ID A0A671TUR4_SPAAU Unreviewed; 1205 AA.
AC A0A671TUR4;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, 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:ENSSAUP00010005096.1};
OS Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010005096.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010005096.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A671TUR4; -.
DR Ensembl; ENSSAUT00010005495.1; ENSSAUP00010005096.1; ENSSAUG00010002441.1.
DR GeneTree; ENSGT00940000165254; -.
DR Proteomes; UP000472265; 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:UP000472265};
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 375..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 416..442
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 913..931
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 951..969
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 55..131
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1060..1087
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 336..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1205 AA; 132098 MW; ECC68DD2FB8938F7 CRC64;
MANSAVEFYP KGTRGGGGGG GRTDGSHAGG DFVVTVNELR ELMELRGVDA LQKVQDSYGD
TEGLCQRLQT SPTEGLSGDP ADLERRCQTF GQNFIPPKKP KTFLELVWEA LQDVTLIILE
AAAIISLGLS FYQPPGKESE SCGNVSGGAA EDEGEGDTGW IEGAAILLSV VCVVLVTAFN
DWSKEKQFRG LQSRIEQEQK FTVVRKGNVI QIPVADMVVG DLAQVKYGDL LPTDGILVQG
NDLKIDESSL TGESDHVRKS VDKDPMLLSG THVMEGSGRM LVTAVGVNSQ TGIIFTLLGA
GEMEEDGKEK KGNLPENENK KQDGGVAMEM QPLKSAEGGE VEDREKKKTS VPKKEKSVLQ
GKLTKLAVQI GKAGLVMSAI TVIILVLYFV INTFVVEGHT WLSECTPVYV QYFVKFFIIG
VTVLVVAVPE GLPLAVTISL AYSVKKMMKD NNLVRHLDAC ETMGNATAIC SDKTGTLTTN
RMTVVQTFLG DTHHRVIPDP GQLNPRTLDL LVNAIAINSA YTSKILPPDV EGGLAKQVGN
KTECGLLGFV LDLQQDYTPV REQIPEERLY KVYTFNSVRK SMSTVIKLPD GSFRLYSKGA
SEIIGIGSLM QINRGDCVIE PMACEGLRTI CIAYRDLPSN PEPDWDNEAE IVTELTCITV
VGIEDPVRPE VPDAIRKCQR AGITVRMVTG DNINTARAIA AKCGIIHPGD DFICLEGKDF
NRRIRNEKGE IEQERIDKIW PKLRVLARSS PTDKHTLVKG IIDSSVIEQR QVVAVTGDGT
NDGPALKKAD VGFAMGIAGT DVAKEASDII LTDDNFSSIV KAVMWGRNVY DSISKFLQFQ
LTVNVVAVIV AFTGACITQD SPLKAVQMLW VNLIMDTFAS LALATEPPTE DLLLRKPYGR
NNPLISLTMM KNILGHGVYQ LVIIFTLLFI GERMFNIDSG RNAPLHSPPS EHYTIIFNTF
VLMQLFNEIN ARKIHGERNV FDGIFANPIF CSIVLGTFAV QIVIVQWGGK PFSCAPLNVE
QWLWCLFVGV GELLWGQVIA TVPTERLPCL KEAGLGLEPG EEEGEELAED EEEIDCAERE
LRRGQILWFR GLNRIQTQMR VVKAFRSSLY EGREKPESRN SIHNFMAHPE FLINDLIHNI
PLIDDTDVDD ESDGQWLETS PHNSLRTLHL SLPLPLLLPS QSDPLTPPPL PASILEPTTP
SVAHP
//
