ID A0A3Q1BK38_AMPOC Unreviewed; 1143 AA.
AC A0A3Q1BK38;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000013953.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000013953.1}
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|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, 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|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; A0A3Q1BK38; -.
DR Ensembl; ENSAOCT00000022176.1; ENSAOCP00000013953.1; ENSAOCG00000018660.1.
DR GeneTree; ENSGT00940000165254; -.
DR OMA; QPNSIVM; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
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; 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; 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; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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 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};
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:UP000257160};
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 369..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 410..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 922..940
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 960..978
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 998..1018
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1030..1051
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 59..133
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1069..1096
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 330..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1143 AA; 125306 MW; 898A84E33B78208D CRC64;
MGEMANSAVE FYPKGTRGGG GGGRADGSHA GGDFGVTVTE LRELMELRGA DAIQKVQDSY
GGTDGLCQRL QSSITDGLSG DPADLERRGQ TYGQNFIPPK KPKTFLELVW EALQDVTLII
LEAAAIISLG LSFYQPPGKE TESCGNVSGG AEDEGEADAG WIEGAAILLS VVCVVLVTAF
NDWSKEKQFR GLQSRIEQEQ KFTVVRKGNV IQIPVADMVV GDLAQVKYGD LLPADGILIQ
GNDLKIDESS LTGESDHVRK SVEKDPMLLS GTHVMEGSGR MLVTAVGVNS QTGIIFTLLG
AGEVEEDGKE KKAKKQDGGV AMEMQPLKSA EGGEVEDREK KKTNVPKKEK SVLQGKLTKL
AVQIGKAGLV MSAITVIILV LYFVINTFVV EGRTWMTECT PVYIQYFVKF FIIGVTVLVV
AVPEGLPLAV TISLAYSVKK MMKDNNLVRH LDACETMGNA TAICSDKTGT LTTNRMTVVQ
TYVGDVHHRV IPDPGQINPR TLDLLVNAIA INSAYTSKIL PPDVEGGLAK QVGNKTECGL
LGFVLDLQQD YAPVRDQIPE ERLYKVYTFN SVRKSMSTVI KLPDGSFRLY SKGASEIMLK
KCSYILDANG EARSFRPRDR DEMVKQVIEP MACEGLRTIC IAYRDLPSNP EPDWENEAEI
VTELTCITVV GIEDPVRPEV PEAIRKCQRA GITVRMVTGD NINTARAIAA KCGIIHPGDD
FICLEGKDFN RRIRNEKGEI EQERIDKIWP KLRVLARSSP TDKHTLVKGI IDSSVVEQRQ
VVAVTGDGTN DGPALKKADV GFAMGIAGTD VAKEASDIIL TDDNFSSIVK AVMWGRNVYD
SISKFLQFQL TVNVVAVIVA FTGACITQDS PLKAVQMLWV NLIMDTFASL ALATEPPTEA
LLLRKPYGRN NPLISLTMMK NILGHGVYQL VIIFTLLFIG ERMFNIDSGR NAPLHSPPSE
HYTIIFNTFV LMQLFNEINA RKIHGERNVF DGIFSNPIFC SIVLGTFAVQ IVIVQWGGKP
FSCAPLNVEQ WLWCLFVGVG ELLWGQVIAT VPTERLPCLK EAGLGLEPSE EEGEELAEDE
EEIDCAEREL RRGQILWFRG LNRIQTQVHW TSETNRNQNS LTGTHTETQQ PEASLSHDSQ
ALC
//
