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Protein

ATP synthase F(0) complex subunit C1, mitochondrial

Gene

Atp5g1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-163210. 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
ATPase protein 9
ATPase subunit c
Gene namesi
Name:Atp5g1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107653. Atp5g1.

Subcellular locationi

Topology

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

This protein is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease).

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6161MitochondrionAdd
BLAST
Chaini62 – 13675ATP synthase F(0) complex subunit C1, mitochondrialPRO_0000395412Add
BLAST

Proteomic databases

PaxDbiQ9CR84.

Expressioni

Gene expression databases

BgeeiQ9CR84.
GenevisibleiQ9CR84. MM.

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

STRINGi10090.ENSMUSP00000088029.

Structurei

3D structure databases

ProteinModelPortaliQ9CR84.
SMRiQ9CR84. Positions 63-134.
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.
InParanoidiQ9CR84.
KOiK02128.
OMAiNSSKQEC.
OrthoDBiEOG7VHT0K.
PhylomeDBiQ9CR84.
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.

Q9CR84-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTTKALLIS PALIRSCTRG LIRPVSASLL SRPEAPSKQP SCSSSPLQVA
60 70 80 90 100
RREFQTSVIS RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN
110 120 130
PSLKQQLFSY AILGFALSEA MGLFCLMVAF LILFAM
Length:136
Mass (Da):14,200
Last modified:June 1, 2001 - v1
Checksum:i12B9ABDEE627994C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121A → V in BAE39897 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008191 mRNA. Translation: BAB25522.1.
AK008998 mRNA. Translation: BAB26015.1.
AK009883 mRNA. Translation: BAB26561.1.
AK010868 mRNA. Translation: BAB27233.1.
AK011054 mRNA. Translation: BAB27363.1.
AK011432 mRNA. Translation: BAB27617.1.
AK167884 mRNA. Translation: BAE39897.1.
AL603682 Genomic DNA. Translation: CAM18271.1.
CH466556 Genomic DNA. Translation: EDL16011.1.
CH466556 Genomic DNA. Translation: EDL16012.1.
CH466556 Genomic DNA. Translation: EDL16013.1.
BC003854 mRNA. Translation: AAH03854.1.
BC094664 mRNA. Translation: AAH94664.1.
CCDSiCCDS25289.1.
RefSeqiNP_001154891.1. NM_001161419.1.
NP_031532.2. NM_007506.6.
UniGeneiMm.258.

Genome annotation databases

EnsembliENSMUST00000090541; ENSMUSP00000088029; ENSMUSG00000006057.
ENSMUST00000107684; ENSMUSP00000103312; ENSMUSG00000006057.
ENSMUST00000107686; ENSMUSP00000103314; ENSMUSG00000006057.
ENSMUST00000178611; ENSMUSP00000137633; ENSMUSG00000006057.
GeneIDi11951.
KEGGimmu:11951.
UCSCiuc007lbf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008191 mRNA. Translation: BAB25522.1.
AK008998 mRNA. Translation: BAB26015.1.
AK009883 mRNA. Translation: BAB26561.1.
AK010868 mRNA. Translation: BAB27233.1.
AK011054 mRNA. Translation: BAB27363.1.
AK011432 mRNA. Translation: BAB27617.1.
AK167884 mRNA. Translation: BAE39897.1.
AL603682 Genomic DNA. Translation: CAM18271.1.
CH466556 Genomic DNA. Translation: EDL16011.1.
CH466556 Genomic DNA. Translation: EDL16012.1.
CH466556 Genomic DNA. Translation: EDL16013.1.
BC003854 mRNA. Translation: AAH03854.1.
BC094664 mRNA. Translation: AAH94664.1.
CCDSiCCDS25289.1.
RefSeqiNP_001154891.1. NM_001161419.1.
NP_031532.2. NM_007506.6.
UniGeneiMm.258.

3D structure databases

ProteinModelPortaliQ9CR84.
SMRiQ9CR84. Positions 63-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000088029.

Proteomic databases

PaxDbiQ9CR84.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090541; ENSMUSP00000088029; ENSMUSG00000006057.
ENSMUST00000107684; ENSMUSP00000103312; ENSMUSG00000006057.
ENSMUST00000107686; ENSMUSP00000103314; ENSMUSG00000006057.
ENSMUST00000178611; ENSMUSP00000137633; ENSMUSG00000006057.
GeneIDi11951.
KEGGimmu:11951.
UCSCiuc007lbf.2. mouse.

Organism-specific databases

CTDi516.
MGIiMGI:107653. Atp5g1.

Phylogenomic databases

eggNOGiKOG3025. Eukaryota.
COG0636. LUCA.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235246.
HOVERGENiHBG050605.
InParanoidiQ9CR84.
KOiK02128.
OMAiNSSKQEC.
OrthoDBiEOG7VHT0K.
PhylomeDBiQ9CR84.
TreeFamiTF300140.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ9CR84.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CR84.
GenevisibleiQ9CR84. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ and C57BL/6J.
    Tissue: Liver, Small intestine and Tongue.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary tumor.

Entry informationi

Entry nameiAT5G1_MOUSE
AccessioniPrimary (citable) accession number: Q9CR84
Secondary accession number(s): Q3TIE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.