ATP synthase lipid-binding protein, mitochondrial precursor

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P05496 (AT5G1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ATP synthase lipid-binding protein, mitochondrial

Alternative name(s):
ATP synthase proteolipid P1
ATPase protein 9
ATPase subunit c

Gene names

Name:

ATP5G1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	136 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
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 mitochondrial ATP synthesis coupled proton transport Traceable author statement. Source: Reactome respiratory electron transport chain Traceable author statement. Source: Reactome
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial proton-transporting ATP synthase complex Traceable author statement. 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 61

Mitochondrion

Chain

62 – 136

ATP synthase lipid-binding protein, mitochondrial

PRO_0000002557

Regions

Transmembrane

77 – 97

Helical; Potential

Transmembrane

112 – 132

Helical; Potential

Sites

Site

119

Reversibly protonated during proton transport By similarity

Experimental info

Sequence conflict

E → G in AAA51806. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P05496 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 1AFF1F16BB532647
Show »

FASTA

136

14,277

        10         20         30         40         50         60 
MQTAGALFIS PALIRCCTRG LIRPVSASFL NSPVNSSKQP SYSNFPLQVA RREFQTSVVS 

        70         80         90        100        110        120 
RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA 

       130 
MGLFCLMVAF LILFAM

« Hide

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: 8328972] [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: 8485160] [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. Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] 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: 15489334] [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: 2883974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-136. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00009075.
PIR	S34066.
RefSeq	NP_001002027.1. NM_001002027.1. NP_005166.1. NM_005175.2.
UniGene	Hs.80986.
3D structure databases
ProteinModelPortal	P05496.
SMR	P05496. Positions 63-134.
ModBase	Search...
Protein-protein interaction databases
STRING	P05496.
Polymorphism databases
DMDM	461588.
Proteomic databases
PRIDE	P05496.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355938; ENSP00000348205; ENSG00000159199. ENST00000393366; ENSP00000377033; ENSG00000159199.
GeneID	516.
KEGG	hsa:516.
UCSC	uc002iog.1. human.
Organism-specific databases
CTD	516.
GeneCards	GC17P046970.
H-InvDB	HIX0202455.
HGNC	HGNC:841. ATP5G1.
MIM	603192. gene.
neXtProt	NX_P05496.
PharmGKB	PA25131.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20701.
HOGENOM	HBG753983.
HOVERGEN	HBG050605.
InParanoid	P05496.
OMA	PALXPSY.
OrthoDB	EOG41ZFCC.
PhylomeDB	P05496.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	P05496.
Bgee	P05496.
CleanEx	HS_ATP5G1.
Genevestigator	P05496.
GermOnline	ENSG00000159199. Homo sapiens.
Family and domain databases
InterPro	IPR000454. ATPase_F0-cplx_csu. IPR020537. ATPase_F0-cplx_csu_DDCD_BS. IPR002379. ATPase_F0/V0-cplx_csu. [Graphical view]
Gene3D	G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.
KO	K02128.
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
NextBio	2139.
SOURCE	Search...

Entry information

Entry name

AT5G1_HUMAN

Accession

Primary (citable) accession number: P05496

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 125 of the entry and version 2 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.

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents