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ATP synthase F(0) complex subunit C1, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase proteolipid P1) (ATPase protein 9) (ATPase subunit c)

 AT5G1_MOUSE             Reviewed;         136 AA.
Q9CR84; Q3TIE9;
13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
23-MAY-2018, entry version 128.
RecName: Full=ATP synthase F(0) complex subunit C1, mitochondrial {ECO:0000305};
AltName: Full=ATP synthase lipid-binding protein;
AltName: Full=ATP synthase membrane subunit c locus 1 {ECO:0000250|UniProtKB:P05496};
AltName: Full=ATP synthase proteolipid P1;
AltName: Full=ATPase protein 9;
AltName: Full=ATPase subunit c;
Flags: Precursor;
Name=Atp5mc1 {ECO:0000250|UniProtKB:P05496}; Synonyms=Atp5g1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=BALB/cJ, and C57BL/6J;
TISSUE=Liver, Small intestine, and Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) 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, F(1) - containing the
extramembraneous catalytic core and F(0) - containing the membrane
proton channel, linked together by a central stalk and a
peripheral stalk. During catalysis, ATP synthesis in the catalytic
domain of F(1) is coupled via a rotary mechanism of the central
stalk subunits to proton translocation. Part of the complex F(0)
domain. A homomeric c-ring of probably 10 subunits is part of the
complex rotary element (By similarity). {ECO:0000250}.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
has three main subunits: a, b and c. Component of an ATP synthase
complex composed of ATP5F1, ATP5MC1, ATP5F1E, ATP5H, ATP5I, ATP5J,
ATP5J2, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
ATP5O, ATP5L, USMG5 and MP68 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-
pass membrane protein {ECO:0000250}.
-!- DISEASE: Note=This protein is the major protein stored in the
storage bodies of animals or humans affected with ceroid
lipofuscinosis (Batten disease).
-!- MISCELLANEOUS: There are three genes which encode the
mitochondrial ATP synthase proteolipid and they specify precursors
with different import sequences but identical mature proteins.
{ECO:0000305}.
-!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK008191; BAB25522.1; -; mRNA.
EMBL; AK008998; BAB26015.1; -; mRNA.
EMBL; AK009883; BAB26561.1; -; mRNA.
EMBL; AK010868; BAB27233.1; -; mRNA.
EMBL; AK011054; BAB27363.1; -; mRNA.
EMBL; AK011432; BAB27617.1; -; mRNA.
EMBL; AK167884; BAE39897.1; -; mRNA.
EMBL; AL603682; CAM18271.1; -; Genomic_DNA.
EMBL; CH466556; EDL16011.1; -; Genomic_DNA.
EMBL; CH466556; EDL16012.1; -; Genomic_DNA.
EMBL; CH466556; EDL16013.1; -; Genomic_DNA.
EMBL; BC003854; AAH03854.1; -; mRNA.
EMBL; BC094664; AAH94664.1; -; mRNA.
CCDS; CCDS25289.1; -.
RefSeq; NP_001154891.1; NM_001161419.1.
RefSeq; NP_031532.2; NM_007506.6.
UniGene; Mm.258; -.
ProteinModelPortal; Q9CR84; -.
SMR; Q9CR84; -.
STRING; 10090.ENSMUSP00000088029; -.
PhosphoSitePlus; Q9CR84; -.
PaxDb; Q9CR84; -.
PRIDE; Q9CR84; -.
Ensembl; ENSMUST00000090541; ENSMUSP00000088029; ENSMUSG00000006057.
Ensembl; ENSMUST00000107684; ENSMUSP00000103312; ENSMUSG00000006057.
Ensembl; ENSMUST00000107686; ENSMUSP00000103314; ENSMUSG00000006057.
Ensembl; ENSMUST00000178611; ENSMUSP00000137633; ENSMUSG00000006057.
GeneID; 11951; -.
KEGG; mmu:11951; -.
UCSC; uc007lbf.2; mouse.
CTD; 11951; -.
MGI; MGI:107653; Atp5g1.
eggNOG; KOG3025; Eukaryota.
eggNOG; COG0636; LUCA.
GeneTree; ENSGT00390000006210; -.
HOGENOM; HOG000235246; -.
HOVERGEN; HBG050605; -.
InParanoid; Q9CR84; -.
KO; K02128; -.
OMA; IRCCTRD; -.
OrthoDB; EOG091G13J1; -.
PhylomeDB; Q9CR84; -.
TreeFam; TF300140; -.
PRO; PR:Q9CR84; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000006057; -.
Genevisible; Q9CR84; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
Gene3D; 1.20.20.10; -; 1.
HAMAP; MF_01396; ATP_synth_c_bact; 1.
InterPro; IPR000454; ATP_synth_F0_csu.
InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
InterPro; IPR038662; ATP_synth_F0_csu_sf.
InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
InterPro; IPR035921; F/V-ATP_Csub_sf.
PANTHER; PTHR10031; PTHR10031; 1.
Pfam; PF00137; ATP-synt_C; 1.
PRINTS; PR00124; ATPASEC.
SUPFAM; SSF81333; SSF81333; 1.
PROSITE; PS00605; ATPASE_C; 1.
2: Evidence at transcript level;
CF(0); Complete proteome; Hydrogen ion transport; Ion transport;
Lipid-binding; Membrane; Mitochondrion; Reference proteome;
Transit peptide; Transmembrane; Transmembrane helix; Transport.
TRANSIT 1 61 Mitochondrion.
CHAIN 62 136 ATP synthase F(0) complex subunit C1,
mitochondrial.
/FTId=PRO_0000395412.
TRANSMEM 77 97 Helical. {ECO:0000255}.
TRANSMEM 112 132 Helical. {ECO:0000255}.
SITE 119 119 Reversibly protonated during proton
transport. {ECO:0000250}.
CONFLICT 12 12 A -> V (in Ref. 1; BAE39897).
{ECO:0000305}.
SEQUENCE 136 AA; 14200 MW; 12B9ABDEE627994C CRC64;
MQTTKALLIS PALIRSCTRG LIRPVSASLL SRPEAPSKQP SCSSSPLQVA RREFQTSVIS
RDIDTAAKFI GAGAATVGVA GSGAGIGTVF GSLIIGYARN PSLKQQLFSY AILGFALSEA
MGLFCLMVAF LILFAM


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