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Q0QEP3 (Q0QEP3_RAT) Unreviewed, UniProtKB/TrEMBL

Last modified May 14, 2014. Version 57. Feed History...

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

Names and origin

Protein namesRecommended name:
ATP synthase subunit beta RuleBase RU003553

EC=3.6.3.14 RuleBase RU003553
Gene names
Name:Atp5b RGD 621368
Synonyms:ATP5B EMBL ABD77234.1
OrganismRattus norvegicus (Rat) EMBL ABD77234.1
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length343 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Produces ATP from ADP in the presence of a proton gradient across the membrane By similarity. RuleBase RU003553

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). RuleBase RU003553

Subunit structure

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c By similarity. RuleBase RU004290

Sequence similarities

Belongs to the ATPase alpha/beta chains family. RuleBase RU000339

Ontologies

Keywords
   Biological processATP synthesis
Hydrogen ion transport RuleBase RU000339
Ion transport
Transport
   Cellular componentCF(1) RuleBase RU003553
   LigandATP-binding RuleBase RU003553
Nucleotide-binding
Gene Ontology (GO)
   Biological_processATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

ATP synthesis coupled proton transport

Inferred from electronic annotation. Source: InterPro

angiogenesis

Inferred from electronic annotation. Source: Ensembl

lipid metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell adhesion involved in substrate-bound cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of intracellular pH

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

mitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

mitochondrial proton-transporting ATP synthase complex

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

proton-transporting ATP synthase complex, catalytic core F(1)

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

proton-transporting ATP synthase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

proton-transporting ATPase activity, rotational mechanism

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Experimental info

Non-terminal residue11 EMBL ABD77234.1
Non-terminal residue3431 EMBL ABD77234.1

Sequences

Sequence LengthMass (Da)Tools
Q0QEP3 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 9E27C3A20F0859D4

FASTA34337,252
        10         20         30         40         50         60 
HAEAPEFIEM SVEQEILVTG IKVVDLLAPY AKGGKIGLFG GAGVGKTVLI MELINNVAKA 

        70         80         90        100        110        120 
HGGYSVFAGV GERTREGNDL YHEMIESGVI NLKDATSKVA LVYGQMNEPP GARARVALTG 

       130        140        150        160        170        180 
LTVAEYFRDQ EGQDVLLFID NIFRFTQAGS EVSALLGRIP SAVGYQPTLA TDMGTMQERI 

       190        200        210        220        230        240 
TTTKKGSITS VQAIYVPADD LTDPAPATTF AHLDATTVLS RAIAELGIYP AVDPLDSTSR 

       250        260        270        280        290        300 
IMDPNIVGSE HYDVARGVQK ILQDYKSLQD IIAILGMDEL SEEDKLTVSR ARKIQRFLSQ 

       310        320        330        340 
PFQVAEVFTG HMGKLVPLKE TIKGFQQILA GDYDHLPEQA FYM 

« Hide

References

[1]"Housekeeping genes for phylogenetic analysis of eutherian relationships."
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Tissue: Liver EMBL ABD77234.1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ403101 mRNA. Translation: ABD77234.1.
UniGeneRn.92965.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000003965.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD621368. Atp5b.

Phylogenomic databases

HOVERGENHBG004307.
InParanoidQ0QEP3.

Gene expression databases

ArrayExpressQ0QEP3.
GenevestigatorQ0QEP3.

Family and domain databases

Gene3D1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01039. atpD. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ0QEP3_RAT
AccessionPrimary (citable) accession number: Q0QEP3
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2006
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)