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Plasma membrane calcium-transporting ATPase 4 (PMCA4) (EC 3.6.3.8) (Plasma membrane calcium ATPase isoform 4) (Plasma membrane calcium pump isoform 4)

 AT2B4_RAT               Reviewed;        1203 AA.
Q64542; Q63127; Q63445; Q64543; Q64544; Q64545;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 169.
RecName: Full=Plasma membrane calcium-transporting ATPase 4 {ECO:0000305};
Short=PMCA4 {ECO:0000303|PubMed:7702574, ECO:0000303|PubMed:7945253};
EC=3.6.3.8 {ECO:0000250|UniProtKB:P23634};
AltName: Full=Plasma membrane calcium ATPase isoform 4 {ECO:0000303|PubMed:7702574};
AltName: Full=Plasma membrane calcium pump isoform 4 {ECO:0000303|PubMed:7945253};
Name=Atp2b4 {ECO:0000312|RGD:621305};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XB; ZB; XA AND ZA), AND TISSUE
SPECIFICITY.
STRAIN=CD Charles River; TISSUE=Testis;
PubMed=7702574; DOI=10.1042/bj3060779;
Keeton T.P., Shull G.E.;
"Primary structure of rat plasma membrane Ca(2+)-ATPase isoform 4 and
analysis of alternative splicing patterns at splice site A.";
Biochem. J. 306:779-785(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 266-455 (ISOFORMS XA/XB).
TISSUE=Lung;
PubMed=7945253; DOI=10.1042/bj3030275;
Howard A., Barley N.F., Legon S., Walters J.R.F.;
"Plasma-membrane calcium-pump isoforms in human and rat liver.";
Biochem. J. 303:275-279(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1081-1203, ALTERNATIVE SPLICING
(ISOFORMS XA/ZA), AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=8428948;
Keeton T.P., Burk S.E., Shull G.E.;
"Alternative splicing of exons encoding the calmodulin-binding domains
and C termini of plasma membrane Ca(2+)-ATPase isoforms 1, 2, 3, and
4.";
J. Biol. Chem. 268:2740-2748(1993).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-334; SER-1064
AND SER-1070, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1115 AND
SER-1126 (ISOFORM XA), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
SER-1103 AND SER-1114 (ISOFORM ZA), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent
enzyme that catalyzes the hydrolysis of ATP coupled with the
transport of calcium out of the cell (By similarity). By
regulating sperm cell calcium homeostasis, may play a role in
sperm motility (By similarity). {ECO:0000250|UniProtKB:P23634,
ECO:0000250|UniProtKB:Q6Q477}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) +
phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.3.8;
Evidence={ECO:0000250|UniProtKB:P23634};
-!- ACTIVITY REGULATION: Activated by calcium/calmodulin.
{ECO:0000250|UniProtKB:P23634}.
-!- SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1.
Interacts with calmodulin. {ECO:0000250|UniProtKB:P23634}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P23634}; 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=4;
Comment=There is a combination of two alternatively spliced
domains at N-terminal site A (X and Z) and at C-terminal site C
(A and B).;
Name=XB; Synonyms=AIICI;
IsoId=Q64542-1; Sequence=Displayed;
Name=XA; Synonyms=AIICII;
IsoId=Q64542-2; Sequence=VSP_000407;
Note=Contains a phosphoserine at position 1115. Contains a
phosphoserine at position 1126. {ECO:0000244|PubMed:22673903};
Name=ZA; Synonyms=AICII;
IsoId=Q64542-3; Sequence=VSP_000406, VSP_000407;
Note=Contains a phosphoserine at position 1103. Contains a
phosphoserine at position 1114. {ECO:0000244|PubMed:22673903};
Name=ZB; Synonyms=AICI;
IsoId=Q64542-4; Sequence=VSP_000406;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Not detected in liver.
The highest levels are found in uterus and stomach. Isoform XA is
found in uterus, brain, stomach, small intestine, colon and
pancreas. Isoform XB is found in uterus, skeletal muscle, lung,
kidney, spleen, stomach, small intestine and pancreas. Isoform ZA
is found in testis and isoform ZB is found in testis and heart.
{ECO:0000269|PubMed:7702574, ECO:0000269|PubMed:8428948}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIB subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U15408; AAA81005.1; -; mRNA.
EMBL; U15408; AAA81006.1; -; mRNA.
