Plasma membrane calcium-transporting ATPase 2

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Q9R0K7 (AT2B2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Plasma membrane calcium-transporting ATPase 2
Short name=PMCA2
EC=3.6.3.8

Alternative name(s):
Plasma membrane calcium ATPase isoform 2
Plasma membrane calcium pump isoform 2

Gene names

Name:	Atp2b2
Synonyms:	Pmca2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1198 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. Plays a role in maintaining balance and hearing. Ref.4
Catalytic activity	ATP + H₂O + Ca²⁺(Side 1) = ADP + phosphate + Ca²⁺(Side 2).
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Mainly expressed in brain cortex. Found at low levels in heart, liver, lung and testis during late gestation. Also found in cochlea (stereocilia and outer wall of hair cells).
Involvement in disease	Atp2b2 null deficient mice are deaf.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIB subfamily. [View classification]

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Calmodulin-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	auditory receptor cell stereocilium organization Inferred from mutant phenotype PubMed 11875276. Source: MGI cGMP metabolic process Inferred from mutant phenotype PubMed 3038581 PubMed 7518067. Source: MGI cerebellar Purkinje cell differentiation Inferred from mutant phenotype Ref.4. Source: MGI cerebellar granule cell differentiation Inferred from mutant phenotype Ref.4. Source: MGI cochlea development Inferred from mutant phenotype Ref.4. Source: DFLAT cytosolic calcium ion homeostasis Inferred from mutant phenotype PubMed 17234811. Source: DFLAT detection of mechanical stimulus involved in sensory perception of sound Inferred from mutant phenotype PubMed 16529873. Source: MGI lactation Inferred from mutant phenotype PubMed 15302868. Source: MGI locomotion Inferred from mutant phenotype PubMed 16880690. Source: MGI locomotory behavior Inferred from mutant phenotype PubMed 16845470 PubMed 2765934 PubMed 3038581 PubMed 7518067 Ref.4. Source: MGI neuromuscular process controlling balance Inferred from mutant phenotype PubMed 15350283 PubMed 16845470 Ref.4. Source: MGI organelle organization Inferred from mutant phenotype PubMed 11875276. Source: MGI otolith mineralization Inferred from mutant phenotype Ref.4. Source: MGI positive regulation of calcium ion transport Inferred from mutant phenotype PubMed 17823248. Source: MGI regulation of cell size Inferred from mutant phenotype PubMed 11875276. Source: MGI regulation of synaptic plasticity Inferred from mutant phenotype PubMed 17409239. Source: MGI serotonin metabolic process Inferred from mutant phenotype PubMed 2765934. Source: MGI synapse organization Inferred from mutant phenotype PubMed 7683393. Source: MGI
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 17823248. Source: MGI cilium Inferred from direct assay PubMed 10441500. Source: MGI endoplasmic reticulum Inferred from direct assay PubMed 17234811. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW neuronal cell body Inferred from direct assay PubMed 10441500. Source: MGI
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB PDZ domain binding Inferred from sequence or structural similarity. Source: UniProtKB calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB calcium-dependent ATPase activity Inferred from mutant phenotype PubMed 17823248. Source: MGI calcium-transporting ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB calmodulin binding Inferred from sequence or structural similarity. Source: UniProtKB protein C-terminus binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1198

