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UQCC3_RAT
ID   UQCC3_RAT               Reviewed;          89 AA.
AC   P0CD94;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Ubiquinol-cytochrome-c reductase complex assembly factor 3 {ECO:0000250|UniProtKB:Q6UW78};
GN   Name=Uqcc3 {ECO:0000250|UniProtKB:Q6UW78};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Brown Norway/NHsdMcwi; TISSUE=Heart;
RA   Kube M., Klages S., Kuhl H., Thiel J., Beck A., Reinhardt R.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
CC   -!- FUNCTION: Required for the assembly of the ubiquinol-cytochrome c
CC       reductase complex (mitochondrial respiratory chain complex III or
CC       cytochrome b-c1 complex), mediating cytochrome b recruitment and
CC       probably stabilization within the complex. Thereby, plays an important
CC       role in ATP production by mitochondria. Cardiolipin-binding protein, it
CC       may also control the cardiolipin composition of mitochondria membranes
CC       and their morphology. {ECO:0000250|UniProtKB:Q6UW78}.
CC   -!- SUBUNIT: Associates with the ubiquinol-cytochrome c reductase complex
CC       (mitochondrial respiratory chain complex III or cytochrome b-c1
CC       complex). {ECO:0000250|UniProtKB:Q6UW78}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q6UW78}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q6UW78}.
CC   -!- PTM: Probably cleaved by OMA1 under mitochondrial stress conditions.
CC       {ECO:0000250|UniProtKB:Q6UW78}.
CC   -!- SIMILARITY: Belongs to the UQCC3 family. {ECO:0000305}.
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DR   EMBL; FM057246; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001162132.1; NM_001168661.1.
DR   AlphaFoldDB; P0CD94; -.
DR   IntAct; P0CD94; 1.
DR   STRING; 10116.ENSRNOP00000064397; -.
DR   PaxDb; P0CD94; -.
DR   Ensembl; ENSRNOT00000074747; ENSRNOP00000064397; ENSRNOG00000045561.
DR   GeneID; 690344; -.
DR   KEGG; rno:690344; -.
DR   UCSC; RGD:1597344; rat.
DR   CTD; 790955; -.
DR   RGD; 1597344; Uqcc3.
DR   eggNOG; ENOG502S9VI; Eukaryota.
DR   GeneTree; ENSGT00390000001930; -.
DR   HOGENOM; CLU_184624_0_0_1; -.
DR   InParanoid; P0CD94; -.
DR   OMA; VAWRKDW; -.
DR   OrthoDB; 1568049at2759; -.
DR   PhylomeDB; P0CD94; -.
DR   PRO; PR:P0CD94; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000045561; Expressed in ovary and 20 other tissues.
DR   Genevisible; P0CD94; RN.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
DR   GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042407; P:cristae formation; ISS:UniProtKB.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; ISS:UniProtKB.
DR   GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; ISS:UniProtKB.
DR   InterPro; IPR027896; UQCC3.
DR   PANTHER; PTHR36465; PTHR36465; 1.
DR   Pfam; PF15141; UQCC3; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..89
FT                   /note="Ubiquinol-cytochrome-c reductase complex assembly
FT                   factor 3"
FT                   /id="PRO_0000391705"
FT   TOPO_DOM        1..7
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q6UW78"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..89
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q6UW78"
FT   REGION          23..80
FT                   /note="Mediates lipid-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q6UW78"
SQ   SEQUENCE   89 AA;  9678 MW;  4DB1F8CD0DFCBEA7 CRC64;
     MEAARKALAV VAVLGAGGGV GSILFALVTP GELQKQLMLQ EMPERDSRRR DEAVRTKELV
     MATLKDAAAT KENVAWRRNW TVRGDGRSA
 
 
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