UniProt: A0A8C7EXW9

Database: UniProt
Entry: A0A8C7EXW9_NEOVI

LinkDB:  A0A8C7EXW9_NEOVI 
Original site:  A0A8C7EXW9_NEOVI

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Ontology (11)   
   GO (11)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (21)   
   InterPro (13)   
   Pfam (6)   
   PROSITE (1)   
   SMART (1)   
All databases (40)   

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ID   A0A8C7EXW9_NEOVI        Unreviewed;      1220 AA.
AC   A0A8C7EXW9;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 18.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   Name=ATP2B3 {ECO:0000313|Ensembl:ENSNVIP00000031182.1};
OS   Neovison vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Neogale.
OX   NCBI_TaxID=452646 {ECO:0000313|Ensembl:ENSNVIP00000031182.1, ECO:0000313|Proteomes:UP000694425};
RN   [1] {ECO:0000313|Ensembl:ENSNVIP00000031182.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSNVIP00000031182.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_044091186.1; XM_044235251.1.
DR   RefSeq; XP_044091187.1; XM_044235252.1.
DR   AlphaFoldDB; A0A8C7EXW9; -.
DR   Ensembl; ENSNVIT00000036120.1; ENSNVIP00000031182.1; ENSNVIG00000023990.1.
DR   GeneID; 122897099; -.
DR   KEGG; nvs:122897099; -.
DR   CTD; 492; -.
DR   GeneTree; ENSGT00940000160765; -.
DR   Proteomes; UP000694425; Unplaced.
DR   GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
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:1905056; F:P-type calcium transporter activity involved in regulation of presynaptic cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0030165; F:PDZ domain binding; IEA:TreeGrafter.
DR   GO; GO:1990034; P:calcium ion export across plasma membrane; IEA:Ensembl.
DR   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR   FunFam; 1.20.1110.10:FF:000001; Calcium-transporting ATPase; 1.
DR   FunFam; 1.20.1110.10:FF:000002; Calcium-transporting ATPase; 1.
DR   FunFam; 1.20.1110.10:FF:000008; Calcium-transporting ATPase; 1.
DR   FunFam; 2.70.150.10:FF:000001; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.1110.10:FF:000032; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.50.1000:FF:000007; Calcium-transporting ATPase; 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; 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; 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:UP000694425};
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        376..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        417..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        852..873
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        929..951
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        971..988
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1000..1025
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          50..126
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1166..1220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1076..1103
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1194..1209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1220 AA;  134071 MW;  6BB61A8285AFE738 CRC64;
     MGDLANSSIE FHPKPQQQRE APQAGGFGCT LAELRSLMEL RGAEALQKVQ EAYGDVSGLC
     RRLKTSPTEG LANNASDLEK RRQIYGQNFI PPKQPKTFLQ LVWEALQDVT LIILEVAAVV
     SLGLSFYAPP GEESEACGNV SAGAEDEGEA EAGWIEGAAI LLSVSCVVLV TAFNDWSKER
     QFRGLQSRIE QEQRFSVIRD GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQGNDLKID
     ESALTGESDH VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEE
     KKDKKGKQQD GAMESSQTKA KKQDGAVAME MQPLKSAEGG EMEEREKKKA SVPKKEKSVL
     QGKLTKLAVQ IGKAGLVMSA ITVIILVLYF VIETFVVDGR AWLAECTPVY VQYFVKFFII
     GVTVLVVAVP EGLPLAVTIS LAYSVKKMMR DNNLVRHLDA CETMGNATAI CSDKTGTLTT
     NRMTVVQSYL GDTHYKEVPA PSTLTPKILD LLVHAISINS AYTTKILPPE KEGALPRQVG
     NKTECALLGF VLDLKRDFQP VREQIPEDKL YKVYTFNSVR KSMSTVIRMP DGGFRLFSKG
     ASEILLKKCT NILNSNGELR GFRPRDRDDM VKKIIEPMAC DGLRTICIAY RDFSATQEPD
     WDNENEVVGD LTCIAVVGIE DPVRPEVPEA IRKCQRAGIT VRMVTGDNIN TARAIAAKCG
     IIQPGEDFLC LEGKEFNRRI RNEKGEIEQE RLDKVWPKLR VLARSSPTDK HTLVKGIIDS
     NTGEQRQVVA VTGDGTNDGP ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM
     WGRNVYDSIS KFLQFQLTVN VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA
     TEPPTEALLL RKPYGRDKPL ISRTMMKNIL GHAVYQLAII FTLLFVGELF FDIDSGRNAP
     LHSPPSEHYT IIFNTFVMMQ LFNEINARKI HGERNVFHGI FSNPIFCTIV LGTFAIQIVI
     VQFGGKPFSC SPLSTEQWLW CLFVGVGELV WGQVIATIPT SQLTCLKEAG HGPGKDEMTD
     EELAEGEEEI DHAERELRRG QILWFRGLNR IQTQIRVVKA FRSSLYEGLE KPESKTSIHN
     FMATPEFLIN DYTHNIPLID DTDVDENEER LRAPPPPAPN QNNNAIDSGI YLTTHGTKSA
     TSSAFSSRPG SPLHSVETSL
//

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