1198

Plasma membrane calcium-transporting ATPase 2

PRO_0000046215

Regions

Topological domain

1 – 94

Cytoplasmic Potential

Transmembrane

95 – 115

Helical; Potential

Topological domain

116 – 152

Extracellular Potential

Transmembrane

153 – 173

Helical; Potential

Topological domain

174 – 345

172

Cytoplasmic Potential

Transmembrane

346 – 365

Helical; Potential

Topological domain

366 – 398

Extracellular Potential

Transmembrane

399 – 416

Helical; Potential

Topological domain

417 – 830

414

Cytoplasmic Potential

Transmembrane

831 – 850

Helical; Potential

Topological domain

851 – 860

Extracellular Potential

Transmembrane

861 – 881

Helical; Potential

Topological domain

882 – 901

Cytoplasmic Potential

Transmembrane

902 – 924

Helical; Potential

Topological domain

925 – 942

Extracellular Potential

Transmembrane

943 – 964

Helical; Potential

Topological domain

965 – 983

Cytoplasmic Potential

Transmembrane

984 – 1005

Helical; Potential

Topological domain

1006 – 1015

Extracellular Potential

Transmembrane

1016 – 1037

Helical; Potential

Topological domain

1038 – 1198

161

Cytoplasmic Potential

Region

1078 – 1095

Calmodulin-binding subdomain A By similarity

Region

1096 – 1105

Calmodulin-binding subdomain B By similarity

Compositional bias

294 – 297

Poly-Glu

Sites

Active site

454

4-aspartylphosphate intermediate By similarity

Metal binding

775

Magnesium By similarity

Metal binding

779

Magnesium By similarity

Amino acid modifications

Modified residue

1094

Phosphothreonine; by PKC By similarity

Modified residue

1156

Phosphoserine; by PKA By similarity

Modified residue

1186

Phosphoserine By similarity

Modified residue

1189

Phosphoserine Ref.5

Modified residue

1193

Phosphoserine By similarity

Modified residue

1196

Phosphothreonine Ref.5

Modified residue

1197

Phosphoserine Ref.6

Natural variations

Natural variant

243

G → S in dfw. Ref.1

Natural variant

412

E → K. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q9R0K7 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: BAA8CC28620D994B
Show »

FASTA

1,198

132,588

        10         20         30         40         50         60 
MGDMTNSDFY SKNQRNESSH GGEFGCTMEE LRSLMELRGT EAVVKIKETY GDTEAICRRL 

        70         80         90        100        110        120 
KTSPVEGLPG TAPDLEKRKQ IFGQNFIPPK KPKTFLQLVW EALQDVTLII LEIAAIISLG 

       130        140        150        160        170        180 
LSFYHPPGES NEGCATAQGG AEDEGEAEAG WIEGAAILLS VICVVLVTAF NDWSKEKQFR 

       190        200        210        220        230        240 
GLQSRIEQEQ KFTVVRAGQV VQIPVAEIVV GDIAQIKYGD LLPADGLFIQ GNDLKIDESS 

       250        260        270        280        290        300 
LTGESDQVRK SVDKDPMLLS GTHVMEGSGR MVVTAVGVNS QTGIIFTLLG AGGEEEEKKD 

       310        320        330        340        350        360 
KKAKQQDGAA AMEMQPLKSA EGGDADDKKK ANMHKKEKSV LQGKLTKLAV QIGKAGLVMS 

       370        380        390        400        410        420 
AITVIILVLY FTVDTFVVNK KPWLTECTPV YVQYFVKFFI IGVTVLVVAV PEGLPLAVTI 

       430        440        450        460        470        480 
SLAYSVKKMM KDNNLVRHLD ACETMGNATA ICSDKTGTLT TNRMTVVQAY VGDVHYKEIP 

       490        500        510        520        530        540 
DPSSINAKTL ELLVNAIAIN SAYTTKILPP EKEGALPRQV GNKTECGLLG FVLDLRQDYE 

       550        560        570        580        590        600 
PVRSQMPEEK LYKVYTFNSV RKSMSTVIKM PDESFRMYSK GASEIVLKKC CKILSGAGEA 

       610        620        630        640        650        660 
RVFRPRDRDE MVKKVIEPMA CDGLRTICVA YRDFPSSPEP DWDNENDILN ELTCICVVGI 

       670        680        690        700        710        720 
EDPVRPEVPE AIRKCQRAGI TVRMVTGDNI NTARAIAIKC GIIHPGEDFL CLEGKEFNRR 

       730        740        750        760        770        780 
IRNEKGEIEQ ERIDKIWPKL RVLARSSPTD KHTLVKGIID STHTEQRQVV AVTGDGTNDG 

       790        800        810        820        830        840 
PALKKADVGF AMGIAGTDVA KEASDIILTD DNFSSIVKAV MWGRNVYDSI SKFLQFQLTV 

       850        860        870        880        890        900 
NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTETLL LRKPYGRNKP 

       910        920        930        940        950        960 
LISRTMMKNI LGHAVYQLTL IFTLLFVGEK MFQIDSGRNA PLHSPPSEHY TIIFNTFVMM 

       970        980        990       1000       1010       1020 
QLFNEINARK IHGERNVFDG IFRNPIFCTI VLGTFAIQIV IVQFGGKPFS CSPLQLDQWM 

      1030       1040       1050       1060       1070       1080 
WCIFIGLGEL VWGQVIATIP TSRLKFLKEA GRLTQKEEIP EEELNEDVEE IDHAERELRR 

      1090       1100       1110       1120       1130       1140 
GQILWFRGLN RIQTQIRVVK AFRSSLYEGL EKPESRTSIH NFMAHPEFRI EDSQPHIPLI 

      1150       1160       1170       1180       1190 
DDTDLEEDAA LKQNSSPPSS LNKNNSAIDS GINLTTDTSK SATSSSPGSP IHSLETSL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in a plasma membrane Ca2+-ATPase gene cause deafness in deafwaddler mice." Street V.A., McKee-Johnson J.W., Fonseca R.C., Tempel B.L., Noben-Trauth K. Nat. Genet. 19:390-394(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT DFW SER-243. Strain: C3H/HeJ.
[2]	"A mouse with a point mutation in plasma membrane Ca2+-ATPase isoform 2 gene showed the reduced Ca2+ influx in cerebellar neurons." Ueno T., Kameyama K., Hirata M., Ogawa M., Hatsuse H., Takagaki Y., Ohmura M., Osawa N., Kudo Y. Neurosci. Res. 42:287-297(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-412. Strain: BALB/C WMS.
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 16-32; 46-58; 62-77; 80-90; 197-249; 251-270; 305-318; 438-455; 464-477; 489-506; 537-543; 554-561; 570-576; 581-588; 593-601; 626-632; 684-694; 757-767; 785-818; 825-832; 931-938; 976-983; 1104-1116; 1130-1152 AND 1164-1180. Strain: C57BL/6. Tissue: Brain.
[4]	"Balance and hearing deficits in mice with a null mutation in the gene encoding plasma membrane Ca2+-ATPase isoform 2." Kozel P.J., Friedman R.A., Erway L.C., Yamoah E.N., Liu L.H., Riddle T., Duffy J.J., Doetschman T., Miller M.L., Cardell E.L., Shull G.E. J. Biol. Chem. 273:18693-18696(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1189 AND THR-1196, MASS SPECTROMETRY. Tissue: Brain cortex.
[6]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1197, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF053471 mRNA. Translation: AAC61255.1. AB030737 mRNA. Translation: BAA83104.1. AB030738 mRNA. Translation: BAA83105.1.
IPI	IPI00127713.
RefSeq	NP_001031761.1. NM_001036684.2. NP_033853.1. NM_009723.5.
UniGene	Mm.321755. Mm.443564.
3D structure databases
ProteinModelPortal	Q9R0K7.
SMR	Q9R0K7. Positions 70-903, 1078-1105.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9R0K7. 3 interactions.
STRING	10090.ENSMUSP00000098605.
PTM databases
PhosphoSite	Q9R0K7.
Proteomic databases
PaxDb	Q9R0K7.
PRIDE	Q9R0K7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000089003; ENSMUSP00000086398; ENSMUSG00000030302. ENSMUST00000101045; ENSMUSP00000098606; ENSMUSG00000030302.
GeneID	11941.
KEGG	mmu:11941.
Organism-specific databases
CTD	491.
MGI	MGI:105368. Atp2b2.
Phylogenomic databases
eggNOG	COG0474.
GeneTree	ENSGT00510000046331.
HOGENOM	HOG000265623.
HOVERGEN	HBG061286.
KO	K05850.
OrthoDB	EOG4K9BBF.
Gene expression databases
ArrayExpress	Q9R0K7.
Bgee	Q9R0K7.
CleanEx	MM_ATP2B2.
Genevestigator	Q9R0K7.
GermOnline	ENSMUSG00000030302. Mus musculus.
Family and domain databases
Gene3D	1.20.1110.10. 3 hits.
InterPro	IPR022141. ATP_Ca_trans_C. IPR006408. ATPase_P-typ_Ca-transp_plasma. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023299. ATPase_P-typ_cyto_domN. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR008250. ATPase_P-typ_transduc_dom_A. IPR001757. Cation_transp_P_typ_ATPase. IPR023214. HAD-like_dom. [Graphical view]
PANTHER	PTHR24093. PTHR24093. 1 hit.
Pfam	PF12424. ATP_Ca_trans_C. 1 hit. PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01517. ATPase-IIB_Ca. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Atp2b2. mouse.
NextBio	280043.
SOURCE	Search...

Entry information

Entry name

AT2B2_MOUSE

Accession

Primary (citable) accession number: Q9R0K7
Secondary accession number(s): O88863

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents