P05496 (AT5G1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase lipid-binding protein, mitochondrial

Alternative name(s):
ATP synthase proteolipid P1
ATPase protein 9
ATPase subunit c

Gene names

Name:

ATP5G1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.
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.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	Lipid-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro mitochondrial ATP synthesis coupled proton transport Traceable author statement. Source: Reactome respiratory electron transport chain Traceable author statement. Source: Reactome
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial proton-transporting ATP synthase complex Inferred from sequence or structural similarity. Source: UniProtKB proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro lipid binding Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Non-traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 61	61	Mitochondrion
	Chain	62 – 136	75	ATP synthase lipid-binding protein, mitochondrial		PRO_0000002557
Regions
	Transmembrane	77 – 97	21	Helical; Potential
	Transmembrane	112 – 132	21	Helical; Potential
Sites
	Site	119	1	Reversibly protonated during proton transport By similarity
Experimental info
	Sequence conflict	53	1	E → G in AAA51806. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P05496 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 1AFF1F16BB532647	FASTA	136	14,277
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00009075.
PIR	S34066.
RefSeq	NP_001002027.1. NM_001002027.1. NP_005166.1. NM_005175.2.
UniGene	Hs.80986.
3D structure databases
ProteinModelPortal	P05496.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000348205.
PTM databases
PhosphoSite	P05496.
Polymorphism databases
DMDM	461588.
Proteomic databases
PaxDb	P05496.
PRIDE	P05496.
Protocols and materials databases
DNASU	516.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355938; ENSP00000348205; ENSG00000159199. ENST00000393366; ENSP00000377033; ENSG00000159199.
GeneID	516.
KEGG	hsa:516.
UCSC	uc002iog.3. human.
Organism-specific databases
CTD	516.
GeneCards	GC17P046970.
HGNC	HGNC:841. ATP5G1.
MIM	603192. gene.
neXtProt	NX_P05496.
PharmGKB	PA25131.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0636.
HOGENOM	HOG000235246.
HOVERGEN	HBG050605.
InParanoid	P05496.
KO	K02128.
OMA	PPALIRC.
OrthoDB	EOG41ZFCC.
PhylomeDB	P05496.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P05496.
Bgee	P05496.
CleanEx	HS_ATP5G1.
Genevestigator	P05496.
GermOnline	ENSG00000159199. Homo sapiens.
Family and domain databases
Gene3D	1.20.20.10. 1 hit.
InterPro	IPR000454. ATPase_F0-cplx_csu. IPR020537. ATPase_F0-cplx_csu_DDCD_BS. IPR002379. ATPase_proteolipid_c_like_dom. [Graphical view]
Pfam	PF00137. ATP-synt_C. 1 hit. [Graphical view]
PRINTS	PR00124. ATPASEC.
SUPFAM	SSF81333. ATPase_F0/V0_c. 1 hit.
PROSITE	PS00605. ATPASE_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP5G1. human.
GenomeRNAi	516.
NextBio	2139.
SOURCE	Search...

Entry information

Entry name

AT5G1_HUMAN

Accession

Primary (citable) accession number: P05496

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.