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Q9R0K7 (AT2B2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1198 AA.
Sequence statusComplete.
Protein existenceEvidence 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).

Subunit structure

Interacts with PDZD11 By similarity.

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 processCalcium transport
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Calmodulin-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from mutant phenotype PubMed 17823248. Source: GOC

auditory receptor cell stereocilium organization

Inferred from mutant phenotype PubMed 11875276. Source: MGI

cGMP metabolic process

Inferred from mutant phenotype PubMed 3038581PubMed 7518067. Source: MGI

calcium ion transport

Inferred from mutant phenotype PubMed 17234811. Source: DFLAT

cell morphogenesis

Inferred from mutant phenotype PubMed 10441500. Source: MGI

cellular calcium ion homeostasis

Inferred from mutant phenotype Ref.2PubMed 17234811. Source: MGI

cerebellar Purkinje cell differentiation

Inferred from mutant phenotype Ref.4. Source: MGI

cerebellar Purkinje cell layer morphogenesis

Inferred from mutant phenotype PubMed 17409239. Source: MGI

cerebellar granule cell differentiation

Inferred from mutant phenotype Ref.4. Source: MGI

cerebellum development

Inferred from mutant phenotype PubMed 16880690. 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

inner ear development

Inferred from mutant phenotype PubMed 11875276. Source: MGI

inner ear morphogenesis

Inferred from mutant phenotype Ref.4. Source: MGI

inner ear receptor cell differentiation

Inferred from mutant phenotype PubMed 11875276. 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 16845470PubMed 2765934PubMed 3038581PubMed 7518067Ref.4. Source: MGI

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 15350283PubMed 16845470Ref.4. Source: MGI

neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

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

sensory perception of sound

Inferred from sequence or structural similarity. Source: UniProtKB

serotonin metabolic process

Inferred from mutant phenotype PubMed 2765934. Source: MGI

synapse organization

Inferred from mutant phenotype PubMed 7683393. Source: MGI

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 17823248. Source: MGI

cilium

Inferred from direct assay PubMed 10441500. Source: MGI

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 17234811. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuronal cell body

Inferred from direct assay PubMed 10441500. Source: MGI

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11981198Plasma membrane calcium-transporting ATPase 2
PRO_0000046215

Regions

Topological domain1 – 9494Cytoplasmic Potential
Transmembrane95 – 11521Helical; Potential
Topological domain116 – 15237Extracellular Potential
Transmembrane153 – 17321Helical; Potential
Topological domain174 – 345172Cytoplasmic Potential
Transmembrane346 – 36520Helical; Potential
Topological domain366 – 39833Extracellular Potential
Transmembrane399 – 41618Helical; Potential
Topological domain417 – 830414Cytoplasmic Potential
Transmembrane831 – 85020Helical; Potential
Topological domain851 – 86010Extracellular Potential
Transmembrane861 – 88121Helical; Potential
Topological domain882 – 90120Cytoplasmic Potential
Transmembrane902 – 92423Helical; Potential
Topological domain925 – 94218Extracellular Potential
Transmembrane943 – 96422Helical; Potential
Topological domain965 – 98319Cytoplasmic Potential
Transmembrane984 – 100522Helical; Potential
Topological domain1006 – 101510Extracellular Potential
Transmembrane1016 – 103722Helical; Potential
Topological domain1038 – 1198161Cytoplasmic Potential
Region1078 – 109518Calmodulin-binding subdomain A By similarity
Region1096 – 110510Calmodulin-binding subdomain B By similarity
Compositional bias294 – 2974Poly-Glu

Sites

Active site45414-aspartylphosphate intermediate By similarity
Metal binding7751Magnesium By similarity
Metal binding7791Magnesium By similarity

Amino acid modifications

Modified residue10941Phosphothreonine; by PKC By similarity
Modified residue11561Phosphoserine; by PKA By similarity

Natural variations

Natural variant2431G → S in dfw. Ref.1
Natural variant4121E → K. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9R0K7 [UniParc].

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

FASTA1,198132,588
        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

[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.
+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.
CCDSCCDS20433.1.
RefSeqNP_001031761.1. NM_001036684.2.
NP_033853.1. NM_009723.5.
UniGeneMm.321755.
Mm.443564.

3D structure databases

ProteinModelPortalQ9R0K7.
SMRQ9R0K7. Positions 1078-1105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198250. 2 interactions.
IntActQ9R0K7. 5 interactions.
MINTMINT-4088651.
STRING10090.ENSMUSP00000098605.

PTM databases

PhosphoSiteQ9R0K7.

Proteomic databases

MaxQBQ9R0K7.
PaxDbQ9R0K7.
PRIDEQ9R0K7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089003; ENSMUSP00000086398; ENSMUSG00000030302.
ENSMUST00000101045; ENSMUSP00000098606; ENSMUSG00000030302.
GeneID11941.
KEGGmmu:11941.
UCSCuc009dhn.1. mouse.

Organism-specific databases

CTD491.
MGIMGI:105368. Atp2b2.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00510000046331.
HOGENOMHOG000265623.
HOVERGENHBG061286.
KOK05850.
OrthoDBEOG7SN8BN.
TreeFamTF300330.

Gene expression databases

ArrayExpressQ9R0K7.
BgeeQ9R0K7.
CleanExMM_ATP2B2.
GenevestigatorQ9R0K7.

Family and domain databases

Gene3D1.20.1110.10. 3 hits.
InterProIPR022141. 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]
PfamPF12424. 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]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAtp2b2. mouse.
NextBio280043.
PROQ9R0K7.
SOURCESearch...

Entry information

Entry nameAT2B2_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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