Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01064
Entry Name
UniProt Accession
Theoretical PI
5.67
Molecular Weight
138559.2
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Plasma membrane calcium-transporting ATPase 3
Protein Synonyms/Alias
PMCA3; 3.6.3.8; Plasma membrane calcium ATPase isoform 3; Plasma membrane calcium pump isoform 3;
Gene Name
Atp2b3
Gene Synonyms/Alias
Pmca3;
Created Date
01-JUN-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
647
Canonical
CDGLRTICIAYRDFS
[1]
S-Palmitoylation
694
Canonical
VPEAIRKCQRAGITV
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Predicted from GPS-Lipid
Functional Description
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell.
Sequence Annotation
Topological domain: 1 97 Cytoplasmic.
Transmembrane: 98 118 Helical.
Topological domain: 119 155 Extracellular.
Transmembrane: 156 176 Helical.
Topological domain: 177 364 Cytoplasmic.
Transmembrane: 365 384 Helical.
Topological domain: 385 417 Extracellular.
Transmembrane: 418 435 Helical.
Topological domain: 436 849 Cytoplasmic.
Transmembrane: 850 869 Helical.
Topological domain: 870 879 Extracellular.
Transmembrane: 880 900 Helical.
Topological domain: 901 920 Cytoplasmic.
Transmembrane: 921 943 Helical.
Topological domain: 944 961 Extracellular.
Transmembrane: 962 983 Helical.
Topological domain: 984 1002 Cytoplasmic.
Transmembrane: 1003 1024 Helical.
Topological domain: 1025 1034 Extracellular.
Transmembrane: 1035 1056 Helical.
Topological domain: 1057 1258 Cytoplasmic.
Region: 1097 1114 Calmodulin-binding subdomain A.
Region: 1115 1124 Calmodulin-binding subdomain B.
Active site: 473 473 4-aspartylphosphate intermediate.
Metal binding site: 794 794 Magnesium.
Metal binding site: 798 798 Magnesium.
Modified residue: 1113 1113 Phosphothreonine; by PKC.
Protein Length
1258 AA.
Protein Sequence
(Canonical)
MGDMANSSIE FHPKPQQQRE VPHVGGFGCT LAELRSLMEL RGAEALQKIQ EAYGDVSGLC  60
RRLKTSPTEG LADNTNDLEK RRQIYGQNFI PPKQPKTFLQ LVWEALQDVT LIILEVAAIV  120
SLGLSFYAPP GEESEACGNV SGGAEDEGEA EAGWIEGAAI LLSVICVVLV TAFNDWSKEK  180
QFRGLQSRIE QEQKFTVIRN GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQGNDLKID  240
ESSLTGESDH VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEE  300
KKDKKGKQQD GAMESSQTKA KKQDGAVAME MQPLKSAEGG EMEEREKKKA NVPKKEKSVL  360
QGKLTKLAVQ IGKAGLVMSA ITVIILVLYF VIETFVVDGR VWLAECTPVY VQYFVKFFII  420
GVTVLVVAVP EGLPLAVTIS LAYSVKKMMK DNNLVRHLDA CETMGNATAI CSDKTGTLTT  480
NRMTVVQSYL GDTHYKEIPA PSALTPKILD LLVHAISINS AYTTKILPPE KEGALPRQVG  540
NKTECALLGF ILDLKRDFQP VREQIPEDQL YKVYTFNSVR KSMSTVIRMP DGGFRLFSKG  600
ASEILLKKCT NILNSNGELR GFRPRDRDDM VKKIIEPMAC DGLRTICIAY RDFSAIQEPD  660
WDNENEVVGD LTCIAVVGIE DPVRPEVPEA IRKCQRAGIT VRMVTGDNIN TARAIAAKCG  720
IIQPGEDFLC LEGKEFNRRI RNEKGEIEQE RLDKVWPKLR VLARSSPTDK HTLVKGIIDS  780
TTGEQRQVVA VTGDGTNDGP ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM  840