EMBL; U15408; AAA81007.1; -; mRNA.
EMBL; U15408; AAA81008.1; -; mRNA.
EMBL; X76452; CAA53990.1; -; mRNA.
EMBL; L05569; AAA50820.1; -; Genomic_DNA.
EMBL; L05566; AAA50820.1; JOINED; Genomic_DNA.
EMBL; L05567; AAA50820.1; JOINED; Genomic_DNA.
PIR; G44525; G44525.
PIR; S50027; S50027.
PIR; S54356; S54356.
PIR; S54357; S54357.
RefSeq; NP_001005871.1; NM_001005871.1. [Q64542-2]
RefSeq; XP_008767668.1; XM_008769446.2. [Q64542-1]
RefSeq; XP_008767669.1; XM_008769447.2. [Q64542-1]
RefSeq; XP_008767670.1; XM_008769448.2. [Q64542-4]
RefSeq; XP_008767671.1; XM_008769449.2. [Q64542-2]
RefSeq; XP_008767672.1; XM_008769450.2. [Q64542-3]
UniGene; Rn.9986; -.
ProteinModelPortal; Q64542; -.
BioGrid; 248232; 1.
IntAct; Q64542; 1.
MINT; Q64542; -.
STRING; 10116.ENSRNOP00000004078; -.
iPTMnet; Q64542; -.
PhosphoSitePlus; Q64542; -.
PaxDb; Q64542; -.
PRIDE; Q64542; -.
Ensembl; ENSRNOT00000004078; ENSRNOP00000004078; ENSRNOG00000003031. [Q64542-1]
Ensembl; ENSRNOT00000046273; ENSRNOP00000039880; ENSRNOG00000003031. [Q64542-2]
GeneID; 29600; -.
KEGG; rno:29600; -.
UCSC; RGD:621305; rat. [Q64542-1]
CTD; 493; -.
RGD; 621305; Atp2b4.
eggNOG; KOG0204; Eukaryota.
eggNOG; ENOG410XNNC; LUCA.
GeneTree; ENSGT00940000154527; -.
HOGENOM; HOG000265623; -.
HOVERGEN; HBG061286; -.
InParanoid; Q64542; -.
KO; K05850; -.
OMA; TQWIFSI; -.
OrthoDB; EOG091G057D; -.
PhylomeDB; Q64542; -.
Reactome; R-RNO-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-RNO-5578775; Ion homeostasis.
Reactome; R-RNO-936837; Ion transport by P-type ATPases.
PRO; PR:Q64542; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000003031; Expressed in 10 organ(s), highest expression level in brain.
Genevisible; Q64542; RN.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0097228; C:sperm principal piece; IDA:RGD.
GO; GO:0030315; C:T-tubule; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005388; F:calcium-transporting ATPase activity; IDA:RGD.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
GO; GO:0036487; F:nitric-oxide synthase inhibitor activity; IEA:Ensembl.
GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
GO; GO:1901660; P:calcium ion export; IMP:RGD.
GO; GO:0070588; P:calcium ion transmembrane transport; IMP:RGD.
GO; GO:0006816; P:calcium ion transport; IDA:RGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0140199; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; IEA:Ensembl.
GO; GO:1900082; P:negative regulation of arginine catabolic process; IEA:Ensembl.
GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:BHF-UCL.
GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
GO; GO:1903249; P:negative regulation of citrulline biosynthetic process; IEA:Ensembl.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IEA:Ensembl.
GO; GO:0098736; P:negative regulation of the force of heart contraction; IEA:Ensembl.
GO; GO:0003407; P:neural retina development; IEP:RGD.
GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IEA:Ensembl.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0051599; P:response to hydrostatic pressure; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEP:RGD.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 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; IPR023214; HAD_sf.
InterPro; IPR006408; P-type_ATPase_IIB.
InterPro; IPR001757; P_typ_ATPase.
PANTHER; PTHR24093:SF276; PTHR24093:SF276; 1.
Pfam; PF12424; ATP_Ca_trans_C; 1.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 1.
TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calcium; Calcium transport;
Calmodulin-binding; Cell membrane; Cell projection; Cilium;
Complete proteome; Flagellum; Hydrolase; Ion transport; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1203 Plasma membrane calcium-transporting
ATPase 4.
/FTId=PRO_0000046221.
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 1203 Cytoplasmic. {ECO:0000255}.
