ID Q6DCT8_XENLA Unreviewed; 1208 AA.
AC Q6DCT8;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=atp2b2.L {ECO:0000313|Xenbase:XB-GENE-960661};
GN Synonyms=atp2b2 {ECO:0000313|RefSeq:NP_001087020.1}, atp2b3
GN {ECO:0000313|RefSeq:NP_001087020.1}, atp2b3-prov
GN {ECO:0000313|EMBL:AAH77905.1}, atp2b4
GN {ECO:0000313|RefSeq:NP_001087020.1,
GN ECO:0000313|Xenbase:XB-GENE-960661}, atp2b4.L
GN {ECO:0000313|RefSeq:NP_001087020.1,
GN ECO:0000313|Xenbase:XB-GENE-960661}, atp2b4.S
GN {ECO:0000313|RefSeq:NP_001087020.1}, mxra1
GN {ECO:0000313|RefSeq:NP_001087020.1}, pmca4
GN {ECO:0000313|RefSeq:NP_001087020.1}, pmca4b
GN {ECO:0000313|RefSeq:NP_001087020.1}, pmca4x
GN {ECO:0000313|RefSeq:NP_001087020.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH77905.1};
RN [1] {ECO:0000313|RefSeq:NP_001087020.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH77905.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000313|EMBL:AAH77905.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001087020.1}
RP IDENTIFICATION.
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 EMBL; BC077905; AAH77905.1; -; mRNA.
DR RefSeq; NP_001087020.1; NM_001093551.1.
DR DNASU; 446855; -.
DR GeneID; 446855; -.
DR KEGG; xla:446855; -.
DR AGR; Xenbase:XB-GENE-960661; -.
DR CTD; 446855; -.
DR Xenbase; XB-GENE-960661; atp2b2.L.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 446855; Expressed in brain and 8 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 2: Evidence at transcript level;
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:UP000186698};
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 405..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 446..472
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 TRANSMEM 1066..1087
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 296..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1098..1125
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 366..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 132588 MW; 787E93DCDC181D1C CRC64;
MGDMSNSDFY SKNQRNEANH AADFGCDLME LRSLMELRGS EAVVKIKECY GDTDGLCKRL
KTSPTEGLPG TVADLEKRRE IFGQNFIPPK KPKTFLQLVW EALQDVTLII LEIAAIISLG
LSFYRPPGGE TEGCGGTAAG AEDEGEAEAG WIEGAAILLS VVCVVLVTAF NDWSKEKQFR
GLQSRIEQEQ KFTVVRGSQV IQIPVAEMVV GDIAQVKYGD LLPTDGIFIQ GNDLKIDESS
LTGESDQVRK SIDKDPMLLS GTHVMEGSGR MLVTAVGVNS QTGIIFTLLG ASEVEDEKKD
KKVGSTHPPS HPPAATDGAA GANAIDNANA SLVNGKMQDG NVESIQNKAK QQDGAAAMEM
QPLKSAEGGD GDDKDKKKSN PHKKEKSVLQ GKLTKLAVQI GKAGLVMSAI TVIILVLYFA
IDTFVVNKRQ WLPECTPIYI QYFVKFFIIG VTVLVVAVPE GLPLAVTISL AYSVKKMMKD
NNLVRHLDAC ETMGNATAIC SDKTGTLTTN RMTVVQAFVG DAHYKEIPDP DGLPAKTLDV
LVHAIAINSA YTSKVLPAEK DGGLPRQVGN KTECGLLGFV LDLKRDYQVV RNKIPEEKLY
KVYTFNSVRK SMSTVVKLDD GSFRMYSKGA SEIILKKCSR ILNEAGEPRI FRPRDRDEMV
KSVIEPMACD GLRTICIAYR DFPMSPEPEW DNENDIVTDL TCLAVVGIED PVRPEVPEAI
RKCQRAGITV RMVTGDNINT ARAIAIKCGI IHPGEDFLCI DGKEFNRRIH NEKGEIEQER
IDKIWPKLRV LARSSPTDKH TLVKGIIDST QVEQRQVVAV TGDGTNDGPA LKKADVGFAM
GIAGTDVAKE ASDIILTDDN FSSIVKAVMW GRNVYDSISK FLQFQLTVNV VAVIVAFTGA
CITQDSPLKA VQMLWVNLIM DTFASLALAT EPPTESLLLR KPYGRNKPLI SRTMMKNILG
HAVYQLTLIF TLLFAGETMF NIDSGRNAPL HSPPSEHYTI IFNTFVMMQL FNEINARKIH
GERNVFDGIF RNPIFCTIVL GTFAIQIVIV QFGGKPFSCS PLQLDQWMWC IFLGFGELVW
GQVISSVPTS RLKFLRGAGN LTQKEENQEE ELNEDAEEID HAERELRRGQ ILWFRGLNRI
QTQIEVVNTF KSGASFQGAL RRQSSTTSQN QDVTNISSPS HVSLSNALSS PTSTSAAAAG
HPRREGIP
//
