Full text data of UQCRC1
UQCRC1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Cytochrome b-c1 complex subunit 1, mitochondrial (Complex III subunit 1; Core protein I; Ubiquinol-cytochrome-c reductase complex core protein 1; Flags: Precursor)
Cytochrome b-c1 complex subunit 1, mitochondrial (Complex III subunit 1; Core protein I; Ubiquinol-cytochrome-c reductase complex core protein 1; Flags: Precursor)
UniProt
P31930
ID QCR1_HUMAN Reviewed; 480 AA.
AC P31930; B2R7R8; Q96DD2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-APR-2006, sequence version 3.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Cytochrome b-c1 complex subunit 1, mitochondrial;
DE AltName: Full=Complex III subunit 1;
DE AltName: Full=Core protein I;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 1;
DE Flags: Precursor;
GN Name=UQCRC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-301.
RC TISSUE=Placenta;
RX PubMed=8407948;
RA Hoffman G.G., Lee S., Christiano A.M., Chung-Honet L.C., Cheng W.,
RA Katchman S., Uitto J., Greenspan D.S.;
RT "Complete coding sequence, intron/exon organization, and chromosomal
RT location of the gene for the core I protein of human ubiquinol-
RT cytochrome c reductase.";
RL J. Biol. Chem. 268:21113-21119(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=8069229;
RA Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.;
RT "A complete cDNA sequence for core I protein subunit of human
RT ubiquinol-cytochrome c reductase.";
RL Biochem. Mol. Biol. Int. 32:797-805(1994).
RN [3]
RP ERRATUM.
RX PubMed=7951059;
RA Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.;
RL Biochem. Mol. Biol. Int. 33:410-410(1994).
RN [4]
RP ERRATUM.
RX PubMed=7981668;
RA Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.;
RL Biochem. Mol. Biol. Int. 33:815-815(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 35-45.
RC TISSUE=Liver;
RX PubMed=8313870; DOI=10.1002/elps.11501401181;
RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C.,
RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
RT "Human liver protein map: update 1993.";
RL Electrophoresis 14:1216-1222(1993).
RN [9]
RP PROTEIN SEQUENCE OF 86-99; 214-225; 229-248; 397-415; 424-442; 448-470
RP AND 473-479, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 143-165; 181-209 AND 397-415.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/BJ20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at
RT the surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP VARIANT SER-301.
RX PubMed=10453733; DOI=10.1007/s004390050988;
RA Valnot I., Kassis J., Chretien D., de Lonlay P., Parfait B.,
RA Munnich A., Kachaner J., Rustin P., Roetig A.;
RT "A mitochondrial cytochrome b mutation but no mutations of nuclearly
RT encoded subunits in ubiquinol cytochrome c reductase (complex III)
RT deficiency.";
RL Hum. Genet. 104:460-466(1999).
CC -!- FUNCTION: This is a component of the ubiquinol-cytochrome c
CC reductase complex (complex III or cytochrome b-c1 complex), which
CC is part of the mitochondrial respiratory chain. This protein may
CC mediate formation of the complex between cytochromes c and c1.
CC -!- SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory
CC subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core
CC proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight
CC proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9,
CC UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1).
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC1/QCR1
CC subfamily.
CC -!- CAUTION: Does not seem to have a protease activity as it lack the
CC zinc-binding site.
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DR EMBL; L16842; AAA20046.1; -; mRNA.
DR EMBL; D26485; BAA05495.1; -; mRNA.
DR EMBL; AK313090; BAG35915.1; -; mRNA.
DR EMBL; CH471055; EAW64898.1; -; Genomic_DNA.
DR EMBL; BC009586; AAH09586.1; -; mRNA.
DR PIR; A48043; A48043.
DR RefSeq; NP_003356.2; NM_003365.2.
DR UniGene; Hs.119251; -.
DR ProteinModelPortal; P31930; -.
DR SMR; P31930; 35-476.
DR IntAct; P31930; 9.
DR MINT; MINT-3012677; -.
