UniProt: A0A1S3LIW7

Database: UniProt
Entry: A0A1S3LIW7_SALSA

LinkDB:  A0A1S3LIW7_SALSA 
Original site:  A0A1S3LIW7_SALSA

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (21)   
   InterPro (13)   
   Pfam (6)   
   PROSITE (1)   
   SMART (1)   
All databases (33)   

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ID   A0A1S3LIW7_SALSA        Unreviewed;      1289 AA.
AC   A0A1S3LIW7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   08-OCT-2025, sequence version 2.
DT   28-JAN-2026, entry version 46.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   Name=LOC106566841 {ECO:0000313|RefSeq:XP_013990775.2};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP001652741, ECO:0000313|RefSeq:XP_013990775.2};
RN   [1] {ECO:0000313|RefSeq:XP_013990775.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (AUG-2025) 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=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
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|RuleBase:RU361146};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU361146}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000256|ARBA:ARBA00006124,
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   RefSeq; XP_013990775.2; XM_014135300.2.
DR   STRING; 8030.ENSSSAP00000048688; -.
DR   PaxDb; 8030-ENSSSAP00000048688; -.
DR   GeneID; 106566841; -.
DR   Proteomes; UP001652741; Chromosome ssa13.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:UniProtKB-ARBA.
DR   GO; GO:0005886; C:plasma 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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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   GO; GO:0030165; F:PDZ domain binding; IEA:TreeGrafter.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:TreeGrafter.
DR   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 3.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
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; IPR059000; ATPase_P-type_domA.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093:SF284; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 3; 1.
DR   Pfam; PF12424; ATP_Ca_trans_C; 2.
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; PF08282; Hydrolase_3; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP001652741};
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};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        379..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        420..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        932..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        970..988
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1008..1028
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          53..129
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1214..1244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1079..1106
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        304..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1289 AA;  141616 MW;  109A87A1083AE47F CRC64;
     MGDLANSSVE FKPKKRGSGG GTEVNHAGDF GATLEDLRDL MELRGAEAIQ KIQENYTDTE
     GLCQRLKTSP ADGLSDNPSD LEKRGQVFGQ NFIPPKKAKS FLELVWEALQ DVTLIILEIA
     AIISLALSFY QPPGEESEAC GNVASGAEDE GEAEAGWIEG AAILLSVVCV VLVTAFNDWS
     KEKQFRGLQS RIEQEQRFAV VRNGTVIQIP VAEMVVGDVA QIKYGDLLPA DGILIQGNDL
     KIDESSLTGE SDHVKKSVDK DPMLLSGTHV MEGSGKMLVT AVGINSQTGI IFTLLGAGEG
     EGEDEKKDKK GKQDGTLENN QNKAKKQDEA VAMEMQPLKS AEGGEVEAEK KKGNVPKKEK
     SVLQGKLTKL AVQIGKAGLV MSAITVIILV MYFVIETFVV QGREWLTECT PVYVQYFVKF
     FIIGVTVLVV AVPEGLPLAV TISLAYSVKK MMKDNNLVRH LDACETMGNA TAICSDKTGT
     LTTNRMTVVQ AYAGDQHFHK VPHPDQMNPK VLDTLVNAIA VNSAYTSKIM PPDKEGGLPK
     QVGNKTECAL LGFILDLKRD YAPVREQIPE EKLYKVYTFN SVRKSMSTVV QLPDGSFRLY
     SKGASEILLK KCSSIMAGGG DPRGFRPRDR DEMVKKVIEP MACDGLRTIC VAYKDLPASP
     EPDWEDEAGI VSDLICITVV GIEDPVRPEV PDAIKKCQRA GITVRMVTGD NINTARAIAA
     KCGIIQPGDD FLCIDGKEFN RRIRNEKGEV EQERIDKVWP KLRVLARSSP TDKHTLVKGI
     IDSTVLEQRQ VVAVTGDGTN DGPALKKADV GFAMGIAGTD VAKEASDIIL TDDNFSSIVK
     AVMWGRNVYD SISKFLQFQL TVNVVAVIVA FTGACITQDS PLKAVQMLWV NLIMDTFASL
     ALATEPPTES LLLRKPYGRN NPLISRTMMK NILGHAIYQL TIIFTLLFAG EKIFNIDSGR
     NAPLHSPPSE HYTIIFNTFV LMQLFNEINA RKIHGERNVF DGIFHNPIFC SIVLGTFLMQ
     FVIVQFGGKP FSCTPLNVEQ WLWCLLVGVG ELLWGQLITT VPTSHLPCLK EAGHALGKEE
     MIDDDMADDE QEIDHAEREL RRGQILWFRG LNRIQTQMEV VSTFKRSGSF QGAARRRSSV
     LSQLHDIQVV KAFRSPLYDG IEKPESKNSI HDFMAHPEFL INDSVHNIPL IDETDIETEE
     SERSDCNNVR LALRQAPPLA KPPQPPSRHR SASRPAPYRQ QSLPVTLNCN NNATAAAENG
     DHLTPKDARL PAASLCRPTS PLHNVETCL
//

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