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Plasma membrane calcium-transporting ATPase 4 (PMCA4) (EC 3.6.3.8) (Matrix-remodeling-associated protein 1) (Plasma membrane calcium ATPase isoform 4) (Plasma membrane calcium pump isoform 4)

 AT2B4_HUMAN             Reviewed;        1241 AA.
P23634; B1APW5; B1APW6; Q13450; Q13452; Q13455; Q16817; Q7Z3S1;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
22-NOV-2017, entry version 189.
RecName: Full=Plasma membrane calcium-transporting ATPase 4 {ECO:0000305};
Short=PMCA4 {ECO:0000303|PubMed:1531651, ECO:0000312|EMBL:AAA50819.1};
EC=3.6.3.8 {ECO:0000269|PubMed:8530416};
AltName: Full=Matrix-remodeling-associated protein 1;
AltName: Full=Plasma membrane calcium ATPase isoform 4;
AltName: Full=Plasma membrane calcium pump isoform 4;
Name=ATP2B4 {ECO:0000312|HGNC:HGNC:817}; Synonyms=ATP2B2, MXRA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM XB), PARTIAL PROTEIN SEQUENCE, AND
SUBCELLULAR LOCATION.
TISSUE=Erythrocyte;
PubMed=2137451;
Strehler E.E., James P., Fischer R., Heim R., Vorherr T.E.,
Filoteo A.G., Penniston J.T., Carafoli E.;
"Peptide sequence analysis and molecular cloning reveal two calcium
pump isoforms in the human erythrocyte membrane.";
J. Biol. Chem. 265:2835-2842(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM XA), AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=1531651;
Brandt P., Neve R.L., Kammesheidt A., Rhoads R.E., Vanaman T.C.;
"Analysis of the tissue-specific distribution of mRNAs encoding the
plasma membrane calcium-pumping ATPases and characterization of an
alternately spliced form of PMCA4 at the cDNA and genomic levels.";
J. Biol. Chem. 267:4376-4385(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM XB).
TISSUE=Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM XA).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XA; XB; XK; ZA; ZB AND
ZK).
TISSUE=Heart muscle;
PubMed=8700162; DOI=10.1007/BF00229314;
Santiago-Garcia J., Mas-Oliva J., Saavedra D., Zarain-Herzberg A.;
"Analysis of mRNA expression and cloning of a novel plasma membrane
Ca(2+)-ATPase splice variant in human heart.";
Mol. Cell. Biochem. 155:173-182(1996).
[8]
PROTEIN SEQUENCE OF 1085-1153 (ISOFORMS XB/ZB), AND CALMODULIN-BINDING
SUBDOMAIN A.
PubMed=2963820;
James P., Maeda M., Fischer R., Verma A.K., Krebs J., Penniston J.T.,
Carafoli E.;
"Identification and primary structure of a calmodulin binding domain
of the Ca2+ pump of human erythrocytes.";
J. Biol. Chem. 263:2905-2910(1988).
[9]
PROTEIN SEQUENCE OF 1177-1190.
PubMed=2966397; DOI=10.1073/pnas.85.9.2914;
Brandt P., Zurini M., Neve R.L., Rhoads R.E., Vanaman T.C.;
"A C-terminal, calmodulin-like regulatory domain from the plasma
membrane Ca2+-pumping ATPase.";
Proc. Natl. Acad. Sci. U.S.A. 85:2914-2918(1988).
[10]
ALTERNATIVE SPLICING (ISOFORMS X AND Z).
TISSUE=Heart;
PubMed=8245032;
Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.;
"Quantitative analysis of alternative splicing options of human plasma
membrane calcium pump genes.";
J. Biol. Chem. 268:25993-26003(1993).
[11]
ERRATUM.
PubMed=7989379;
Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.;
J. Biol. Chem. 269:32022-32022(1994).
[12]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND MUTAGENESIS OF
ASP-672; VAL-674; ARG-675; LYS-686 AND ARG-693.
PubMed=8530416; DOI=10.1074/jbc.270.50.30111;
Adamo H.P., Filoteo A.G., Enyedi A., Penniston J.T.;
"Mutants in the putative nucleotide-binding region of the plasma
membrane Ca(2+)-pump. A reduction in activity due to slow
dephosphorylation.";
J. Biol. Chem. 270:30111-30114(1995).
[13]
INTERACTION WITH PDZD11.