DR STRING; 9606.ENSP00000203407; -.
DR DrugBank; DB01117; Atovaquone.
DR MEROPS; M16.973; -.
DR PhosphoSite; P31930; -.
DR DMDM; 92090651; -.
DR OGP; P31930; -.
DR REPRODUCTION-2DPAGE; IPI00013847; -.
DR SWISS-2DPAGE; P31930; -.
DR UCD-2DPAGE; P31930; -.
DR PaxDb; P31930; -.
DR PeptideAtlas; P31930; -.
DR PRIDE; P31930; -.
DR Ensembl; ENST00000203407; ENSP00000203407; ENSG00000010256.
DR GeneID; 7384; -.
DR KEGG; hsa:7384; -.
DR UCSC; uc003cub.1; human.
DR CTD; 7384; -.
DR GeneCards; GC03M048636; -.
DR HGNC; HGNC:12585; UQCRC1.
DR HPA; HPA002815; -.
DR HPA; HPA003525; -.
DR MIM; 191328; gene.
DR neXtProt; NX_P31930; -.
DR PharmGKB; PA37216; -.
DR eggNOG; COG0612; -.
DR HOGENOM; HOG000242450; -.
DR HOVERGEN; HBG006393; -.
DR InParanoid; P31930; -.
DR KO; K00414; -.
DR OMA; DDMMFFL; -.
DR OrthoDB; EOG74R1QJ; -.
DR PhylomeDB; P31930; -.
DR Reactome; REACT_111217; Metabolism.
DR SignaLink; P31930; -.
DR ChiTaRS; UQCRC1; human.
DR GeneWiki; UQCRC1; -.
DR GenomeRNAi; 7384; -.
DR NextBio; 28912; -.
DR PRO; PR:P31930; -.
DR ArrayExpress; P31930; -.
DR Bgee; P31930; -.
DR CleanEx; HS_UQCRC1; -.
DR Genevestigator; P31930; -.
DR GO; GO:0005746; C:mitochondrial respiratory chain; TAS:ProtInc.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; TAS:ProtInc.
DR GO; GO:0009060; P:aerobic respiration; TAS:ProtInc.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:Ensembl.
DR GO; GO:0006119; P:oxidative phosphorylation; TAS:ProtInc.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 3.30.830.10; -; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011237; Pept_M16_dom.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing;
KW Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Polymorphism; Reference proteome;
KW Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1 34 Mitochondrion.
FT CHAIN 35 480 Cytochrome b-c1 complex subunit 1,
FT mitochondrial.
FT /FTId=PRO_0000026786.
FT MOD_RES 111 111 N6-acetyllysine.
FT MOD_RES 138 138 N6-acetyllysine (By similarity).
FT MOD_RES 163 163 N6-acetyllysine (By similarity).
FT MOD_RES 248 248 N6-acetyllysine (By similarity).
FT VARIANT 215 215 D -> H (in dbSNP:rs17080284).
FT /FTId=VAR_034581.
FT VARIANT 301 301 N -> S (in dbSNP:rs144710790).
FT /FTId=VAR_013629.
SQ SEQUENCE 480 AA; 52646 MW; E76B082166CAF48F CRC64;
MAASVVCRAA TAGAQVLLRA RRSPALLRTP ALRSTATFAQ ALQFVPETQV SLLDNGLRVA
SEQSSQPTCT VGVWIDVGSR FETEKNNGAG YFLEHLAFKG TKNRPGSALE KEVESMGAHL
NAYSTREHTA YYIKALSKDL PKAVELLGDI VQNCSLEDSQ IEKERDVILR EMQENDASMR
DVVFNYLHAT AFQGTPLAQA VEGPSENVRK LSRADLTEYL STHYKAPRMV LAAAGGVEHQ
QLLDLAQKHL GGIPWTYAED AVPTLTPCRF TGSEIRHRDD ALPFAHVAIA VEGPGWASPD
NVALQVANAI IGHYDCTYGG GVHLSSPLAS GAVANKLCQS FQTFSICYAE TGLLGAHFVC
DRMKIDDMMF VLQGQWMRLC TSATESEVAR GKNILRNALV SHLDGTTPVC EDIGRSLLTY
GRRIPLAEWE SRIAEVDASV VREICSKYIY DQCPAVAGYG PIEQLPDYNR IRSGMFWLRF
//
ID QCR1_HUMAN Reviewed; 480 AA.
AC P31930; B2R7R8; Q96DD2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-APR-2006, sequence version 3.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Cytochrome b-c1 complex subunit 1, mitochondrial;
DE AltName: Full=Complex III subunit 1;
DE AltName: Full=Core protein I;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 1;
DE Flags: Precursor;
GN Name=UQCRC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-301.
RC TISSUE=Placenta;
RX PubMed=8407948;
RA Hoffman G.G., Lee S., Christiano A.M., Chung-Honet L.C., Cheng W.,
RA Katchman S., Uitto J., Greenspan D.S.;
RT "Complete coding sequence, intron/exon organization, and chromosomal
RT location of the gene for the core I protein of human ubiquinol-
RT cytochrome c reductase.";
RL J. Biol. Chem. 268:21113-21119(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=8069229;
RA Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.;
RT "A complete cDNA sequence for core I protein subunit of human
RT ubiquinol-cytochrome c reductase.";
RL Biochem. Mol. Biol. Int. 32:797-805(1994).
RN [3]
RP ERRATUM.
RX PubMed=7951059;
RA Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.;
RL Biochem. Mol. Biol. Int. 33:410-410(1994).
RN [4]
RP ERRATUM.
RX PubMed=7981668;
RA Islam M.M., Tanaka M., Suzuki H., Torii K., Hattori N., Ozawa T.;
RL Biochem. Mol. Biol. Int. 33:815-815(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 35-45.
RC TISSUE=Liver;
RX PubMed=8313870; DOI=10.1002/elps.11501401181;
RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C.,
RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
RT "Human liver protein map: update 1993.";
RL Electrophoresis 14:1216-1222(1993).
RN [9]
RP PROTEIN SEQUENCE OF 86-99; 214-225; 229-248; 397-415; 424-442; 448-470
RP AND 473-479, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 143-165; 181-209 AND 397-415.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/BJ20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at
RT the surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP VARIANT SER-301.
RX PubMed=10453733; DOI=10.1007/s004390050988;
RA Valnot I., Kassis J., Chretien D., de Lonlay P., Parfait B.,
RA Munnich A., Kachaner J., Rustin P., Roetig A.;
RT "A mitochondrial cytochrome b mutation but no mutations of nuclearly
RT encoded subunits in ubiquinol cytochrome c reductase (complex III)
RT deficiency.";
RL Hum. Genet. 104:460-466(1999).
CC -!- FUNCTION: This is a component of the ubiquinol-cytochrome c
CC reductase complex (complex III or cytochrome b-c1 complex), which
CC is part of the mitochondrial respiratory chain. This protein may
CC mediate formation of the complex between cytochromes c and c1.
CC -!- SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory
CC subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core
CC proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight
CC proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9,
CC UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1).
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC1/QCR1
CC subfamily.
CC -!- CAUTION: Does not seem to have a protease activity as it lack the
CC zinc-binding site.
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DR EMBL; L16842; AAA20046.1; -; mRNA.
DR EMBL; D26485; BAA05495.1; -; mRNA.
DR EMBL; AK313090; BAG35915.1; -; mRNA.
DR EMBL; CH471055; EAW64898.1; -; Genomic_DNA.
DR EMBL; BC009586; AAH09586.1; -; mRNA.
DR PIR; A48043; A48043.
DR RefSeq; NP_003356.2; NM_003365.2.
DR UniGene; Hs.119251; -.
DR ProteinModelPortal; P31930; -.
DR SMR; P31930; 35-476.
DR IntAct; P31930; 9.
DR MINT; MINT-3012677; -.
DR STRING; 9606.ENSP00000203407; -.
