Q0QEP3 (Q0QEP3_RAT) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) EMBL ABD77234.1

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	343 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Produces ATP from ADP in the presence of a proton gradient across the membrane By similarity.
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out).
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 process	ATP synthesis Hydrogen ion transport RuleBase RU000339 Ion transport Transport
Cellular component	CF(1) RuleBase RU003553
Ligand	ATP-binding RuleBase RU003299 Nucleotide-binding
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC ATP 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: Compara lipid metabolic process Inferred from electronic annotation. Source: Compara negative regulation of cell adhesion involved in substrate-bound cell migration Inferred from electronic annotation. Source: Compara regulation of intracellular pH Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara mitochondrial nucleoid Inferred from electronic annotation. Source: Compara mitochondrial proton-transporting ATP synthase complex Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW eukaryotic cell surface binding Inferred from electronic annotation. Source: Compara proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Experimental info
	Non-terminal residue	1	1	EMBL ABD77234.1
	Non-terminal residue	343	1	EMBL ABD77234.1

Sequences

	Sequence		Length	Mass (Da)
	Q0QEP3 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 9E27C3A20F0859D4	FASTA	343	37,252
	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

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.
IPI	IPI00551812.
UniGene	Rn.92965.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000003965. Q0QEP3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	621368. Atp5b.
Phylogenomic databases
HOVERGEN	HBG004307.
InParanoid	Q0QEP3.
Gene expression databases
ArrayExpress	Q0QEP3.
Genevestigator	Q0QEP3.
Family and domain databases
Gene3D	1.10.1140.10. 1 hit.
InterPro	IPR003593. 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. [Graphical view]
PANTHER	PTHR15184:SF8. PTHR15184:SF8. 1 hit.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit.
TIGRFAMs	TIGR01039. atpD. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q0QEP3_RAT

Accession

Primary (citable) accession number: Q0QEP3

Entry history

Integrated into UniProtKB/TrEMBL:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)