PubMed=12763866; DOI=10.1111/j.1749-6632.2003.tb07230.x;
Goellner G.M., DeMarco S.J., Strehler E.E.;
"Characterization of PISP, a novel single-PDZ protein that binds to
all plasma membrane Ca2+-ATPase b-splice variants.";
Ann. N. Y. Acad. Sci. 986:461-471(2003).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
INTERACTION WITH SLC35G1 AND STIM1.
PubMed=22084111; DOI=10.1073/pnas.1117231108;
Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.;
"POST, partner of stromal interaction molecule 1 (STIM1), targets
STIM1 to multiple transporters.";
Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-328, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
STRUCTURE BY NMR OF 1086-1104 IN COMPLEX WITH CALMODULIN.
PubMed=10493800; DOI=10.1021/bi9908235;
Elshorst B., Hennig M., Foersterling H., Diener A., Maurer M.,
Schulte P., Schwalbe H., Griesinger C., Krebs J., Schmid H.,
Vorherr T.E., Carafoli E.;
"NMR solution structure of a complex of calmodulin with a binding
peptide of the Ca(2+) pump.";
Biochemistry 38:12320-12332(1999).
-!- FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent
enzyme that catalyzes the hydrolysis of ATP coupled with the
transport of calcium out of the cell (PubMed:8530416). By
regulating sperm cell calcium homeostasis, may play a role in
sperm motility (By similarity). {ECO:0000250|UniProtKB:Q6Q477,
ECO:0000269|PubMed:8530416}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate
+ Ca(2+)(Side 2). {ECO:0000269|PubMed:8530416}.
-!- ENZYME REGULATION: Activated by calcium/calmodulin.
{ECO:0000269|PubMed:8530416}.
-!- SUBUNIT: Interacts with PDZD11 (PubMed:12763866). Interacts with
SLC35G1 and STIM1 (PubMed:22084111). Interacts with calmodulin
(PubMed:2963820, PubMed:10493800). {ECO:0000269|PubMed:10493800,
ECO:0000269|PubMed:12763866, ECO:0000269|PubMed:22084111,
ECO:0000269|PubMed:2963820}.
-!- INTERACTION:
P01258:CALCA; NbExp=2; IntAct=EBI-1174388, EBI-1018474;
Q63622:Dlg2 (xeno); NbExp=2; IntAct=EBI-1174437, EBI-396947;
Q62936:Dlg3 (xeno); NbExp=2; IntAct=EBI-1174437, EBI-349596;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2137451};
Multi-pass membrane protein {ECO:0000255}. Cell projection,
cilium, flagellum membrane {ECO:0000250|UniProtKB:Q6Q477}; Multi-
pass membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=There is a combination of two alternatively spliced
domains at N-terminal site A (X and Z) and at C-terminal site
B/C (A, B, D and K). The splice sites have mostly been studied
independently. Full isoforms so far detected are isoform XA and
isoform XB. Experimental confirmation may be lacking for some
isoforms.;
Name=XD; Synonyms=AIICIV;
IsoId=P23634-1; Sequence=Displayed;
Name=XA; Synonyms=AIICII;
IsoId=P23634-2; Sequence=VSP_000405;
Name=ZA; Synonyms=AICII;
IsoId=P23634-3; Sequence=VSP_000402, VSP_000405;
Name=XK; Synonyms=XG;
IsoId=P23634-4; Sequence=VSP_000403, VSP_000405;
Name=ZK; Synonyms=ZG;
IsoId=P23634-5; Sequence=VSP_000402, VSP_000403, VSP_000405;
Name=XB; Synonyms=AIICI, hPMCA4b;
IsoId=P23634-6; Sequence=VSP_000404;
Name=ZB; Synonyms=AICI;
IsoId=P23634-7; Sequence=VSP_000402, VSP_000404;
Name=ZD; Synonyms=AICIV;
IsoId=P23634-8; Sequence=VSP_000402;
-!- TISSUE SPECIFICITY: Isoform XB is the most abundant isoform and is
expressed ubiquitously. Isoforms containing segment Z have only
been detected in heart, while isoforms containing segment a have
been found in heart, stomach and brain cortex.
{ECO:0000269|PubMed:1531651}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIB subfamily. {ECO:0000305}.
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EMBL; M25874; AAA50819.1; -; mRNA.
EMBL; M83363; AAA36455.1; -; mRNA.
EMBL; BX537444; CAD97686.1; -; mRNA.
EMBL; U42026; AAB17577.1; -; mRNA.
EMBL; U42061; AAB17578.1; -; mRNA.
EMBL; U42062; AAB17579.1; -; mRNA.
EMBL; U42378; AAB17580.1; -; mRNA.
EMBL; AL513343; CAI17025.1; -; Genomic_DNA.
EMBL; AC114402; CAI17025.1; JOINED; Genomic_DNA.
EMBL; AL513343; CAI17026.1; -; Genomic_DNA.
EMBL; AC114402; CAI17026.1; JOINED; Genomic_DNA.
EMBL; CH471067; EAW91483.1; -; Genomic_DNA.
EMBL; CH471067; EAW91486.1; -; Genomic_DNA.
EMBL; BC140774; AAI40775.1; -; mRNA.
CCDS; CCDS1440.1; -. [P23634-6]
CCDS; CCDS30977.1; -. [P23634-2]
PIR; A35547; A35547.
RefSeq; NP_001001396.1; NM_001001396.2. [P23634-2]
RefSeq; NP_001675.3; NM_001684.4. [P23634-6]
UniGene; Hs.343522; -.
UniGene; Hs.733333; -.
PDB; 1CFF; NMR; -; B=1086-1104.
PDB; 2KNE; NMR; -; B=1086-1149.
PDBsum; 1CFF; -.
PDBsum; 2KNE; -.
ProteinModelPortal; P23634; -.
SMR; P23634; -.
BioGrid; 106983; 63.
DIP; DIP-6128N; -.
ELM; P23634; -.
IntAct; P23634; 22.
MINT; MINT-219327; -.
STRING; 9606.ENSP00000350310; -.
TCDB; 3.A.3.2.1; the p-type atpase (p-atpase) superfamily.
iPTMnet; P23634; -.
PhosphoSitePlus; P23634; -.
SwissPalm; P23634; -.
BioMuta; ATP2B4; -.
DMDM; 14286105; -.
EPD; P23634; -.
MaxQB; P23634; -.
PaxDb; P23634; -.
PeptideAtlas; P23634; -.
PRIDE; P23634; -.
DNASU; 493; -.
Ensembl; ENST00000341360; ENSP00000340930; ENSG00000058668. [P23634-2]
Ensembl; ENST00000357681; ENSP00000350310; ENSG00000058668. [P23634-6]
Ensembl; ENST00000367218; ENSP00000356187; ENSG00000058668. [P23634-2]
GeneID; 493; -.
KEGG; hsa:493; -.
UCSC; uc001gzv.4; human. [P23634-1]
CTD; 493; -.
DisGeNET; 493; -.
EuPathDB; HostDB:ENSG00000058668.14; -.
GeneCards; ATP2B4; -.
HGNC; HGNC:817; ATP2B4.
HPA; CAB016118; -.
HPA; HPA040431; -.
MIM; 108732; gene.
neXtProt; NX_P23634; -.
OpenTargets; ENSG00000058668; -.
PharmGKB; PA25110; -.
eggNOG; KOG0204; Eukaryota.
eggNOG; ENOG410XNNC; LUCA.
GeneTree; ENSGT00510000046331; -.
HOVERGEN; HBG061286; -.
InParanoid; P23634; -.
KO; K05850; -.
OMA; NAVDCNQ; -.
PhylomeDB; P23634; -.
TreeFam; TF300330; -.
Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
ChiTaRS; ATP2B4; human.
EvolutionaryTrace; P23634; -.
GeneWiki; ATP2B4; -.
GenomeRNAi; 493; -.
PRO; PR:P23634; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000058668; -.
CleanEx; HS_ATP2B2; -.
CleanEx; HS_ATP2B4; -.
ExpressionAtlas; P23634; baseline and differential.
Genevisible; P23634; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005901; C:caveola; TAS:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043234; C:protein complex; ISS:BHF-UCL.
GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
GO; GO:0097228; C:sperm principal piece; IEA:Ensembl.
GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005388; F:calcium-transporting ATPase activity; IMP:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
GO; GO:0036487; F:nitric-oxide synthase inhibitor activity; IDA:BHF-UCL.
GO; GO:0030165; F:PDZ domain binding; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0030346; F:protein phosphatase 2B binding; IDA:BHF-UCL.
GO; GO:0097110; F:scaffold protein binding; ISS:BHF-UCL.
GO; GO:1901660; P:calcium ion export; IEA:Ensembl.
GO; GO:0098703; P:calcium ion import across plasma membrane; IC:BHF-UCL.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IC:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; IMP:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:BHF-UCL.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IDA:BHF-UCL.
GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:1901205; P:negative regulation of adrenergic receptor signaling pathway involved in heart process; IDA:BHF-UCL.
GO; GO:1900082; P:negative regulation of arginine catabolic process; IDA:BHF-UCL.
GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IDA:BHF-UCL.
GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IMP:BHF-UCL.
GO; GO:1903249; P:negative regulation of citrulline biosynthetic process; IDA:BHF-UCL.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IDA:BHF-UCL.
GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; NAS:BHF-UCL.
GO; GO:0098736; P:negative regulation of the force of heart contraction; IDA:BHF-UCL.
GO; GO:0003407; P:neural retina development; IEA:Ensembl.
GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IDA:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IMP:CACAO.
GO; GO:1902305; P:regulation of sodium ion transmembrane transport; IC:BHF-UCL.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0051599; P:response to hydrostatic pressure; IMP:BHF-UCL.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
Gene3D; 3.40.1110.10; -; 1.
InterPro; IPR034304; ATP2B4.
InterPro; IPR022141; ATP_Ca_trans_C.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006408; P-type_ATPase_IIB.
InterPro; IPR001757; P_typ_ATPase.
PANTHER; PTHR24093:SF276; PTHR24093:SF276; 1.
Pfam; PF12424; ATP_Ca_trans_C; 2.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Calcium;
Calcium transport; Calmodulin-binding; Cell membrane; Cell projection;
Complete proteome; Direct protein sequencing; Hydrolase;
Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1241 Plasma membrane calcium-transporting
ATPase 4.
/FTId=PRO_0000046220.
TOPO_DOM 1 92 Cytoplasmic. {ECO:0000255}.
TRANSMEM 93 113 Helical. {ECO:0000255}.
TOPO_DOM 114 150 Extracellular. {ECO:0000255}.
TRANSMEM 151 171 Helical. {ECO:0000255}.
TOPO_DOM 172 356 Cytoplasmic. {ECO:0000255}.
TRANSMEM 357 376 Helical. {ECO:0000255}.
TOPO_DOM 377 409 Extracellular. {ECO:0000255}.
TRANSMEM 410 427 Helical. {ECO:0000255}.
TOPO_DOM 428 840 Cytoplasmic. {ECO:0000255}.
TRANSMEM 841 860 Helical. {ECO:0000255}.
TOPO_DOM 861 870 Extracellular. {ECO:0000255}.
TRANSMEM 871 891 Helical. {ECO:0000255}.
TOPO_DOM 892 911 Cytoplasmic. {ECO:0000255}.
TRANSMEM 912 934 Helical. {ECO:0000255}.
TOPO_DOM 935 952 Extracellular. {ECO:0000255}.
TRANSMEM 953 974 Helical. {ECO:0000255}.
TOPO_DOM 975 993 Cytoplasmic. {ECO:0000255}.
TRANSMEM 994 1015 Helical. {ECO:0000255}.
TOPO_DOM 1016 1025 Extracellular. {ECO:0000255}.
TRANSMEM 1026 1047 Helical. {ECO:0000255}.
TOPO_DOM 1048 1241 Cytoplasmic. {ECO:0000255}.
REGION 1086 1103 Calmodulin-binding subdomain A.
{ECO:0000269|PubMed:2963820}.
REGION 1104 1113 Calmodulin-binding subdomain B.
{ECO:0000250|UniProtKB:P20020}.
ACT_SITE 465 465 4-aspartylphosphate intermediate.
{ECO:0000250|UniProtKB:P19156}.
METAL 785 785 Magnesium. {ECO:0000250}.
METAL 789 789 Magnesium. {ECO:0000250}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1102 1102 Phosphothreonine; by PKC. {ECO:0000250}.
VAR_SEQ 301 312 Missing (in isoform ZA, isoform ZK,
isoform ZB and isoform ZD).
{ECO:0000305}.
/FTId=VSP_000402.
VAR_SEQ 1009 1044 Missing (in isoform XK and isoform ZK).
{ECO:0000305}.
/FTId=VSP_000403.
VAR_SEQ 1104 1139 Missing (in isoform XB and isoform ZB).
{ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:2137451}.
/FTId=VSP_000404.
