ID A0A6I8REL0_XENTR Unreviewed; 1257 AA.
AC A0A6I8REL0;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, 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|RefSeq:XP_002934276.2,
GN ECO:0000313|RefSeq:XP_031756962.1,
GN ECO:0000313|Xenbase:XB-GENE-960658};
GN Synonyms=atp2b4 {ECO:0000313|Ensembl:ENSXETP00000083392,
GN ECO:0000313|Xenbase:XB-GENE-960658};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000083392};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000083392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000083392};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000083392}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2020) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_002934276.2, ECO:0000313|RefSeq:XP_031756962.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002934276.2,
RC ECO:0000313|RefSeq:XP_031756962.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002934276.2,
RC ECO:0000313|RefSeq:XP_031756962.1};
RG RefSeq;
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 RefSeq; XP_002934276.2; XM_002934230.5.
DR RefSeq; XP_031756962.1; XM_031901102.1.
DR Ensembl; ENSXETT00000090853; ENSXETP00000083392; ENSXETG00000003618.
DR GeneID; 100487776; -.
DR KEGG; xtr:100487776; -.
DR CTD; 491; -.
DR Xenbase; XB-GENE-960658; atp2b2.
DR OMA; IQHCKRA; -.
DR OrthoDB; 847at2759; -.
DR Reactome; R-XTR-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-XTR-5578775; Ion homeostasis.
DR Reactome; R-XTR-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000008143; Chromosome 4.
DR Bgee; ENSXETG00000003618; Expressed in brain and 3 other cell types or tissues.
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; 2.
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; 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; 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 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:UP000008143};
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 416..437
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 457..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 969..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1007..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1077..1098
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 47..123
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 295..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 138424 MW; 2B03982C76E0BF91 CRC64;
MGDMSNSDFY SKNQRNEANH AADYGCTLME LRSLMELRGT EAVVKIKECY ADTDGLCRRL
KTSPTEGLPG TAADLEKRRQ TFGQNFIPPK KPKTFLQLVW EALQDVTLII LEIAAIISLG
LSFYRPPGGE TEGCGGAAAG AEDEGEAEAG WIEGAAILLS VVCVVLVTAF NDWSKEKQFR
GLQSRIEQEQ KFTVVRGSQV IQIPVAEMVV GDIAQVKYGD LLPTDGIFIQ GNDLKIDESS
LTGESDQVRK SVDKDPMLLS GTHVMEGSGR MLVTAVGVNS QTGIIFTLLG ASEAEDEKKD
KKGVKKEEGP QLQVGSTHPP SHPPAATDGA AGANAIDNAN ASLVNGKMQD GNVESIQNKA
KQQDGAAAME MQPLKSAEGG DGDDKDKKKS NPHKKEKSVL QGKLTKLAVQ IGKAGLVMSA
ITVIILVLYF AIDTFVVNKR QWLPECTPIY IQYFVKFFII GVTVLVVAVP EGLPLAVTIS
LAYSVKKMMK DNNLVRHLDA CETMGNATAI CSDKTGTLTT NRMTVVQAFV GDVHYKEIPD
PDGLPAKTLD VLVHAIAINS AYTSKVLPAE KDGGLPRQVG NKTECGLLGF VLDLKRDYQV
VRNKIPEEKL YKVYTFNSVR KSMSTVVKLE DGSYRMYSKG ASEIVLKKCS RTLNEAGEPR
IFRPRDRDDM VKNVIEPMAC DGLRTICIAY RDFPMSPEPD WDNENDIVTD LTCLAVVGIE
DPVRPEVPEA IRKCQRAGIT VRMVTGDNIN TARAIAIKCG IIHPGEDFLC IEGKEFNRRI
RNEKGEIEQE RIDKIWPKLR VLARSSPTDK HTLVKGIIDS TQVEQRQVVA VTGDGTNDGP
ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM WGRNVYDSIS KFLQFQLTVN
VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA TEPPTESLLL RKPYGRNKPL
ISRTMMKNIL GHAVYQLTLI FTLLFVGEDL FNIDSGRNAP LHSPPSEHYT IIFNTFVMMQ
LFNEINARKI HGERNVFDGI FRNPIFCTIV LGTFAIQIVI VQFGGKPFSC SPLQLDQWMW
CIFLGFGELV WGQVITSIPT SRLKFLKGAG HLTQKEEIPE EELNEDVEEI DHAERELRRG
QILWFRGLNR IQTQIRVVKA FRSSLYEGLE KPDSRTSIHN FMTHPEFKIE DSQPHIPLID
DTDLEEDPAL KQNSSQPPSP NKNNNAIDSG INLTTDTSKS ATSSSPGSPI HSLETSL
//