REGION 1086 1103 Calmodulin-binding subdomain A.
{ECO:0000250|UniProtKB:P20020,
ECO:0000250|UniProtKB:P23634}.
REGION 1104 1113 Calmodulin-binding subdomain B.
{ECO:0000250|UniProtKB:P20020}.
COMPBIAS 297 303 Poly-Lys.
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:0000250|UniProtKB:P23634}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 334 334 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1070 1070 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1102 1102 Phosphothreonine; by PKC. {ECO:0000250}.
MOD_RES 1144 1144 Phosphoserine.
{ECO:0000250|UniProtKB:Q6Q477}.
VAR_SEQ 301 312 Missing (in isoform ZA and isoform ZB).
{ECO:0000303|PubMed:7702574}.
/FTId=VSP_000406.
VAR_SEQ 1105 1203 RVVKVFHSFRDVIHKSKNQVSIHSFMTQPEYAADDEMSQSF
LNQEESPSLASKSRITKRLSDAETVSQNNTNNNAVDCHQVQ
IVASHPNSPLQSQETPV -> EVINKFQTGASFKGVLRRQN
LSQQLDVKLVPSSYSEAVASVRTSPSTSSAVTPPPVGNQSG
QSIS (in isoform XA and isoform ZA).
{ECO:0000303|PubMed:7702574}.
/FTId=VSP_000407.
CONFLICT 431 431 I -> V (in Ref. 2; CAA53990).
{ECO:0000305}.
SEQUENCE 1203 AA; 133094 MW; B7A6C8D4556F6398 CRC64;
MTNPSGHNLP ANSVAESYEG EFGCTLMDLR KLMELRAADA VTQISAHYGS VQEICARLKT
SPVEGLSGNP ADLEKRRLVF GKNMIPPKKP KTFLELVWEA LQDVTLIILE IAAIISLVLS
FYRPPGGENE ICGHIVSNPE EDEEGETGWI EGAAILASVI IVVFVTAFND WSKEKQFRGL
QSRIELEQKF SIIRNGQLIQ LPVAEIVVGD IAQVKYGDLL PADGILIQGN DLKIDESSLT
GESDHVKKTL DKDPMLLSGT HVMEGSGRMV VTAVGINSQT GIIFTLLGAN EEEDDEKKKK
GKKQGVSENR NKAKTQDGVA LEIQPLNSQE GLDSEEKEKK ASKGPKKEKS VLQGKLTRLA
VQIGKAGLIM SILTVLILIL YFVVDNFVIQ RRAWLPECTP VYIQYFVKFF IIGVTVLVVA
VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL TMNRMTVVQA
YIGGTHYRQI PKPDDLPPNV LDLIVNSICI NSAYTSKILP PEKEGGLPRQ VGNKTECGLL
GFVTDLKQDY QAVRSEMPEE KLFKVYTFNS VRKSMSTVIR KPEGGFRVFS KGASEIMLRK
CDRILNKEGG IVPFKTKDRD NMVRNVIEPM ASEGLRTIGI AYRDFDGEEP SWENENEIFT
GLVCIAVVGI EDPVRPEVPD AINKCKRAGI TVRMVTGDNV NTARAIATKC GILTPGDDFL
CLEGKEFNRL IRNEKGEVEQ EKLDKVWPRL RVLARSSPTD KHTLVKGIID SNIGEQRQVV
AVTGDGTNDG PALKKADVGF AMGIAGTDVA KEASDIILTD DNFTSIVKAV MWGRNVYDSI
SKFLQFQLTV NVVAVIVAFS GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTDSLL
RRRPYGRNKP LISRTMMKNI LGHAVYQLGI VFLLVFAGDK LFDIDSGRKA PLNSPPSQHY
TIVFNTFVLM QLFNEINSRK IHGEKNVFAG VYRNIIFCSV VLGTFFCQIL IVEVGGKPFS
CTNLTMEQWM WCLFIGIGEL LWGQVISAIP TKSLKFLKEA GHGSDKEEIS KDAEGLEEID
HAEMELRRGQ ILWVRGLNRI QTQIRVVKVF HSFRDVIHKS KNQVSIHSFM TQPEYAADDE
MSQSFLNQEE SPSLASKSRI TKRLSDAETV SQNNTNNNAV DCHQVQIVAS HPNSPLQSQE
TPV


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