VAR_SEQ 1140 1241 IKVVKAFHSSLHESIQKPYNQKSIHSFMTHPEFAIEEELPR
TPLLDEEEEENPDKASKFGTRVLLLDGEVTPYANTNNNAVD
CNQVQLPQSDSSLQSLETSV -> VAVAPVKSSPTTSVPAV
SSPPMGNQSGQSVP (in isoform XA, isoform
XK, isoform ZA and isoform ZK).
{ECO:0000303|PubMed:1531651,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_000405.
MUTAGEN 672 672 D->Q: Strongly decreased calcium
transport activity. Slowed decomposition
of the phosphorylated intermediate.
{ECO:0000269|PubMed:8530416}.
MUTAGEN 674 674 V->P: Decreased calcium transport
activity. {ECO:0000269|PubMed:8530416}.
MUTAGEN 675 675 R->K,D,L: Decreased calcium transport
activity. {ECO:0000269|PubMed:8530416}.
MUTAGEN 686 686 K->L: Decreased calcium transport
activity. {ECO:0000269|PubMed:8530416}.
MUTAGEN 693 693 R->I: Mildly decreased calcium transport
activity. {ECO:0000269|PubMed:8530416}.
CONFLICT 492 492 S -> C (in Ref. 3; CAD97686).
{ECO:0000305}.
CONFLICT 1144 1144 K -> N (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 1147 1147 H -> S (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 1153 1153 S -> F (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 1178 1178 L -> Q (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 1187 1187 E -> Q (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 1190 1190 E -> G (in Ref. 3; CAD97686).
{ECO:0000305}.
TURN 1087 1089 {ECO:0000244|PDB:2KNE}.
TURN 1090 1092 {ECO:0000244|PDB:1CFF}.
HELIX 1093 1102 {ECO:0000244|PDB:1CFF}.
SEQUENCE 1241 AA; 137920 MW; 568544103CD5F494 CRC64;
MTNPSDRVLP ANSMAESREG DFGCTVMELR KLMELRSRDA LTQINVHYGG VQNLCSRLKT
SPVEGLSGNP ADLEKRRQVF GHNVIPPKKP KTFLELVWEA LQDVTLIILE IAAIISLVLS
FYRPAGEENE LCGQVATTPE DENEAQAGWI EGAAILFSVI IVVLVTAFND WSKEKQFRGL
QCRIEQEQKF SIIRNGQLIQ LPVAEIVVGD IAQVKYGDLL PADGILIQGN DLKIDESSLT
GESDHVKKSL DKDPMLLSGT HVMEGSGRMV VTAVGVNSQT GIILTLLGVN EDDEGEKKKK
GKKQGVPENR NKAKTQDGVA LEIQPLNSQE GIDNEEKDKK AVKVPKKEKS VLQGKLTRLA
VQIGKAGLLM SALTVFILIL YFVIDNFVIN RRPWLPECTP IYIQYFVKFF IIGITVLVVA
VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL TMNRMTVVQA
YIGGIHYRQI PSPDVFLPKV LDLIVNGISI NSAYTSKILP PEKEGGLPRQ VGNKTECALL
GFVTDLKQDY QAVRNEVPEE KLYKVYTFNS VRKSMSTVIR NPNGGFRMYS KGASEIILRK
CNRILDRKGE AVPFKNKDRD DMVRTVIEPM ACDGLRTICI AYRDFDDTEP SWDNENEILT
ELTCIAVVGI EDPVRPEVPD AIAKCKQAGI TVRMVTGDNI NTARAIATKC GILTPGDDFL
CLEGKEFNRL IRNEKGEVEQ EKLDKIWPKL RVLARSSPTD KHTLVKGIID STVGEHRQVV
AVTGDGTNDG PALKKADVGF AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI
SKFLQFQLTV NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTESLL
KRRPYGRNKP LISRTMMKNI LGHAFYQLIV IFILVFAGEK FFDIDSGRKA PLHSPPSQHY
TIVFNTFVLM QLFNEINSRK IHGEKNVFSG IYRNIIFCSV VLGTFICQIF IVEFGGKPFS
CTSLSLSQWL WCLFIGIGEL LWGQFISAIP TRSLKFLKEA GHGTTKEEIT KDAEGLDEID
HAEMELRRGQ ILWFRGLNRI QTQIDVINTF QTGASFKGVL RRQNMGQHLD VKLVPSSSYI
KVVKAFHSSL HESIQKPYNQ KSIHSFMTHP EFAIEEELPR TPLLDEEEEE NPDKASKFGT
RVLLLDGEVT PYANTNNNAV DCNQVQLPQS DSSLQSLETS V


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