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Reviewed, UniProtKB/Swiss-Prot Q80XR2 (AT2C1_MOUSE)

Last modified October 13, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Calcium-transporting ATPase type 2C member 1
      Short name=ATPase 2C1
    EC=3.6.3.8
Alternative name(s):
    ATP-dependent Ca(2+) pump PMR1
Gene names
Name: Atp2c1
Synonyms: Pmr1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length918 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium By similarity.

Catalytic activity

ATP + H2O + Ca2+(Cis) = ADP + phosphate + Ca2+(Trans).

Subcellular location

Golgi apparatus › Golgi stack membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IIA subfamily.

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Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentGolgi apparatus
Membrane
   DomainTransmembrane
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

Golgi calcium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi calcium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-dependent cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

cellular manganese ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

epidermis development

Inferred from sequence or structural similarity. Source: UniProtKB

manganese ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB cascade

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentGolgi membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-transporting ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

manganese-transporting ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

signal transducer activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Calcium-transporting ATPase type 2C member 1
PRO_0000046224

Regions

Topological domain1 – 7878Cytoplasmic Potential
Transmembrane79 – 9517 Potential
Topological domain96 – 994Extracellular Potential
Transmembrane100 – 12122 Potential
Topological domain122 – 262141Cytoplasmic Potential
Transmembrane263 – 28220 Potential
Topological domain283 – 29412Extracellular Potential
Transmembrane295 – 31622 Potential
Topological domain317 – 699383Cytoplasmic Potential
Transmembrane700 – 72223 Potential
Topological domain723 – 7275Extracellular Potential
Transmembrane728 – 75124 Potential
Topological domain752 – 77524Cytoplasmic Potential
Transmembrane776 – 79419 Potential
Topological domain795 – 8017Extracellular Potential
Transmembrane802 – 82726 Potential
Topological domain828 – 84215Cytoplasmic Potential
Transmembrane843 – 86220 Potential
Topological domain863 – 87513Extracellular Potential
Transmembrane876 – 89217 Potential
Topological domain893 – 91826Cytoplasmic Potential

Sites

Active site34914-aspartylphosphate intermediate By similarity
Metal binding6431Magnesium By similarity
Metal binding6471Magnesium By similarity

Experimental info

Sequence conflict1561V → A in CAD82864. Ref.1
Sequence conflict1891I → T in CAD82864. Ref.1
Sequence conflict2171F → S in CAD82864. Ref.1
Sequence conflict2801M → T in CAD82864. Ref.1
Sequence conflict7431S → P in CAD82864. Ref.1
Sequence conflict8131C → R in CAD82864. Ref.1
Sequence conflict9021E → G in CAD82864. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q80XR2-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3323CF4FD3D9D487

FASTA918100,301
        10         20         30         40         50         60 
MKVARFQKIP NVENETMIPV LTSKRASELA VSEVAGLLQA DLQNGLNKSE VSHRRAFHGW 

        70         80         90        100        110        120 
NEFDISEDEP LWKKYISQFK NPLIMLLLAS AVISILMRQF DDAVSITVAI VIVVTVAFVQ 

       130        140        150        160        170        180 
EYRSEKSLEE LSKLVPPECH CVREGKLEHT LARDLVPGDT VCLSVGDRVP ADLRLFEAVD 

       190        200        210        220        230        240 
LSVDESSLIG ETAPCSKVTA PQPAANGDLA SRSNIAFMGT LVRCGKAKGI VIGTGENSEF 

       250        260        270        280        290        300 
GEVFKMMQAE EAPKTPLQKS MDLLGKQLSF YSFGIIGIIM LVGWLLGKDI LEMFTISVSL 

       310        320        330        340        350        360 
AVAAIPEGLP IVVTVTLALG VMRMVKKRAI VKKLPIVETL GCCNVICSDK TGTLTKNEMT 

       370        380        390        400        410        420 
VTHILTSDGL HAEVTGVGYN QFGEVIVDGD VVHGFYNPAV SRIVEAGCVC NDAVIRNNTL 

       430        440        450        460        470        480 
MGKPTEGALI ALAMKMGLDG LQQDYIRKAE YPFSSEQKWM AVKCVHRTQQ DRPEICFMKG 

       490        500        510        520        530        540 
AYEQVIKYCT TYNSKGQTLA LTQQQRDLYQ QEKARMGSAG LRVLALASGP ELGQLTFLGL 

       550        560        570        580        590        600 
VGIIDPPRTG VKEAVTTLIA SGVSIKMITG DSQETAIAIA SRLGLYSKTS QSVSGEEVDT 

       610        620        630        640        650        660 
MEVQHLSQIV PKVAVFYRAS PRHKMKIIKS LQKNGAVVAM TGDGVNDAVA LKAADIGVAM 

       670        680        690        700        710        720 
GQTGTDVCKE AADMILVDDD FQTIMSAIEE GKGIYNNIKN FVRFQLSTSI AALTLISLAT 

       730        740        750        760        770        780 
LMNFPNPLNA MQILWINIIM DGSPAQSLGV EPVDKDVIRK PPRNWKDSIL TKNLILKILV 

       790        800        810        820        830        840 
SSIIIVCGTL FVFWRELRDN VITPRDTTMT FTCFVFFDMF NALSSRSQTK SVFEIGLCSN 

       850        860        870        880        890        900 
KMFCYAVLGS IMGQLLVIYF PPLQKVFQTE SLSILDLLFL LGLTSSVCIV SEIIKKVERS 

       910 
REKVQKNAGS ASSSFLEV

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References

« Hide 'large scale' references
[1]"Role for plasma membrane-related Ca2+-ATPase-1 (ATP2C1) in pancreatic beta-cell Ca2+ homeostasis revealed by RNA silencing."
Mitchell K.J., Tsuboi T., Rutter G.A.
Diabetes 53:393-400(2004) [PubMed: 14747290] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 127-133, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AJ551270 mRNA. Translation: CAD82864.1.
BC043091 mRNA. Translation: AAH43091.1.
IPIIPI00336323.
RefSeqNP_778190.3.
UniGeneMm.326247

3D structure databases

HSSPHSSP built from PDB template 1EUL based on UniProtKB P04191.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ80XR2.

PTM databases

PhosphoSiteQ80XR2.

Proteomic databases

PRIDEQ80XR2.

Genome annotation databases

EnsemblENSMUST00000038118; ENSMUSP00000039103; ENSMUSG00000032570; Mus musculus. [Genome view]
ENSMUST00000085133; ENSMUSP00000082220; ENSMUSG00000032570; Mus musculus. [Genome view]
GeneID235574.
KEGGmmu:235574.
UCSCuc009rif.1. mouse.

Organism-specific databases

MGIMGI:1889008. Atp2c1.

Phylogenomic databases

HOVERGENQ80XR2.

Enzyme and pathway databases

BRENDA3.6.3.8. 244.

Gene expression databases

ArrayExpressQ80XR2.
BgeeQ80XR2.
CleanExMM_ATP2C1.
GenevestigatorQ80XR2.
GermOnlineENSMUSG00000032570. Mus musculus.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-reg.
IPR006413. ATPase_P-typ_Ca-transp_PMR1.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR000695. ATPase_P-typ_H-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
[Graphical view]
PANTHERPTHR11939. ATPase_P. 1 hit.
PfamPF00689. 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.
PR00120. HATPASE.
TIGRFAMsTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 4 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio382755.
SOURCESearch...

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Entry information

Entry nameAT2C1_MOUSE
AccessionPrimary (citable) accession number: Q80XR2
Secondary accession number(s): Q80YZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2003
Last modified: October 13, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents