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Reviewed, UniProtKB/Swiss-Prot Q5R5K5 (AT2C1_PONAB)

Last modified October 13, 2009. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
    Calcium-transporting ATPase type 2C member 1
      Short name=ATPase 2C1
    EC=3.6.3.8
Gene names
Name: ATP2C1
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

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

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 membrane; Multi-pass membrane protein By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentGolgi apparatus
Membrane
   DomainTransmembrane
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Calcium-transporting ATPase type 2C member 1
PRO_0000326150

Regions

Topological domain1 – 7575Cytoplasmic Potential
Transmembrane76 – 9621 Potential
Topological domain97 – 982Extracellular Potential
Transmembrane99 – 11921 Potential
Topological domain120 – 267148Cytoplasmic Potential
Transmembrane268 – 28821 Potential
Topological domain289 – 30214Extracellular Potential
Transmembrane303 – 32321 Potential
Topological domain324 – 703380Cytoplasmic Potential
Transmembrane704 – 72421 Potential
Topological domain725 – 7328Extracellular Potential
Transmembrane733 – 75321 Potential
Topological domain754 – 77320Cytoplasmic Potential
Transmembrane774 – 79421 Potential
Topological domain795 – 84248Extracellular Potential
Transmembrane843 – 86321 Potential
Topological domain864 – 87310Cytoplasmic Potential
Transmembrane874 – 89421 Potential
Topological domain895 – 91824Extracellular Potential

Sites

Active site35014-aspartylphosphate intermediate By similarity
Metal binding6431Magnesium By similarity
Metal binding6471Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R5K5-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 96C2EE903944AD83

FASTA918100,400
        10         20         30         40         50         60 
MKVARFQKIP NGENETMIPV LTSKKASELP VSEVASILQA DLQNGLNKCE VSHRRAFHGW 

        70         80         90        100        110        120 
NEFDISEDEP LWKKYISQFK NPLIMLLLAS AVISVLMHQF DDAVSITVAI LIVVTVAFVQ 

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

       190        200        210        220        230        240 
LSIDESSLTG ETTPCSKVTA PQPAATNGDL ASRSNIAFMG TLVRCGKAKG VVIGTGENSE 

       250        260        270        280        290        300 
FGEVFKMMQA EEAPKTPLQK SMDLLGKQLS FYSFGIIGII MLVGWLLGKD ILEMFTISVS 

       310        320        330        340        350        360 
LAVAAIPEGL PIVVTVTLAL GVMRMVKKRA IVKKLPIVET LGCCNVICSD KTGTLTKNEM 

       370        380        390        400        410        420 
TVTHIFTSDG LHAEVTGVGY NQFGEVIVDG DVVHGFYNPA VSRIVEAGCV CNDAVIRNNT 

       430        440        450        460        470        480 
LMGKPTEGAL IALAMKMGLD GLQQDYIRKA EYPFSSEQKW MAVKCVHRTQ QDRPEICFMK 

       490        500        510        520        530        540 
GAYEQVIKYC TTYQSKGQTL TLTQQQRDVQ QEKARMGSAG LRVLALASGP ELGQLTFLGL 

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

       610        620        630        640        650        660 
MDVQQLSQIV PKVAVFYRAS PRHKMKIIKS LQKNGSVVAM TGDGVNDAVA LKAADIGVAM 

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

       730        740        750        760        770        780 
LMNFPNPLNA MQILWINIIM DGPPAQSLGV 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 AEIIKKVERS 

       910 
REKIQKHVSS TSSSFLEV 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

CR860853 mRNA. Translation: CAH92961.1.
UniGenePab.18630

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENQ5R5K5.

Enzyme and pathway databases

BRENDA3.6.3.8. 269192.

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...

Entry information

Entry nameAT2C1_PONAB
AccessionPrimary (citable) accession number: Q5R5K5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: December 21, 2004
Last modified: October 13, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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