UniProt: A0A9J8BBQ6

Database: UniProt
Entry: A0A9J8BBQ6_CYPCA

LinkDB:  A0A9J8BBQ6_CYPCA 
Original site:  A0A9J8BBQ6_CYPCA

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (21)   
   InterPro (13)   
   Pfam (6)   
   PROSITE (1)   
   SMART (1)   
All databases (33)   

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ID   A0A9J8BBQ6_CYPCA        Unreviewed;      1175 AA.
AC   A0A9J8BBQ6;
DT   28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2023, sequence version 1.
DT   28-JAN-2026, entry version 13.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS   Cyprinus carpio carpio.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000154033.1, ECO:0000313|Proteomes:UP001108240};
RN   [1] {ECO:0000313|Ensembl:ENSCCRP00000154033.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSCCRP00000154033.1}
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; A0A9J8BBQ6; -.
DR   Ensembl; ENSCCRT00000149703.1; ENSCCRP00000154033.1; ENSCCRG00000040699.2.
DR   GeneTree; ENSGT00940000165254; -.
DR   Proteomes; UP001108240; Unplaced.
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   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:000002; 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   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:UP001108240};
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        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        928..946
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        966..984
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1004..1024
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          334..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1175 AA;  129344 MW;  3849F089ACF2B513 CRC64;
     MGDLGNSTVD FHPKKPGMDK EGHEGDFGVT VEELCSLMEL RGAEALQKIQ ENYTDTETLC
     HRLKTSPADG LSDNPADLEK RRQVFGMNFI PPKKPKTFLQ LVWEALQDVT LIILEIAAII
     SLGLSFYQPP GGEIEACGNV SSGAEDEGEA EAGWIEGAAI LLSVFCVVLV TAFNDWSKEK
     QFRGLQSRIE QEQRFAVVRN GTVIQIPVAE MVVGDIAQIK YGDLLPADGV LIQGNDLKID
     ESSLTGESDH VSKSIDKDPM LLSGTHVMEG SGKMLVTAVG VNSQTGIIFT LLGAGEVEEE
     KKDCKKGWHL TNYPDTKCLM KQDEAVAMEM QPLKSAEGGE VEEKEKKKTS VPKKEKSVLQ
     GKLTKLAVQI GKAGLVMSAI TVIILMLYFV IETFVIQGRV WLTECTPIYV QYFVKFFIIG
     VTVLVVAVPE GLPLAVTISL AYSVKKMMKD NNLVRHLDAC ETMGNATAIC SDKTGTLTTN
     RMTVVQIYVG DQLFPDIPRP DQINPKTLEL MTSAIAVNCA YTSKIMAADK EGGLPKQVGN
     KTECALLGLV LGLKQDYQAV REQIPEEKLY KVYTFNSVRK SMSTVLQMPD GSFRLYSKGA
     SEILLRKCSF ILGRDDEARA FRARDKDEMV KKVIEPMACD GLRTICIAYR ELPADPMPDW
     ENETDIVSNL TCITVVGIED PVRPEVPEAI RKCQRAGITV RMVTGDNINT ARAIAAKCGI
     IHPGDDFLCI EGKEFNRRIR NEKGEIEQER IDKIWPKLRV LARSSPTDKH TLVKGIIDST
     TAEQRQVVAV TGDGTNDGPA LKKADVGFAM GIAGTDVAKE ASDIILTDDN FSSIVKAVMW
     GRNVYDSISK FLQFQLTVNV VAVIVAFTGA CITQDSPLKA VQMLWVNLIM DTLASLALAT
     EPPNEALLLR KPYGRNNPLI SRTMMKNILG HAVYQLTIIF TLLFVGEKIF DIDSGRNAPL
     HAPPSEHYTI IFNTFVLMQL FNEINARKIH GERNVFDGIF SNPIFCSIVL GTFAIQIVIV
     QFGGKPFSCS PLNAEQWLWC LFVGMGELIW GQVISSVPTH QLKCLREAGH GPAPDEIMDE
     DLADDEDEID HAERELRRGQ ILWFRGLNRI QTQMEVVSTF KRSGSFQGAV RRRSSVLSQL
     HDVTNNSTPS HVVLSTANAT GAPGSESLHS VNGTS
//

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