Reviewed, UniProtKB/Swiss-Prot P18859 (ATP5J_HUMAN)

Names and origin

Protein names

Recommended name:
    ATP synthase-coupling factor 6, mitochondrial
      Short name=ATPase subunit F6

Gene names

Name:	ATP5J
Synonyms:	ATP5A, ATPM

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	108 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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 and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
Subcellular location	Mitochondrion. Mitochondrion inner membrane.
Sequence similarities	Belongs to the eukaryotic ATPase subunit F6 family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: InterPro
Molecular function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 32	32	Mitochondrion Ref.7
	Chain	33 – 108	76	ATP synthase-coupling factor 6, mitochondrial		PRO_0000002527
Amino acid modifications
	Modified residue	41	1	N6-acetyllysine Ref.9
	Modified residue	46	1	N6-acetyllysine Ref.9
	Modified residue	99	1	N6-acetyllysine Ref.9
	Modified residue	105	1	N6-acetyllysine Ref.9
Experimental info
	Sequence conflict	68	1	Q → H in AAA58630. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P18859-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: EDC1A14F01A10F17	FASTA	108	12,588
	10 20 30 40 50 60 MILQRLFRFS SVIRSAVSVH LRRNIGVTAV AFNKELDPIQ KLFVDKIREY KSKRQTSGGP 70 80 90 100 VDASSEYQQE LERELFKLKQ MFGNADMNTF PTFKFEDPKF EVIEKPQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encoded precursor of coupling factor 6." Javed A.A., Ogata K., Sanadi D.R. Gene 97:307-310(1991) [PubMed: 1825642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning of cDNA for the import precursor of human coupling factor 6 of H(+)-ATP synthase in mitochondria." Higuti T., Tsurumi C., Kawamura Y., Tsujita H., Osaka F., Yoshihara Y., Tani I., Tanaka K., Ichihara A. Biochem. Biophys. Res. Commun. 178:793-799(1991) [PubMed: 1830479] [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: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[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 (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L. Nature 405:311-319(2000) [PubMed: 10830953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[7]	"Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed: 1286669] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-43. Tissue: Liver.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-46; LYS-99 AND LYS-105, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M37104 mRNA. Translation: AAA51807.1. M73031 mRNA. Translation: AAA58630.1. AL110183 mRNA. Translation: CAB53667.1. BT007244 mRNA. Translation: AAP35908.1. AP001694 Genomic DNA. No translation available. BC001178 mRNA. Translation: AAH01178.1.
IPI	IPI00002521.
PIR	JT0563.
RefSeq	NP_001003696.1. NP_001003697.1. NP_001003701.1. NP_001003703.1. NP_001676.2.
UniGene	Hs.246310
3D structure databases
SMR	P18859. Positions 33-108.
ModBase	Search...
Protein-protein interaction databases
STRING	P18859.
PTM databases
PhosphoSite	P18859.
2-D gel databases
SWISS-2DPAGE	P18859.
Proteomic databases
PRIDE	P18859.
Genome annotation databases
Ensembl	ENST00000284971; ENSP00000284971; ENSG00000154723; Homo sapiens. [Genome view] ENST00000400087; ENSP00000382959; ENSG00000154723; Homo sapiens. [Genome view] ENST00000400089; ENSP00000382961; ENSG00000154723; Homo sapiens. [Genome view] ENST00000400090; ENSP00000382962; ENSG00000154723; Homo sapiens. [Genome view] ENST00000400093; ENSP00000382965; ENSG00000154723; Homo sapiens. [Genome view] ENST00000400094; ENSP00000382966; ENSG00000154723; Homo sapiens. [Genome view] ENST00000400099; ENSP00000382971; ENSG00000154723; Homo sapiens. [Genome view] ENST00000434850; ENSP00000402597; ENSG00000154723; Homo sapiens. [Genome view] ENST00000457143; ENSP00000389649; ENSG00000154723; Homo sapiens. [Genome view]
GeneID	522.
KEGG	hsa:522.
UCSC	uc002yls.1. human.
Organism-specific databases
CTD	522.
GeneCards	GC21M026018.
H-InvDB	HIX0016040.
HGNC	HGNC:847. ATP5J.
MIM	603152. gene.
PharmGKB	PA25137.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P18859.
HOVERGEN	P18859.
OMA	DMNTFPN.
Enzyme and pathway databases
Pathway_Interaction_DB	hnf3apathway. FOXA1 transcription factor network.
Reactome	REACT_1505. Integration of energy metabolism. REACT_15380. Diabetes pathways. REACT_1698. Metablism of nucleotides.
Gene expression databases
ArrayExpress	P18859.
Bgee	P18859.
CleanEx	HS_ATP5J.
Genevestigator	P18859.
GermOnline	ENSG00000154723. Homo sapiens.
Family and domain databases
InterPro	IPR008387. ATPase_F0-cplx_f6su_mt. IPR016349. ATPase_F0-cplx_f6su_mt_subgr. [Graphical view]
PANTHER	PTHR12441. ATPase_F0_F6_mt. 1 hit.
Pfam	PF05511. ATP-synt_F6. 1 hit. [Graphical view]
PIRSF	PIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	2163.
SOURCE	Search...

Entry information

Entry name

ATP5J_HUMAN

Accession

Primary (citable) accession number: P18859

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	November 3, 2009
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.