Q06055 (AT5G2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase lipid-binding protein, mitochondrial

Alternative name(s):
ATP synthase proteolipid P2
ATPase protein 9
ATPase subunit c

Gene names

Name:	ATP5G2
ORF Names:	PSEC0033

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	141 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.
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
Coding sequence diversity	Alternative splicing Polymorphism
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 ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro response to ethanol Inferred from electronic annotation. Source: Compara
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial proton-transporting ATP synthase complex Traceable author statement Ref.1. Source: ProtInc 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...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q06055-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q06055-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPELILYVAITLSVAERLVGPGHACAEPSFRSSRCSAPLCLLCSGSSSPATAPHPLKM

Note: Derived from EST data.

Isoform 3 (identifier: Q06055-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPELILSPATAPHPLKM

Note: Derived from EST data.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 66	66	Mitochondrion By similarity
	Chain	67 – 141	75	ATP synthase lipid-binding protein, mitochondrial		PRO_0000002562
Regions
	Transmembrane	82 – 102	21	Helical; Potential
	Transmembrane	117 – 137	21	Helical; Potential
Sites
	Site	124	1	Reversibly protonated during proton transport By similarity
Natural variations
	Alternative sequence	1	1	M → MPELILYVAITLSVAERLVG PGHACAEPSFRSSRCSAPLC LLCSGSSSPATAPHPLKM in isoform 2.		VSP_037348
	Alternative sequence	1	1	M → MPELILSPATAPHPLKM in isoform 3.		VSP_037349
	Natural variant	58	1	S → I. Corresponds to variant rs13819 [ dbSNP | Ensembl ].		VAR_011920
	Natural variant	141	1	M → K. Corresponds to variant rs1803177 [ dbSNP | Ensembl ].		VAR_011921
Experimental info
	Sequence conflict	63	1	A → T in BAG52118. Ref.3
	Sequence conflict	107	1	S → F in BAG52118. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 6E627A504A7AE52D	FASTA	141	14,637
	10 20 30 40 50 60 MFACSKFVST PSLVKSTSQL LSRPLSAVVL KRPEILTDES LSSLAVSCPL TSLVSSRSFQ 70 80 90 100 110 120 TSAISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII GYARNPSLKQ QLFSYAILGF 130 140 ALSEAMGLFC LMVAFLILFA M
	Isoform 2 [UniParc]. Checksum: 6ACCBD405F313CC8	FASTA	198	20,513
	10 20 30 40 50 60 MPELILYVAI TLSVAERLVG PGHACAEPSF RSSRCSAPLC LLCSGSSSPA TAPHPLKMFA 70 80 90 100 110 120 CSKFVSTPSL VKSTSQLLSR PLSAVVLKRP EILTDESLSS LAVSCPLTSL VSSRSFQTSA 130 140 150 160 170 180 ISRDIDTAAK FIGAGAATVG VAGSGAGIGT VFGSLIIGYA RNPSLKQQLF SYAILGFALS 190 EAMGLFCLMV AFLILFAM
	Isoform 3 [UniParc]. Checksum: 84032DCC16E10CED	FASTA	157	16,334
	10 20 30 40 50 60 MPELILSPAT APHPLKMFAC SKFVSTPSLV KSTSQLLSRP LSAVVLKRPE ILTDESLSSL 70 80 90 100 110 120 AVSCPLTSLV SSRSFQTSAI SRDIDTAAKF IGAGAATVGV AGSGAGIGTV FGSLIIGYAR 130 140 150 NPSLKQQLFS YAILGFALSE AMGLFCLMVA FLILFAM

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] (ISOFORM 1).
[3]	"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries." Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T. DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1). 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 87-141 (ISOFORMS 1/2/3). Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X69908 Genomic DNA. Translation: CAA49533.1. D13119 mRNA. Translation: BAA02421.1. AK075351 mRNA. Translation: BAG52118.1. AC073594 Genomic DNA. No translation available. BC020826 mRNA. Translation: AAH20826.1.
IPI	IPI00028482. IPI00456749. IPI00792819.
PIR	S34067.
RefSeq	NP_001002031.1. NM_001002031.2. NP_005167.2. NM_005176.5.
UniGene	Hs.524464.
3D structure databases
ProteinModelPortal	Q06055.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q06055. 2 interactions.
STRING	9606.ENSP00000377878.
PTM databases
PhosphoSite	Q06055.
Polymorphism databases
DMDM	461592.
Proteomic databases
PaxDb	Q06055.
PRIDE	Q06055.
Protocols and materials databases
DNASU	517.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000338662; ENSP00000340315; ENSG00000135390. ENST00000394349; ENSP00000377878; ENSG00000135390. ENST00000549164; ENSP00000447317; ENSG00000135390.
GeneID	517.
KEGG	hsa:517.
UCSC	uc001sec.3. human. uc001sed.3. human. uc009znc.3. human.
Organism-specific databases
CTD	517.
GeneCards	GC12M054029.
H-InvDB	HIX0201895.
HGNC	HGNC:842. ATP5G2.
HPA	HPA051469.
MIM	603193. gene.
neXtProt	NX_Q06055.
PharmGKB	PA25132.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0636.
HOGENOM	HOG000235246.
HOVERGEN	HBG050605.
InParanoid	Q06055.
KO	K02128.
OMA	HPLKMYT.
OrthoDB	EOG4X0MTN.
PhylomeDB	Q06055.
Gene expression databases
ArrayExpress	Q06055.
Bgee	Q06055.
CleanEx	HS_ATP5G2.
Genevestigator	Q06055.
GermOnline	ENSG00000135390. 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	ATP5G2. human.
GenomeRNAi	517.
NextBio	2145.
SOURCE	Search...

Entry information

Entry name

AT5G2_HUMAN

Accession

Primary (citable) accession number: Q06055
Secondary accession number(s): B3KQQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 127 of the entry and version 1 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.