WGRNVYDSIS KFLQFQLTVN VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA  900
TEPPTESLLL RKPYGRDKPL ISRTMMKNIL GHAVYQLTII FTLLFVGELF FDIDSGRNAP  960
LHSPPSEHYT IIFNTFVMMQ LFNEINARKI HGERNVFDGI FSNPIFCTIV LGTFGIQIVI  1020
VQFGGKPFSC SPLSTEQWLW CLFVGVGELV WGQVIATIPT SQLKCLKEAG HGPGKDEMTD  1080
EELAEGEEEI DHAERELRRG QILWFRGLNR IQTQMEVVST FKRSGSFQGA VRRRSSVLSQ  1140
LHDVTNLSTP THIRVVKAFR SSLYEGLEKP ESKSCIHNFM ATPEFLINDY THNIPLIDDT  1200
DVDENEERLR APPPPPPNQN NNAIDSGIYL TTHATKSATS SAFSSRPGSP LHSMETSL    1258
FASTA
(Canonical)
>LipidDB-10116-01064|Q64568
MGDMANSSIEFHPKPQQQREVPHVGGFGCTLAELRSLMELRGAEALQKIQEAYGDVSGLC
RRLKTSPTEGLADNTNDLEKRRQIYGQNFIPPKQPKTFLQLVWEALQDVTLIILEVAAIV
SLGLSFYAPPGEESEACGNVSGGAEDEGEAEAGWIEGAAILLSVICVVLVTAFNDWSKEK
QFRGLQSRIEQEQKFTVIRNGQLLQVPVAALVVGDIAQVKYGDLLPADGVLIQGNDLKID
ESSLTGESDHVRKSADKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEE
KKDKKGKQQDGAMESSQTKAKKQDGAVAMEMQPLKSAEGGEMEEREKKKANVPKKEKSVL
QGKLTKLAVQIGKAGLVMSAITVIILVLYFVIETFVVDGRVWLAECTPVYVQYFVKFFII
GVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTT
NRMTVVQSYLGDTHYKEIPAPSALTPKILDLLVHAISINSAYTTKILPPEKEGALPRQVG
NKTECALLGFILDLKRDFQPVREQIPEDQLYKVYTFNSVRKSMSTVIRMPDGGFRLFSKG
ASEILLKKCTNILNSNGELRGFRPRDRDDMVKKIIEPMACDGLRTICIAYRDFSAIQEPD
WDNENEVVGDLTCIAVVGIEDPVRPEVPEAIRKCQRAGITVRMVTGDNINTARAIAAKCG
IIQPGEDFLCLEGKEFNRRIRNEKGEIEQERLDKVWPKLRVLARSSPTDKHTLVKGIIDS
TTGEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVM
WGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALA
TEPPTESLLLRKPYGRDKPLISRTMMKNILGHAVYQLTIIFTLLFVGELFFDIDSGRNAP
LHSPPSEHYTIIFNTFVMMQLFNEINARKIHGERNVFDGIFSNPIFCTIVLGTFGIQIVI
VQFGGKPFSCSPLSTEQWLWCLFVGVGELVWGQVIATIPTSQLKCLKEAGHGPGKDEMTD
EELAEGEEEIDHAERELRRGQILWFRGLNRIQTQMEVVSTFKRSGSFQGAVRRRSSVLSQ
LHDVTNLSTPTHIRVVKAFRSSLYEGLEKPESKSCIHNFMATPEFLINDYTHNIPLIDDT
DVDENEERLRAPPPPPPNQNNNAIDSGIYLTTHATKSATSSAFSSRPGSPLHSMETSL
Gene Ontology
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0045121; C:membrane raft; IDA:RGD
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0005388; F:calcium-transporting ATPase activity; IEA:UniProtKB-EC
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0030165; F:PDZ domain binding; IPI:RGD
GO:0007420; P:brain development; IEP:RGD
GO:0003407; P:neural retina development; IEP:RGD
Interpro
InterPro; IPR022141; ATP_Ca_trans_C
InterPro; IPR006408; ATPase_P-typ_Ca-transp_plasma
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N
InterPro; IPR023299; ATPase_P-typ_cyto_domN
InterPro; IPR018303; ATPase_P-typ_P_site
InterPro; IPR023298; ATPase_P-typ_TM_dom
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A
InterPro; IPR001757; Cation_transp_P_typ_ATPase
InterPro; IPR023214; HAD-like_dom
Pfam
Pfam; PF12424; ATP_Ca_trans_C;
Pfam; PF00689; Cation_ATPase_C;
Pfam; PF00690; Cation_ATPase_N;
Pfam; PF00122; E1-E2_ATPase;
Pfam; PF00702; Hydrolase;
SMART
SMART; SM00831; Cation_ATPase_N;
PROSITE
PROSITE; PS00154; ATPASE_E1_E2;
PRINTS
PRINTS; PR00119; CATATPASE;