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Protein

Cytochrome b-c1 complex subunit 1, mitochondrial

Gene

Uqcrc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.

Protein family/group databases

MEROPSiM16.975.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b-c1 complex subunit 1, mitochondrial
Alternative name(s):
Complex III subunit 1
Core protein I
Ubiquinol-cytochrome-c reductase complex core protein 1
Gene namesi
Name:Uqcrc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:107876. Uqcrc1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: MGI
  • mitochondrial respiratory chain complex III Source: GO_Central
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434MitochondrionBy similarityAdd
BLAST
Chaini35 – 480446Cytochrome b-c1 complex subunit 1, mitochondrialPRO_0000026787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-acetyllysineCombined sources
Modified residuei138 – 1381N6-acetyllysineCombined sources
Modified residuei163 – 1631N6-acetyllysine; alternateCombined sources
Modified residuei163 – 1631N6-succinyllysine; alternateCombined sources
Modified residuei212 – 2121PhosphoserineBy similarity
Modified residuei214 – 2141PhosphothreonineBy similarity
Modified residuei248 – 2481N6-acetyllysineCombined sources

Post-translational modificationi

Acetylation of Lys-138 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CZ13.
MaxQBiQ9CZ13.
PaxDbiQ9CZ13.
PeptideAtlasiQ9CZ13.
PRIDEiQ9CZ13.
TopDownProteomicsiQ9CZ13.

2D gel databases

REPRODUCTION-2DPAGEIPI00111885.
Q9CZ13.
UCD-2DPAGEQ9CZ13.

PTM databases

iPTMnetiQ9CZ13.
PhosphoSiteiQ9CZ13.
SwissPalmiQ9CZ13.

Expressioni

Gene expression databases

BgeeiQ9CZ13.
CleanExiMM_UQCRC1.
ExpressionAtlasiQ9CZ13. baseline and differential.
GenevisibleiQ9CZ13. MM.

Interactioni

Subunit structurei

The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204459. 4 interactions.
IntActiQ9CZ13. 10 interactions.
MINTiMINT-1842368.
STRINGi10090.ENSMUSP00000026743.

Structurei

3D structure databases

ProteinModelPortaliQ9CZ13.
SMRiQ9CZ13. Positions 35-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0960. Eukaryota.
COG0612. LUCA.
GeneTreeiENSGT00550000074701.
HOGENOMiHOG000242450.
HOVERGENiHBG006393.
InParanoidiQ9CZ13.
KOiK00414.
OMAiFFLQGQW.
OrthoDBiEOG74R1QJ.
TreeFamiTF105032.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CZ13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASAVCRAA CSGTQVLLRT RRSPALLRLP ALRGTATFAQ ALQSVPETQV
60 70 80 90 100
SILDNGLRVA SEQSSHATCT VGVWIDAGSR YETEKNNGAG YFLEHLAFKG
110 120 130 140 150
TKNRPGNALE KEVESIGAHL NAYSTREHTA YLIKALSKDL PKVVELLADI
160 170 180 190 200
VQNSSLEDSQ IEKERDVILR EMQENDASMQ NVVFDYLHAT AFQGTPLAQA
210 220 230 240 250
VEGPSENVRR LSRTDLTDYL NRHYKAPRMV LAAAGGVEHQ QLLDLAQKHL
260 270 280 290 300
SSVSRVYEED AVPGLTPCRF TGSEIRHRDD ALPLAHVAIA VEGPGWANPD
310 320 330 340 350
NVTLQVANAI IGHYDCTYGG GVHLSSPLAS VAVANKLCQS FQTFNISYSD
360 370 380 390 400
TGLLGAHFVC DAMSIDDMVF FLQGQWMRLC TSATESEVTR GKNILRNALV
410 420 430 440 450
SHLDGTTPVC EDIGRSLLTY GRRIPLAEWE SRIQEVDAQM LRDICSKYFY
460 470 480
DQCPAVAGYG PIEQLPDYNR IRSGMFWLRF
Length:480
Mass (Da):52,852
Last modified:July 27, 2011 - v2
Checksum:i8150C97C655A91C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231H → N in BAB28666 (PubMed:16141072).Curated
Sequence conflicti318 – 3181Y → C in BAB28666 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013128 mRNA. Translation: BAB28666.1.
AK010553 mRNA. Translation: BAB27022.1.
AK151764 mRNA. Translation: BAE30670.1.
AK160337 mRNA. Translation: BAE35744.1.
CH466560 Genomic DNA. Translation: EDL21324.1.
CCDSiCCDS23540.1.
RefSeqiNP_079683.2. NM_025407.2.
UniGeneiMm.335460.

