AT2B2_OREMO
ID AT2B2_OREMO Reviewed; 1112 AA.
AC P58165;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Plasma membrane calcium-transporting ATPase 2;
DE Short=PMCA2;
DE EC=7.2.2.10;
DE AltName: Full=Plasma membrane calcium ATPase isoform 2;
DE AltName: Full=Plasma membrane calcium pump isoform 2;
DE Flags: Fragment;
GN Name=atp2b2; Synonyms=pmca;
OS Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8127;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang C.-H., Leu J.-H., Chou C.-M., Hwang S.-P.L., Huang C.-J., Hwang P.-P.;
RT "Partial cDNA sequence of Mozambique tilapia (Oreochromis mossambicus)
RT plasma membrane calcium ATPase (PMCA).";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of calcium out of the cell.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000305}.
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DR EMBL; AF236669; AAK15034.1; -; mRNA.
DR AlphaFoldDB; P58165; -.
DR SMR; P58165; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030322; ATP2B2.
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 PANTHER; PTHR24093:SF377; PTHR24093:SF377; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Cell membrane;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..>1112
FT /note="Plasma membrane calcium-transporting ATPase 2"
FT /id="PRO_0000046217"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..426
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..878
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 879..888
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 889..909
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 910..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..952
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 953..970
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 971..992
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 993..1011
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1033
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1034..1043
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1044..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..>1112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 298..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..>1112
FT /note="Calmodulin-binding subdomain A"
FT /evidence="ECO:0000250"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 482
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 803
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 807
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT NON_TER 1112
SQ SEQUENCE 1112 AA; 122487 MW; 8BBECB082E58C861 CRC64;
MGDMSNSDFY AKNQRNEGNH AAAFGCSLME LRSLMELRGT EAVVKLQEDY GGVEGLCKRL
KTSPTEGLAG AQTDLDKRKE IFGKNLIPPK KPKTFLQLVW EALQDVTLII LEIAALISLG
LSFYHPPGET GGESCGAAAG GVEDEGEADA GWIEGAAILL SVVCVVLVTA FNDWSKEKQF
RGLQSRIEQE QKFQVVRGSQ VIQLPVADIL VGDIAQIKYG DLLPSDGVLI QGNDLKIDES
SLTGESDHVK KSADKDPMLL SGTHVMEGSG RMVVTAVGVN SQTGIIFTLL GAGVEEEEKK
EKKGGAVEDG HQNTGKMQDG NMESNQIKVK KQDGAAAMEM QPLKSAEGGE ADEKERKKVS
APKKEKSVLQ GKLTKLAVQI GKAGLLMSAI TVIILVLYFA IDNFVMQKRP WMPECTPIYI
QYFVKFFIIG VTVLVVAVPE GLPLAVTISL AYSVKKMMKD NNLVRHLDAC ETMGNATAIC
SDKTGTLTTN RMTAVQLYVG DVRYKEIPDP GVLPPKSLDL LVNAISINSA YTTKILPPDK
EGGLPKQVGN KTECGLLGLV LELKRDYQPI RNQIPEEKLY KVYTFNSVRK SMSTVIKLPD
GSFRMYSKGA SEIVLKKCSH ILNEVGEPRV FRPRDKDEMV KKVIEPMACD GLRTICVAYR
DFSSNPEPNW DDENNILNDL TAICVVGIED PVRPEVPNAI QKCQRAGITV RMVTGANINT
ARAIAIKCGI IHPGEDFLCI DGKEFNRRIR NEKGEVEQER IDKVWPKLRV LARSSPTDKH
TLVKGIIDST MADQRQVVAV TGDGTNDGPA LKKADVGFAM GIAGTDVAKE ASDIILTDDN
FSSIVKAVMW GRNVYDSISK FLQFQLTVNV VAVIVAFTGA CITQDSPLKA VQMLWVNLIM
DTFASLALAT EPPTESLLKR KPYGRNKPLI SSTMTKNILG HGVYQLIIIF TLLFVGEQIF
DIDSGRNAPL HSPPSEHYTI IFNTFVMMQL FNEINARKIH GERNVFDGIF RNPIFCSIVF
GTFAVQIVIV QFGGKPFSCQ PLDLEKWMWC VFLGLGELVW GQVIATIPNS RLRFLRRAGQ
LTQKDELPEE DVNEENEEID HAERELRRGQ IL