DR DrugBank; DB01117; Atovaquone.
DR MEROPS; M16.973; -.
DR PhosphoSite; P31930; -.
DR DMDM; 92090651; -.
DR OGP; P31930; -.
DR REPRODUCTION-2DPAGE; IPI00013847; -.
DR SWISS-2DPAGE; P31930; -.
DR UCD-2DPAGE; P31930; -.
DR PaxDb; P31930; -.
DR PeptideAtlas; P31930; -.
DR PRIDE; P31930; -.
DR Ensembl; ENST00000203407; ENSP00000203407; ENSG00000010256.
DR GeneID; 7384; -.
DR KEGG; hsa:7384; -.
DR UCSC; uc003cub.1; human.
DR CTD; 7384; -.
DR GeneCards; GC03M048636; -.
DR HGNC; HGNC:12585; UQCRC1.
DR HPA; HPA002815; -.
DR HPA; HPA003525; -.
DR MIM; 191328; gene.
DR neXtProt; NX_P31930; -.
DR PharmGKB; PA37216; -.
DR eggNOG; COG0612; -.
DR HOGENOM; HOG000242450; -.
DR HOVERGEN; HBG006393; -.
DR InParanoid; P31930; -.
DR KO; K00414; -.
DR OMA; DDMMFFL; -.
DR OrthoDB; EOG74R1QJ; -.
DR PhylomeDB; P31930; -.
DR Reactome; REACT_111217; Metabolism.
DR SignaLink; P31930; -.
DR ChiTaRS; UQCRC1; human.
DR GeneWiki; UQCRC1; -.
DR GenomeRNAi; 7384; -.
DR NextBio; 28912; -.
DR PRO; PR:P31930; -.
DR ArrayExpress; P31930; -.
DR Bgee; P31930; -.
DR CleanEx; HS_UQCRC1; -.
DR Genevestigator; P31930; -.
DR GO; GO:0005746; C:mitochondrial respiratory chain; TAS:ProtInc.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; TAS:ProtInc.
DR GO; GO:0009060; P:aerobic respiration; TAS:ProtInc.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:Ensembl.
DR GO; GO:0006119; P:oxidative phosphorylation; TAS:ProtInc.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 3.30.830.10; -; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011237; Pept_M16_dom.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing;
KW Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Polymorphism; Reference proteome;
KW Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1 34 Mitochondrion.
FT CHAIN 35 480 Cytochrome b-c1 complex subunit 1,
FT mitochondrial.
FT /FTId=PRO_0000026786.
FT MOD_RES 111 111 N6-acetyllysine.
FT MOD_RES 138 138 N6-acetyllysine (By similarity).
FT MOD_RES 163 163 N6-acetyllysine (By similarity).
FT MOD_RES 248 248 N6-acetyllysine (By similarity).
FT VARIANT 215 215 D -> H (in dbSNP:rs17080284).
FT /FTId=VAR_034581.
FT VARIANT 301 301 N -> S (in dbSNP:rs144710790).
FT /FTId=VAR_013629.
SQ SEQUENCE 480 AA; 52646 MW; E76B082166CAF48F CRC64;
MAASVVCRAA TAGAQVLLRA RRSPALLRTP ALRSTATFAQ ALQFVPETQV SLLDNGLRVA
SEQSSQPTCT VGVWIDVGSR FETEKNNGAG YFLEHLAFKG TKNRPGSALE KEVESMGAHL
NAYSTREHTA YYIKALSKDL PKAVELLGDI VQNCSLEDSQ IEKERDVILR EMQENDASMR
DVVFNYLHAT AFQGTPLAQA VEGPSENVRK LSRADLTEYL STHYKAPRMV LAAAGGVEHQ
QLLDLAQKHL GGIPWTYAED AVPTLTPCRF TGSEIRHRDD ALPFAHVAIA VEGPGWASPD
NVALQVANAI IGHYDCTYGG GVHLSSPLAS GAVANKLCQS FQTFSICYAE TGLLGAHFVC
DRMKIDDMMF VLQGQWMRLC TSATESEVAR GKNILRNALV SHLDGTTPVC EDIGRSLLTY
GRRIPLAEWE SRIAEVDASV VREICSKYIY DQCPAVAGYG PIEQLPDYNR IRSGMFWLRF
//
MIM
191328
*RECORD*
*FIELD* NO
191328
*FIELD* TI
*191328 UBIQUINOL-CYTOCHROME c REDUCTASE CORE PROTEIN I; UQCRC1
;;CYTOCHROME bc1
*FIELD* TX
read more
DESCRIPTION
The ubiquinol-cytochrome c reductase complex is an oligomeric enzyme
that catalyzes transfer of electrons from coenzyme QH2 to
ferricytochrome c with the coupled translocation of protons across the
mitochondrial inner membrane. Core I protein is a nuclear-encoded
component (summary by Hoffman et al., 1993).
