ID A0A3Q2G692_CYPVA Unreviewed; 1246 AA.
AC A0A3Q2G692;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000018825.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000018825.1}
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|RuleBase:RU361146}; Multi-
CC pass membrane protein {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 RefSeq; XP_015256072.1; XM_015400586.1.
DR AlphaFoldDB; A0A3Q2G692; -.
DR Ensembl; ENSCVAT00000027869.1; ENSCVAP00000018825.1; ENSCVAG00000022167.1.
DR GeneID; 107101601; -.
DR CTD; 491; -.
DR GeneTree; ENSGT00940000166500; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000265020; 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: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; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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 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:UP000265020};
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 403..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 446..472
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 881..902
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 958..976
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 996..1014
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1034..1054
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 49..123
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 362..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1246 AA; 137358 MW; DF87240BDCDF2D19 CRC64;
MGDMSNSDFY AKNQRKESNH AAGFGCSVME LRSLMELRGT EAVVKLQEDY GAVEGLCMRL
KTSPTEGLAG VQTDLDKRRE IFGKNLIPPK KPKTFLQLVW EALQDVTLII LEIAALISLG
LSFYHPPGQT SGEACGAAAG GVEDEGEADA GWIEGAAILL SVVCVVIVTA FNDWSKEKQF
RGLQSRIEQE QKFQVVRGSQ VIQLPVADIV VGDIAQIKYG DLLPADGVLI QGNDLKIDES
SLTGESDHVK KAADKDPMLL SGTHVMEGSG RMVVTAVGVN SQTGIIFTLL GASVEEEEKK
EKKDCSHPPI HPIATIATDG AAGINAPGTA SLINGKMQDG NMESNQIKVK KQDGAAAMEM
QPLKSAEGGE ADEKERKRVS APKKEKSVLQ GKLTKLAVQI GKAGLLMSAI TVIILVLYFA
IDNFVMEKRP WMPECTPVYI QYFVKFFIIG VTVLVVAVPE GLPLAVTISL AYSVKKMMKD
NNLVRHLDAC ETMGNATAIC SDKTGTLTTN RMTVVQCYIG DVHYKKIPDP GVIPPKTLEL
LINAIAINSA YTTKILPPDK EGGLPKQVGN KTECGLLGLI LDLKRDYQPI RNQIPEEKLY
KVYTFNSVRK SMSTVIKLTD GSFRMYSKGA SEIVLKKCSH ILNEVGEPRV FRPRDKDEMV
KKVIEPMACE GLRTICVAYR DFPRDPEPKW DDENNILSDL TAICVVGIED PVRPEVPDAI
LKCQRAGITV RMVTGDNINT ARAIAIKCGI IHPGEDFLCI DGKEFNRRIR NEKGEVEQER
IDKVWPKLRV LARSSPTDKH TLVKGIIDST MADQRQVVAV TGDGTNDGPA LKKADVGFAM
GIAGTDVAKE ASDIILTDDN FSSIVKAVMW GRNVYDSISK FLQFQLTVNV VAVIVAFTGA
CITQDSPLKA VQMLWVNLIM DTFASLALAT EPPTESLLKR KPYGRNKPLI SSTMTKNILG
HAVYQLIIIF TLLFIGEKIF DIDSGRNAPL HSPPSEHYTI IFNTFVMMQL FNEINARKIH
GERNVFEGIF RNPIFCSIVF GTFAIQIVIV QFGGKPFSCQ PLDLEKWMWC VFLGMGELVW
GQVIATIPNS NLRFLRRAGQ LTQKDELPED DVNEENEEID HAERELRRGQ ILWFRGLNRI
QTQIRVVNAF RSSLYEGLEK PDSRTSIHNF MTHPEFRIDD STPSIPLIDD TDDDSARRRT
KYSSQPSSPN KNNNAIDSGI NLTIDISKSA ASSSPASPLH SLETSL
//