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P57709 (AT2C1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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):
Secretory pathway Ca(2+)-transporting ATPase
Gene names
Name:ATP2C1
Synonyms:SPCA
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2].

Subcellular location

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

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. [View classification]

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentGolgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
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

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-KW

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

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 – 953953Calcium-transporting ATPase type 2C member 1
PRO_0000046222

Regions

Topological domain1 – 104104Cytoplasmic By similarity
Transmembrane105 – 12521Helical; Name=1; By similarity
Topological domain126 – 13813Lumenal By similarity
Transmembrane139 – 15719Helical; Name=2; By similarity
Topological domain158 – 296139Cytoplasmic By similarity
Transmembrane297 – 31620Helical; Name=3; By similarity
Topological domain317 – 32812Lumenal By similarity
Transmembrane329 – 34618Helical; Name=4; By similarity
Topological domain347 – 733387Cytoplasmic By similarity
Transmembrane734 – 75320Helical; Name=5; By similarity
Topological domain754 – 76310Lumenal By similarity
Transmembrane764 – 78421Helical; Name=6; By similarity
Topological domain785 – 80420Cytoplasmic By similarity
Transmembrane805 – 82420Helical; Name=7; By similarity
Topological domain825 – 84218Lumenal By similarity
Transmembrane843 – 86220Helical; Name=8; By similarity
Topological domain863 – 87513Cytoplasmic By similarity
Transmembrane876 – 89419Helical; Name=9; By similarity
Topological domain895 – 90915Lumenal By similarity
Transmembrane910 – 93021Helical; Name=10; By similarity
Topological domain931 – 95323Cytoplasmic By similarity

Sites

Active site38414-aspartylphosphate intermediate By similarity
Metal binding3371Calcium 2; via carbonyl oxygen By similarity
Metal binding3381Calcium 2; via carbonyl oxygen By similarity
Metal binding3401Calcium 2; via carbonyl oxygen By similarity
Metal binding3421Calcium 2 By similarity
Metal binding6781Magnesium By similarity
Metal binding6821Magnesium By similarity
Metal binding7721Calcium 2 By similarity
Metal binding7761Calcium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P57709 [UniParc].

Last modified January 11, 2001. Version 1.
Checksum: 2412EEB45AFB000F

FASTA953104,780
        10         20         30         40         50         60 
MDNLLPQSRF SYFKKYPIHA IRKYLSMLRN QKEEEQVARF QKIPNAENET MIPVLTSKKA 

        70         80         90        100        110        120 
SELPVSEVAS ILQADLQNGL NKCEVSHRRA FHGWNEFDIS EDEPLWKKYI SQFKNPLIML 

       130        140        150        160        170        180 
LLASAVISVL MHQFDDAVSI TVAILIVVTV AFVQEYRSEK SLEELSKLMP PECHCVREGK 

       190        200        210        220        230        240 
LEHTLARDLV PGDTVCLSVG DRVPADLRLF EAVDLSVDES SLTGETTPCS KVTAPQPAAT 

       250        260        270        280        290        300 
NGDLASRSNI AFMGTLVRCG KAKGIVIGTG ENSEFGEVFK MMQAEEAPKT PLQKSMDLLG 

       310        320        330        340        350        360 
KQLSFYSFGI IGIIMLVGWL LGKDILEMFT ISVSLAVAAI PEGLPIVVTV TLALGVMRMV 

       370        380        390        400        410        420 
KKRAIVKKLP IVETLGCCNV ICSDKTGTLT KNEMTVTHIF TSDGLRAEVT GVGYNPFGEV 

       430        440        450        460        470        480 
IVDGDVVHGF YNPSVSRIVE AGCVCNDAVI RNNTLMGKPT EGALIALAMK MGLDGLQQDY 

       490        500        510        520        530        540 
IRKAEYPFSS EQKWMAVKCV HRTQQDRPEI CFMKGAYEQV IKYCTTYHSK GQTLTLTQQQ 

       550        560        570        580        590        600 
RDLYQQEKAQ MGSAGLRVLA LASGPELGQL TFLGLVGIID PPRTGVKEAV TTLIASGVSI 

       610        620        630        640        650        660 
KMITGDSQET AVAIASRLGL YSKTSQSVSG EEIDAMDVQQ LSQIVPKVAV FYRASPRHKM 

       670        680        690        700        710        720 
KIIKSLQKNG SVVAMTGDGV NDAVALKAAD IGVAMGQTGT DVCKEAADMI LVDDDFQTIM 

       730        740        750        760        770        780 
SAIEEGKGIY NNIKNFVRFQ LSTSIAALTL ISLATLMNFP NPLNAMQILW INIIMDGPPA 

       790        800        810        820        830        840 
QSLGVEPVDK DVIRKPPRNW KDSILTKNLI LKILVSSIII VCGTLFVFWR ELRDNVITPR 

       850        860        870        880        890        900 
DTTMTFTCFV FFDMFNALSS RSQTKSVFEI GLCSNKMFCY AVLGSIMGQL LVIYFPPLQK 

       910        920        930        940        950 
VFQTESLSIL DLLFLLGLTS SVCIVAEIIK KVERSREKIQ KPVSSTSSSF LEV

« Hide

References

[1]"Bos taurus mRNA encoding putative secretory pathway Ca2+-transporting ATPase (SPCA)."
Prapong S., Reinhardt T.A.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF230532 mRNA. Translation: AAF64433.1.
IPIIPI00709888.
RefSeqNP_786979.1. NM_175785.2.
UniGeneBt.269.

3D structure databases

ProteinModelPortalP57709.
ModBaseSearch...

Proteomic databases

PRIDEP57709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000015441; ENSBTAP00000015441; ENSBTAG00000011626.
GeneID327663.
KEGGbta:327663.

Organism-specific databases

CTD27032.

Phylogenomic databases

eggNOGmaNOG07595.
GeneTreeENSGT00560000076887.
HOVERGENHBG106478.
InParanoidP57709.
OMALMPPECH.
OrthoDBEOG4QC14N.
PhylomeDBP57709.

Family and domain databases

InterProIPR023306. ATPase_cation_domN.
IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006413. ATPase_P-typ_Ca-transp_PMR1.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR000695. ATPase_P-typ_H-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits.
KOK01537.
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.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAT2C1_BOVIN
AccessionPrimary (citable) accession number: P57709
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: January 25, 2012
This is version 92 of the entry and version 1 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

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