ID A0A8C5A107_GADMO Unreviewed; 1250 AA.
AC A0A8C5A107;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 3.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=atp2b2 {ECO:0000313|Ensembl:ENSGMOP00000024569.1};
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049 {ECO:0000313|Ensembl:ENSGMOP00000024569.1, ECO:0000313|Proteomes:UP000694546};
RN [1] {ECO:0000313|Ensembl:ENSGMOP00000024569.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSGMOP00000024569.1}
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 AlphaFoldDB; A0A8C5A107; -.
DR Ensembl; ENSGMOT00000077208.1; ENSGMOP00000024569.1; ENSGMOG00000003698.2.
DR GeneTree; ENSGT00940000166500; -.
DR Proteomes; UP000694546; Chromosome 13.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:TreeGrafter.
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 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; 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:SF377; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 2; 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 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:UP000694546};
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 409..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 450..476
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 885..904
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 962..980
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1000..1018
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 48..124
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 295..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 137198 MW; 22383E1F9F789FE9 CRC64;
MGDMSNSSDF YAKNQRSENN HAGGFGVSVL ELRSLMEQRA TEAVVRVQEE YGGVEGLCSR
LNTSPTEGLT SSQADLDKRR EVYGENTIPP KKPKTFLELV WEALQDVTLI ILEVAAVVSL
GLSFYRPPGD TSVDSCGAAA GGEEGEGEAG WIEGAAILLS VVCVVLVTAF NDWSKEKQFR
GLQSRIQQEQ KFQVVRDGQV VQLPVADLVV GDIAQIKYGD LLPTDGILIQ GNDLKIDESS
LTGESDHVKK DTEHDPMLLS GTHVMEGSGR MVVTAVGVNS QTGIIFTLLG AGTEEEELKE
KKDEDGLRNA DHTASHPIAT ITTDGASAGN IGNATLINGK MQDGNMEINQ TKVKKQDGAA
AMEMQPLKSA EGGEPDEKEK RKVNVSKKDK SVLQGKLTKL AVQIGKAGLL MSSITVIMLV
LTFVIDTFVV QGLPWLTECT PIYIQYFVKF FIVGVTVLVV AVPEGLPLAV TISLAYSVKK
MMKDNNLVRH LDACETMGNA TAICSDKTGT LTTNRMTAVQ CYIADVHHKV VPDPGALPPK
SLDVLMHAIS INSAYTSKIL PPDIEGGLPK QVGNKTECGL LGLVLDLKRD YQPIRKQMPE
ELLYKVYTFN SARKSMSTVV KQPDGSYRMY SKGASEIMLK KCNRILNEVG EPRVFRPRDR
DEMVKKVIEP MACEGLRTIC VAYRDFPASP EPLWDEEDLI LNDLIAVSVV GIEDPVRPEV
PDAIMKCQHA GITVRMVTGD NINTARAIAI KCGIIHPGED FLCIDGKEFN RRIRNEKGEV
EQERMDKVWP KLRVLARSSP TDKHTLVKGI IDSTMVAQRQ VVAVTGDGTN DGPALKKADV
GFAMGIAGTD VAKEASDIIL TDDNFSSIVK AVMWGRNVYD SISKFLQFQL TVNVVAVIVA
FTGACVTQDS PLKAVQMLWV NLIMDTFASL ALATEPPTES LLKRRPYGRN KPLISSTMTK
NILGHAVYQL IIIFTLLFAG EKIFDIDSGR GAPLHSPPSE HYTIIFNAFV MMQIFNEINA
RKIHGERNVF EGIFRNPIFC TIVFGTIVLQ VLIVQLGGKP FSCVALDIEK WMWCVFLGMG
ELLWGQVIST IPNSGLRFLR RAGQLSQKDE LPEDDVNDDN EEIDHAEREL RRGQILWFRG
LNRIQTQIRV VNAFRSSLYE GLEKPDSRTS IHNYMTHPEF RIDDATPHMP LIDTADLGSA
RDHLKYGSTP PSPNKNNNAI DGVVNLAVSE SQSASSSSPA SPLHSLETSL
//
