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Protein

ATP synthase F(0) complex subunit C3, mitochondrial

Gene

ATP5G3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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
Sitei125 – 1251Reversibly protonated during proton transportBy similarity

GO - Molecular functioni

  • hydrogen ion transmembrane transporter activity Source: InterPro
  • lipid binding Source: UniProtKB-KW
  • transporter activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-163210. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase F(0) complex subunit C3, mitochondrial
Alternative name(s):
ATP synthase lipid-binding protein
ATP synthase proteolipid P3
ATP synthase proton-transporting mitochondrial F(0) complex subunit C3
ATPase protein 9
ATPase subunit c
Gene namesi
Name:ATP5G3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:843. ATP5G3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei83 – 10321HelicalSequence analysisAdd
BLAST
Transmembranei118 – 13821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25133.

Polymorphism and mutation databases

BioMutaiATP5G3.
DMDMi1352048.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6767MitochondrionAdd
BLAST
Chaini68 – 14275ATP synthase F(0) complex subunit C3, mitochondrialPRO_0000002567Add
BLAST

Proteomic databases

EPDiP48201.
PaxDbiP48201.
PRIDEiP48201.
TopDownProteomicsiP48201.

PTM databases

iPTMnetiP48201.
PhosphoSiteiP48201.

Expressioni

Gene expression databases

BgeeiP48201.
CleanExiHS_ATP5G3.
GenevisibleiP48201. HS.

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.

Protein-protein interaction databases

BioGridi107003. 9 interactions.
IntActiP48201. 1 interaction.
MINTiMINT-1036155.
STRINGi9606.ENSP00000284727.

Structurei

3D structure databases

ProteinModelPortaliP48201.
SMRiP48201. Positions 69-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3025. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235246.
HOVERGENiHBG050605.
InParanoidiP48201.
KOiK02128.
OMAiCKMFACA.
OrthoDBiEOG7VHT0K.
PhylomeDBiP48201.
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.

P48201-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFACAKLACT PSLIRAGSRV AYRPISASVL SRPEASRTGE GSTVFNGAQN
60 70 80 90 100
GVSQLIQREF QTSAISRDID TAAKFIGAGA ATVGVAGSGA GIGTVFGSLI
110 120 130 140
IGYARNPSLK QQLFSYAILG FALSEAMGLF CLMVAFLILF AM
Length:142
Mass (Da):14,693
Last modified:February 1, 1996 - v1
Checksum:i19EC0D1710A0AA3F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931G → E.
Corresponds to variant rs1802622 [ dbSNP | Ensembl ].
VAR_011922

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09813 mRNA. Translation: AAA78807.1.
AK311999 mRNA. Translation: BAG34937.1.
AC096649 Genomic DNA. Translation: AAX88970.1.
CH471058 Genomic DNA. Translation: EAX11106.1.
CH471058 Genomic DNA. Translation: EAX11107.1.
BC106881 mRNA. Translation: AAI06882.1.
CCDSiCCDS2263.1.
PIRiI38612.
RefSeqiNP_001002258.1. NM_001002258.4.
NP_001680.1. NM_001689.4.
UniGeneiHs.429.

Genome annotation databases

EnsembliENST00000284727; ENSP00000284727; ENSG00000154518.
ENST00000392541; ENSP00000376324; ENSG00000154518.
ENST00000409194; ENSP00000387317; ENSG00000154518.
GeneIDi518.
KEGGihsa:518.
UCSCiuc002ujz.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09813 mRNA. Translation: AAA78807.1.
AK311999 mRNA. Translation: BAG34937.1.
AC096649 Genomic DNA. Translation: AAX88970.1.
CH471058 Genomic DNA. Translation: EAX11106.1.
CH471058 Genomic DNA. Translation: EAX11107.1.
BC106881 mRNA. Translation: AAI06882.1.
CCDSiCCDS2263.1.
PIRiI38612.
RefSeqiNP_001002258.1. NM_001002258.4.
NP_001680.1. NM_001689.4.
UniGeneiHs.429.

3D structure databases

ProteinModelPortaliP48201.
SMRiP48201. Positions 69-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107003. 9 interactions.
IntActiP48201. 1 interaction.
MINTiMINT-1036155.
STRINGi9606.ENSP00000284727.

PTM databases

iPTMnetiP48201.
PhosphoSiteiP48201.

Polymorphism and mutation databases

BioMutaiATP5G3.
DMDMi1352048.

Proteomic databases

EPDiP48201.
PaxDbiP48201.
PRIDEiP48201.
TopDownProteomicsiP48201.

Protocols and materials databases

DNASUi518.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284727; ENSP00000284727; ENSG00000154518.
ENST00000392541; ENSP00000376324; ENSG00000154518.
ENST00000409194; ENSP00000387317; ENSG00000154518.
GeneIDi518.
KEGGihsa:518.
UCSCiuc002ujz.5. human.

Organism-specific databases

CTDi518.
GeneCardsiATP5G3.
HGNCiHGNC:843. ATP5G3.
MIMi602736. gene.
neXtProtiNX_P48201.
PharmGKBiPA25133.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3025. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235246.
HOVERGENiHBG050605.
InParanoidiP48201.
KOiK02128.
OMAiCKMFACA.
OrthoDBiEOG7VHT0K.
PhylomeDBiP48201.
TreeFamiTF300140.

Enzyme and pathway databases

ReactomeiR-HSA-163210. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiATP5G3. human.
GeneWikiiATP5G3.
GenomeRNAii518.
PROiP48201.
SOURCEiSearch...

Gene expression databases

BgeeiP48201.
CleanExiHS_ATP5G3.
GenevisibleiP48201. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3)."
    Yan W.L., Lerner T.J., Haines J.L., Gusella J.F.
    Genomics 24:375-377(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: 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].
    Tissue: Subthalamic nucleus.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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].

Entry informationi

Entry nameiAT5G3_HUMAN
AccessioniPrimary (citable) accession number: P48201
Secondary accession number(s): B2R4Z0, D3DPF0, Q4ZFX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 141 of the entry and version 1 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.