P36542 (ATPG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit gamma, mitochondrial

Alternative name(s):
F-ATPase gamma subunit

Gene names

Name:	ATP5C1
Synonyms:	ATP5C, ATP5CL1

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	298 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 F1 domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
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. Mitochondrion inner membrane; Peripheral membrane protein By similarity.
Tissue specificity	Isoform Heart is expressed specifically in the heart and skeletal muscle, which require rapid energy supply. Isoform Liver is expressed in the brain, liver and kidney. Isoform Heart and Isoform Liver are expressed in the skin, intestine, stomach and aorta.
Sequence similarities	Belongs to the ATPase gamma chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay PubMed 12110673. Source: GOC mitochondrial ATP synthesis coupled proton transport Inferred by curator PubMed 12110673. Source: UniProtKB oxidative phosphorylation Non-traceable author statement Ref.1. Source: UniProtKB respiratory electron transport chain Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro transmembrane transporter activity Inferred by curator PubMed 12110673. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Liver (identifier: P36542-1)

Also known as: L;

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 Heart (identifier: P36542-2)

Also known as: H;

The sequence of this isoform differs from the canonical sequence as follows:
     298-298: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion
	Chain	26 – 298	273	ATP synthase subunit gamma, mitochondrial		PRO_0000002685
Amino acid modifications
	Modified residue	55	1	N6-acetyllysine Ref.8
	Modified residue	79	1	N6-acetyllysine By similarity
	Modified residue	90	1	N6-acetyllysine By similarity
	Modified residue	115	1	N6-acetyllysine By similarity
	Modified residue	146	1	Phosphoserine By similarity
	Modified residue	154	1	N6-acetyllysine Ref.8
	Modified residue	197	1	N6-acetyllysine Ref.8
Natural variations
	Alternative sequence	298	1	Missing in isoform Heart.		VSP_000439
Experimental info
	Sequence conflict	45	1	T → A in AAH16812. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform Liver (L) [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 021A95168FD53E04	FASTA	298	32,996
	10 20 30 40 50 60 MFSRAGVAGL SAWTLQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE 70 80 90 100 110 120 RELKPARIYG LGSLALYEKA DIKGPEDKKK HLLIGVSSDR GLCGAIHSSI AKQMKSEVAT 130 140 150 160 170 180 LTAAGKEVML VGIGDKIRGI LYRTHSDQFL VAFKEVGRKP PTFGDASVIA LELLNSGYEF 190 200 210 220 230 240 DEGSIIFNKF RSVISYKTEE KPIFSLNTVA SADSMSIYDD IDADVLQNYQ EYNLANIIYY 250 260 270 280 290 SLKESTTSEQ SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD
	Isoform Heart (H) [UniParc]. Checksum: CA95168FD53E0447	FASTA	297	32,881
	10 20 30 40 50 60 MFSRAGVAGL SAWTLQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE 70 80 90 100 110 120 RELKPARIYG LGSLALYEKA DIKGPEDKKK HLLIGVSSDR GLCGAIHSSI AKQMKSEVAT 130 140 150 160 170 180 LTAAGKEVML VGIGDKIRGI LYRTHSDQFL VAFKEVGRKP PTFGDASVIA LELLNSGYEF 190 200 210 220 230 240 DEGSIIFNKF RSVISYKTEE KPIFSLNTVA SADSMSIYDD IDADVLQNYQ EYNLANIIYY 250 260 270 280 290 SLKESTTSEQ SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene structure of human mitochondrial ATP synthase gamma-subunit. Tissue specificity produced by alternative RNA splicing." Matsuda C., Endo H., Ohta S., Kagawa Y. J. Biol. Chem. 268:24950-24958(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS HEART AND LIVER). Tissue: Heart and Liver.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HEART). Tissue: Trachea.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LIVER).
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LIVER). Tissue: Liver, Muscle, Placenta and Urinary bladder.
[7]	Bienvenut W.V., Glen H., Frame M.C. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 68-79; 116-126; 144-154; 263-277 AND 286-298, MASS SPECTROMETRY. Tissue: Osteosarcoma.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-154 AND LYS-197, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16561 Genomic DNA. Translation: BAA03994.1. D16561 Genomic DNA. Translation: BAA03995.1. D16562 mRNA. Translation: BAA03996.1. D16563 mRNA. Translation: BAA03997.1. AK292896 mRNA. Translation: BAF85585.1. CR457403 mRNA. Translation: CAG33684.1. AL353754, AL158044 Genomic DNA. Translation: CAH73453.1. AL353754, AL158044 Genomic DNA. Translation: CAH73454.1. AL158044, AL353754 Genomic DNA. Translation: CAI12960.1. AL158044, AL353754 Genomic DNA. Translation: CAI12961.1. CH471072 Genomic DNA. Translation: EAW86372.1. CH471072 Genomic DNA. Translation: EAW86373.1. BC000470 mRNA. Translation: AAH00470.1. BC000931 mRNA. Translation: AAH00931.1. BC013394 mRNA. Translation: AAH13394.1. BC016812 mRNA. Translation: AAH16812.1. BC020824 mRNA. Translation: AAH20824.1.
IPI	IPI00395769. IPI00478410.
PIR	A49108.
RefSeq	NP_001001973.1. NM_001001973.1. NP_005165.1. NM_005174.2.
UniGene	Hs.271135.
3D structure databases
ProteinModelPortal	P36542.
ModBase	Search...
Protein-protein interaction databases
IntAct	P36542. 29 interactions.
MINT	MINT-1378900.
STRING	9606.ENSP00000349142.
PTM databases
PhosphoSite	P36542.
Polymorphism databases
DMDM	543875.
2D gel databases
UCD-2DPAGE	P36542.
Proteomic databases
PaxDb	P36542.
PRIDE	P36542.
Protocols and materials databases
DNASU	509.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000335698; ENSP00000338568; ENSG00000165629. ENST00000356708; ENSP00000349142; ENSG00000165629.
GeneID	509.
KEGG	hsa:509.
UCSC	uc001iju.3. human.
Organism-specific databases
CTD	509.
GeneCards	GC10P007830.
HGNC	HGNC:833. ATP5C1.
MIM	108729. gene.
neXtProt	NX_P36542.
PharmGKB	PA25125.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0224.
HOGENOM	HOG000215911.
HOVERGEN	HBG000933.
InParanoid	P36542.
KO	K02136.
OMA	QQRGMAT.
OrthoDB	EOG4FJ899.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	P36542.
Bgee	P36542.
CleanEx	HS_ATP5C1.
Genevestigator	P36542.
GermOnline	ENSG00000165629. Homo sapiens.
Family and domain databases
InterPro	IPR000131. ATPase_F1-cplx_gsu. IPR023632. ATPase_F1_gsu_CS. IPR023633. ATPase_F1_gsu_dom. [Graphical view]
PANTHER	PTHR11693. PTHR11693. 1 hit.
Pfam	PF00231. ATP-synt. 1 hit. [Graphical view]
PRINTS	PR00126. ATPASEGAMMA.
SUPFAM	SSF52943. ATPase_gamma. 1 hit.
TIGRFAMs	TIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITE	PS00153. ATPASE_GAMMA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP5C1. human.
GenomeRNAi	509.
NextBio	2117.
SOURCE	Search...

Entry information

Entry name

ATPG_HUMAN

Accession

Primary (citable) accession number: P36542
Secondary accession number(s): A8KA31 , Q5VYP3, Q6I9V2, Q96AS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 135 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.