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P05496 (AT5G1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase F(0) complex subunit C1, mitochondrial
Alternative name(s):
ATP synthase lipid-binding protein
ATP synthase proteolipid P1
ATP synthase proton-transporting mitochondrial F(0) complex subunit C1
ATPase protein 9
ATPase subunit c
Gene names
Name:ATP5G1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. HAMAP-Rule MF_01396

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. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity.

Subcellular location

Mitochondrion membrane; Multi-pass membrane protein HAMAP-Rule MF_01396.

Miscellaneous

There are three genes which encode the mitochondrial ATP synthase proteolipid and they specify precursors with different import sequences but identical mature proteins. Is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease).

Sequence similarities

Belongs to the ATPase C chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6161Mitochondrion HAMAP-Rule MF_01396
Chain62 – 13675ATP synthase F(0) complex subunit C1, mitochondrial HAMAP-Rule MF_01396
PRO_0000002557

Regions

Transmembrane77 – 9721Helical; Potential
Transmembrane112 – 13221Helical; Potential

Sites

Site1191Reversibly protonated during proton transport By similarity

Experimental info

Sequence conflict531E → G in AAA51806. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P05496 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 1AFF1F16BB532647

FASTA13614,277
        10         20         30         40         50         60 
MQTAGALFIS PALIRCCTRG LIRPVSASFL NSPVNSSKQP SYSNFPLQVA RREFQTSVVS 

        70         80         90        100        110        120 
RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA 

       130 
MGLFCLMVAF LILFAM 

« Hide

References

« Hide 'large scale' references
[1]"Sequences of members of the human gene family for the c subunit of mitochondrial ATP synthase."
Dyer M.R., Walker J.E.
Biochem. J. 293:51-64(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular cloning and sequence of two cDNAs for human subunit c of H(+)-ATP synthase in mitochondria."
Higuti T., Kawamura Y., Kuroiwa K., Miyazaki S., Tsujita H.
Biochim. Biophys. Acta 1173:87-90(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[6]"Human liver cDNA clones encoding proteolipid subunit 9 of the mitochondrial ATPase complex."
Farrell L.B., Nagley P.
Biochem. Biophys. Res. Commun. 144:1257-1264(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-136.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69907 Genomic DNA. Translation: CAA49532.1.
D13118 mRNA. Translation: BAA02420.1.
AL080089 mRNA. Translation: CAB45704.1.
BT007230 mRNA. Translation: AAP35894.1.
BC004963 mRNA. Translation: AAH04963.1.
M16453 mRNA. Translation: AAA51806.1.
PIRS34066.
RefSeqNP_001002027.1. NM_001002027.1.
NP_005166.1. NM_005175.2.
UniGeneHs.80986.

3D structure databases

ProteinModelPortalP05496.
SMRP05496. Positions 63-134.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107001. 1 interaction.
STRING9606.ENSP00000348205.

PTM databases

PhosphoSiteP05496.

Proteomic databases

PaxDbP05496.
PRIDEP05496.

Protocols and materials databases

DNASU516.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355938; ENSP00000348205; ENSG00000159199.
ENST00000393366; ENSP00000377033; ENSG00000159199.
GeneID516.
KEGGhsa:516.
UCSCuc002iog.3. human.

Organism-specific databases

CTD516.
GeneCardsGC17P046970.
HGNCHGNC:841. ATP5G1.
MIM603192. gene.
neXtProtNX_P05496.
PharmGKBPA25131.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0636.
HOGENOMHOG000235246.
HOVERGENHBG050605.
InParanoidP05496.
KOK02128.
OMAPPALIRC.
OrthoDBEOG7VHT0K.
PhylomeDBP05496.
TreeFamTF300140.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP05496.
BgeeP05496.
CleanExHS_ATP5G1.
GenevestigatorP05496.

Family and domain databases

Gene3D1.20.20.10. 1 hit.
HAMAPMF_01396. ATP_synth_c_bact.
InterProIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSPR00124. ATPASEC.
SUPFAMSSF81333. SSF81333. 1 hit.
PROSITEPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5G1. human.
GeneWikiATP5G1.
GenomeRNAi516.
NextBio2139.
PROP05496.
SOURCESearch...

Entry information

Entry nameAT5G1_HUMAN
AccessionPrimary (citable) accession number: P05496
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM