTEE CLAYFGVSET TGLTPDQVKR HLEKYGHNEL
     PAEEGKSLWE LVLEQFEDLL VRILLLAACI SFVLAWFEEG EETVTAFVEP FVILLILIAN
     AIVGVWQERN AENAIEALKE YEPEMGKVYR ADRKSVQRIK ARDIVPGDIV EVAVGDKVPA
     DIRILTIKST TLRVDQSILT GESVSVIKHT EPVPDPRAVN QDKKNMLFSG TNIAAGKAIG
     IVATTGVNTE IGKIRDQMAA TEQDKTPLQQ KLDEFGEQLS KVISLICVAV WLINIGHFND
     PVHGGSWIRG AIYYFKIAVA LAVAAIPEGL PAVITTCLAL GTRRMAKKNA IVRSLPSVET
     LGCTSVICSD KTGTLTTNQM SVCKMFIIDR VDGDLCLLNE FSITGSTYAP EGEVLKNDKP
     VRSGQYDGLV ELATICALCN DSSLDFNEAK GVYEKVGEAT ETALTTLVEK MNVFNTEVRN
     LSKVERANAC NSVIRQLMKK EFTLEFSRDR KSMSVYCSPA KSRAAVGNKM FVKGAPEGVI
     DRCNYVRVGT TRVPMTGPVK EKILSVIKEW GTGRDTLRCL ALATRDTPPK REEMVLDDST
     KFMEYETDLT FVGVVGMLDP PRKEVMGSIQ LCRDAGIRVI MITGDNKGTA IAICRRIGIF
     GENDDVADRA YTGREFDDLP LAEQREACRR ACCFARVEPS HKSKIVEYLQ SYDEITAMTG
     DGVNDAPALK KAEIGIAMGS GTAVAKTASE MVLADDNFST IVAAVEEGRA IYNNMKQFIR
     YLISSNVGEV VCIFLTAALG LPEALIPVQL LWVNLVTDGL PATALGFNPP DLDIMDRPPR
     TPKEPLISGW LFFRYMAIGG YVGAATVGAA AWWFLYAEDG PHVTYSQLTH FMKCSEHNPD
     FEGVDCEVFE APEPMTMALS VLVTIEMCNA LNSLSENQSL MRMPPWVNIW LVGSICLSMS
     LHFLILYVDP LPMIFKLQAL DLYHWLMVLK ISLPVIGIDE ILKFVARNYL EGKRLPPSAS
     ASPCPSSSGP PGPFPPFPRL TPLSPMQTWS PRHPHNLPSP LGP
//
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