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P36542 (ATPG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene names
Name:ATP5C1
Synonyms:ATP5C, ATP5CL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processATP synthesis
Hydrogen ion transport
Ion transport
Transport
   Cellular componentCF(1)
Membrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Non-traceable author statement Ref.1. Source: UniProtKB

ATP catabolic process

Inferred from direct assay PubMed 12110673. Source: GOC

cellular metabolic process

Traceable author statement. Source: Reactome

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

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrial proton-transporting ATP synthase complex

Inferred from direct assay PubMed 12110673. Source: UniProtKB

mitochondrial proton-transporting ATP synthase complex, catalytic core F(1)

Non-traceable author statement Ref.1. Source: UniProtKB

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion
Chain26 – 298273ATP synthase subunit gamma, mitochondrial
PRO_0000002685

Amino acid modifications

Modified residue391N6-acetyllysine By similarity
Modified residue491N6-succinyllysine By similarity
Modified residue551N6-acetyllysine Ref.8
Modified residue1151N6-acetyllysine; alternate By similarity
Modified residue1151N6-succinyllysine; alternate By similarity
Modified residue1541N6-acetyllysine; alternate Ref.8
Modified residue1541N6-succinyllysine; alternate By similarity
Modified residue1971N6-acetyllysine Ref.8
Modified residue2701N6-succinyllysine By similarity

Natural variations

Alternative sequence2981Missing in isoform Heart.
VSP_000439

Experimental info

Sequence conflict451T → A in AAH16812. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform Liver (L) [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 021A95168FD53E04

FASTA29832,996
        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 

« Hide

Isoform Heart (H) [UniParc].

Checksum: CA95168FD53E0447
Show »

FASTA29732,881

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
CCDSCCDS31142.1. [P36542-1]
CCDS7081.1. [P36542-2]
PIRA49108.
RefSeqNP_001001973.1. NM_001001973.1. [P36542-1]
NP_005165.1. NM_005174.2. [P36542-2]
UniGeneHs.271135.

3D structure databases

ProteinModelPortalP36542.
SMRP36542. Positions 26-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106997. 51 interactions.
IntActP36542. 35 interactions.
MINTMINT-1378900.
STRING9606.ENSP00000349142.

PTM databases

PhosphoSiteP36542.

Polymorphism databases

DMDM543875.

2D gel databases

UCD-2DPAGEP36542.

Proteomic databases

MaxQBP36542.
PaxDbP36542.
PRIDEP36542.

Protocols and materials databases

DNASU509.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335698; ENSP00000338568; ENSG00000165629. [P36542-2]
ENST00000356708; ENSP00000349142; ENSG00000165629. [P36542-1]
GeneID509.
KEGGhsa:509.
UCSCuc001iju.3. human. [P36542-1]

Organism-specific databases

CTD509.
GeneCardsGC10P007830.
HGNCHGNC:833. ATP5C1.
HPAHPA060949.
MIM108729. gene.
neXtProtNX_P36542.
PharmGKBPA25125.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0224.
HOGENOMHOG000215911.
HOVERGENHBG000933.
InParanoidP36542.
KOK02136.
OMAMATLKDX.
OrthoDBEOG7QK0D3.
PhylomeDBP36542.
TreeFamTF105765.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP36542.
BgeeP36542.
CleanExHS_ATP5C1.
GenevestigatorP36542.

Family and domain databases

InterProIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERPTHR11693. PTHR11693. 1 hit.
PfamPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSPR00126. ATPASEGAMMA.
SUPFAMSSF52943. SSF52943. 1 hit.
TIGRFAMsTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5C1. human.
GeneWikiATP5C1.
GenomeRNAi509.
NextBio2117.
PROP36542.
SOURCESearch...

Entry information

Entry nameATPG_HUMAN
AccessionPrimary (citable) accession number: P36542
Secondary accession number(s): A8KA31 expand/collapse secondary AC list , Q5VYP3, Q6I9V2, Q96AS8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 146 of the entry and version 1 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 10

Human chromosome 10: entries, gene names and cross-references to MIM