Genome annotation databases

EnsembliENSMUST00000026743; ENSMUSP00000026743; ENSMUSG00000025651.
ENSMUST00000202750; ENSMUSP00000144124; ENSMUSG00000107235.
GeneIDi22273.
KEGGimmu:22273.
UCSCiuc009rrg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013128 mRNA. Translation: BAB28666.1.
AK010553 mRNA. Translation: BAB27022.1.
AK151764 mRNA. Translation: BAE30670.1.
AK160337 mRNA. Translation: BAE35744.1.
CH466560 Genomic DNA. Translation: EDL21324.1.
CCDSiCCDS23540.1.
RefSeqiNP_079683.2. NM_025407.2.
UniGeneiMm.335460.

3D structure databases

ProteinModelPortaliQ9CZ13.
SMRiQ9CZ13. Positions 35-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204459. 4 interactions.
IntActiQ9CZ13. 10 interactions.
MINTiMINT-1842368.
STRINGi10090.ENSMUSP00000026743.

Protein family/group databases

MEROPSiM16.975.

PTM databases

iPTMnetiQ9CZ13.
PhosphoSiteiQ9CZ13.
SwissPalmiQ9CZ13.

2D gel databases

REPRODUCTION-2DPAGEIPI00111885.
Q9CZ13.
UCD-2DPAGEQ9CZ13.

Proteomic databases

EPDiQ9CZ13.
MaxQBiQ9CZ13.
PaxDbiQ9CZ13.
PeptideAtlasiQ9CZ13.
PRIDEiQ9CZ13.
TopDownProteomicsiQ9CZ13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026743; ENSMUSP00000026743; ENSMUSG00000025651.
ENSMUST00000202750; ENSMUSP00000144124; ENSMUSG00000107235.
GeneIDi22273.
KEGGimmu:22273.
UCSCiuc009rrg.1. mouse.

Organism-specific databases

CTDi7384.
MGIiMGI:107876. Uqcrc1.

Phylogenomic databases

eggNOGiKOG0960. Eukaryota.
COG0612. LUCA.
GeneTreeiENSGT00550000074701.
HOGENOMiHOG000242450.
HOVERGENiHBG006393.
InParanoidiQ9CZ13.
KOiK00414.
OMAiFFLQGQW.
OrthoDBiEOG74R1QJ.
TreeFamiTF105032.

Enzyme and pathway databases

ReactomeiR-MMU-611105. Respiratory electron transport.

Miscellaneous databases

PROiQ9CZ13.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CZ13.
CleanExiMM_UQCRC1.
ExpressionAtlasiQ9CZ13. baseline and differential.
GenevisibleiQ9CZ13. MM.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: C57BL/6J.
    Tissue: Bone marrow and Embryo.
  2. 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].
  3. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 59-80; 86-99; 112-134; 143-163; 214-222; 229-248; 256-276; 379-390; 397-442; 448-470 AND 473-479, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111; LYS-138; LYS-163 AND LYS-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiQCR1_MOUSE
AccessioniPrimary (citable) accession number: Q9CZ13
Secondary accession number(s): Q3TV75, Q9CWL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Does not seem to have a protease activity as it lack the zinc-binding site.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.