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P05496

- AT5G1_HUMAN

UniProt

P05496 - AT5G1_HUMAN

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Protein

ATP synthase F(0) complex subunit C1, mitochondrial

Gene

ATP5G1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei119 – 1191Reversibly protonated during proton transportBy similarity

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro
  2. lipid binding Source: UniProtKB-KW
  3. transporter activity Source: ProtInc

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. cellular metabolic process Source: Reactome
  3. mitochondrial ATP synthesis coupled proton transport Source: Reactome
  4. respiratory electron transport chain Source: Reactome
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.
REACT_6759. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase F(0) complex subunit C1, mitochondrial
Alternative name(s):
ATP synthase lipid-binding protein
ATP synthase proteolipid P1
ATP synthase proton-transporting mitochondrial F(0) complex subunit C1
ATPase protein 9
ATPase subunit c
Gene namesi
Name:ATP5G1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:841. ATP5G1.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: Reactome
  3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  4. mitochondrion Source: LIFEdb
  5. proton-transporting ATP synthase complex, coupling factor F(o) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25131.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6161MitochondrionAdd
BLAST
Chaini62 – 13675ATP synthase F(0) complex subunit C1, mitochondrialPRO_0000002557Add
BLAST

Proteomic databases

MaxQBiP05496.
PaxDbiP05496.
PRIDEiP05496.

PTM databases

PhosphoSiteiP05496.

Expressioni

Gene expression databases

BgeeiP05496.
CleanExiHS_ATP5G1.
ExpressionAtlasiP05496. baseline and differential.
GenevestigatoriP05496.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi107001. 5 interactions.
STRINGi9606.ENSP00000348205.

Structurei

3D structure databases

ProteinModelPortaliP05496.
SMRiP05496. Positions 63-134.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei77 – 9721HelicalSequence AnalysisAdd
BLAST
Transmembranei112 – 13221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0636.
HOGENOMiHOG000235246.
HOVERGENiHBG050605.
InParanoidiP05496.
KOiK02128.
OrthoDBiEOG7VHT0K.
PhylomeDBiP05496.
TreeFamiTF300140.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05496-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQTAGALFIS PALIRCCTRG LIRPVSASFL NSPVNSSKQP SYSNFPLQVA
60 70 80 90 100
RREFQTSVVS RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN
110 120 130
PSLKQQLFSY AILGFALSEA MGLFCLMVAF LILFAM
Length:136
Mass (Da):14,277
Last modified:February 1, 1994 - v2
Checksum:i1AFF1F16BB532647
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531E → G in AAA51806. (PubMed:2883974)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11539.1.
PIRiS34066.
RefSeqiNP_001002027.1. NM_001002027.1.
NP_005166.1. NM_005175.2.
UniGeneiHs.80986.

Genome annotation databases

EnsembliENST00000355938; ENSP00000348205; ENSG00000159199.
ENST00000393366; ENSP00000377033; ENSG00000159199.
GeneIDi516.
KEGGihsa:516.
UCSCiuc002iog.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11539.1.
PIRi S34066.
RefSeqi NP_001002027.1. NM_001002027.1.
NP_005166.1. NM_005175.2.
UniGenei Hs.80986.

3D structure databases

ProteinModelPortali P05496.
SMRi P05496. Positions 63-134.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107001. 5 interactions.
STRINGi 9606.ENSP00000348205.

PTM databases

PhosphoSitei P05496.

Proteomic databases

MaxQBi P05496.
PaxDbi P05496.
PRIDEi P05496.

Protocols and materials databases

DNASUi 516.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355938 ; ENSP00000348205 ; ENSG00000159199 .
ENST00000393366 ; ENSP00000377033 ; ENSG00000159199 .
GeneIDi 516.
KEGGi hsa:516.
UCSCi uc002iog.3. human.

Organism-specific databases

CTDi 516.
GeneCardsi GC17P046970.
HGNCi HGNC:841. ATP5G1.
MIMi 603192. gene.
neXtProti NX_P05496.
PharmGKBi PA25131.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0636.
HOGENOMi HOG000235246.
HOVERGENi HBG050605.
InParanoidi P05496.
KOi K02128.
OrthoDBi EOG7VHT0K.
PhylomeDBi P05496.
TreeFami TF300140.

Enzyme and pathway databases

Reactomei REACT_118595. Mitochondrial protein import.
REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSi ATP5G1. human.
GeneWikii ATP5G1.
GenomeRNAii 516.
NextBioi 2139.
PROi P05496.
SOURCEi Search...

Gene expression databases

Bgeei P05496.
CleanExi HS_ATP5G1.
ExpressionAtlasi P05496. baseline and differential.
Genevestigatori P05496.

Family and domain databases

Gene3Di 1.20.20.10. 1 hit.
HAMAPi MF_01396. ATP_synth_c_bact.
InterProi IPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view ]
Pfami PF00137. ATP-synt_C. 1 hit.
[Graphical view ]
PRINTSi PR00124. ATPASEC.
SUPFAMi SSF81333. SSF81333. 1 hit.
PROSITEi PS00605. ATPASE_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiAT5G1_HUMAN
AccessioniPrimary (citable) accession number: P05496
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1994
Last modified: October 29, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3