CLONING
Hoffman et al. (1993) isolated and characterized genomic clones that
contained the entire gene for the human core I protein. The nucleotide
sequence of the human core I gene predicted a 480-amino acid protein.
Comparisons indicated that in mammals the core I protein and the small
subunit of mitochondrial processing peptidase are similar but
genetically distinct proteins.
MAPPING
By restriction mapping, Hoffman et al. (1993) found that the UQCRC1 gene
is located immediately upstream of the gene for type VII collagen
(COL7A1; 120120), which had been assigned by them and by others to
3p21.3.
*FIELD* RF
1. Hoffman, G. G.; Lee, S.; Christiano, A. M.; Chung-Honet, L. C.;
Cheng, W.; Katchman, S.; Uitto, J.; Greenspan, D. S.: Complete coding
sequence, intron/exon organization, and chromosomal location of the
gene for the core I protein of human ubiquinol-cytochrome c reductase. J.
Biol. Chem. 268: 21113-21119, 1993.
*FIELD* CD
Victor A. McKusick: 11/10/1993
*FIELD* ED
carol: 01/06/2014
alopez: 2/22/2005
mark: 10/1/1997
terry: 9/23/1997
mimadm: 6/7/1995
carol: 11/10/1993
*RECORD*
*FIELD* NO
191328
*FIELD* TI
*191328 UBIQUINOL-CYTOCHROME c REDUCTASE CORE PROTEIN I; UQCRC1
;;CYTOCHROME bc1
*FIELD* TX
read more
DESCRIPTION
The ubiquinol-cytochrome c reductase complex is an oligomeric enzyme
that catalyzes transfer of electrons from coenzyme QH2 to
ferricytochrome c with the coupled translocation of protons across the
mitochondrial inner membrane. Core I protein is a nuclear-encoded
component (summary by Hoffman et al., 1993).
CLONING
Hoffman et al. (1993) isolated and characterized genomic clones that
contained the entire gene for the human core I protein. The nucleotide
sequence of the human core I gene predicted a 480-amino acid protein.
Comparisons indicated that in mammals the core I protein and the small
subunit of mitochondrial processing peptidase are similar but
genetically distinct proteins.
MAPPING
By restriction mapping, Hoffman et al. (1993) found that the UQCRC1 gene
is located immediately upstream of the gene for type VII collagen
(COL7A1; 120120), which had been assigned by them and by others to
3p21.3.
*FIELD* RF
1. Hoffman, G. G.; Lee, S.; Christiano, A. M.; Chung-Honet, L. C.;
Cheng, W.; Katchman, S.; Uitto, J.; Greenspan, D. S.: Complete coding
sequence, intron/exon organization, and chromosomal location of the
gene for the core I protein of human ubiquinol-cytochrome c reductase. J.
Biol. Chem. 268: 21113-21119, 1993.
*FIELD* CD
Victor A. McKusick: 11/10/1993
*FIELD* ED
carol: 01/06/2014
alopez: 2/22/2005
mark: 10/1/1997
terry: 9/23/1997
mimadm: 6/7/1995
carol: 11/10/1993