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P31800

- QCR1_BOVIN

UniProt

P31800 - QCR1_BOVIN

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Protein

Cytochrome b-c1 complex subunit 1, mitochondrial

Gene

UQCRC1

Organism
Bos taurus (Bovine)
Status
Reviewed - 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.

GO - Molecular functioni

  1. catalytic activity Source: InterPro
  2. metal ion binding Source: InterPro

GO - Biological processi

  1. oxidation-reduction process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Protein family/group databases

MEROPSiM16.973.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: AgBase
  2. mitochondrion Source: AgBase
  3. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434Mitochondrion1 PublicationAdd
BLAST
Chaini35 – 480446Cytochrome b-c1 complex subunit 1, mitochondrialPRO_0000026785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-acetyllysineBy similarity
Modified residuei138 – 1381N6-acetyllysineBy similarity
Modified residuei163 – 1631N6-acetyllysine; alternateBy similarity
Modified residuei163 – 1631N6-succinyllysine; alternateBy similarity
Modified residuei248 – 2481N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP31800.
PRIDEiP31800.

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).

Protein-protein interaction databases

DIPiDIP-1105N.
IntActiP31800. 3 interactions.
MINTiMINT-149960.
STRINGi9913.ENSBTAP00000025422.

Structurei

Secondary structure

1
480
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 425Combined sources
Beta strandi49 – 524Combined sources
Beta strandi54 – 563Combined sources
Beta strandi58 – 636Combined sources
Beta strandi67 – 7610Combined sources
Helixi79 – 813Combined sources
Turni84 – 885Combined sources
Helixi89 – 968Combined sources
Beta strandi97 – 993Combined sources
Beta strandi101 – 1044Combined sources
Turni105 – 1073Combined sources
Helixi108 – 1158Combined sources
Beta strandi119 – 1246Combined sources
Beta strandi129 – 1368Combined sources
Helixi137 – 1393Combined sources
Helixi140 – 15314Combined sources
Helixi158 – 17518Combined sources
Helixi179 – 19113Combined sources
Turni192 – 1943Combined sources
Helixi196 – 1983Combined sources
Helixi205 – 2106Combined sources
Helixi213 – 22311Combined sources
Helixi226 – 2283Combined sources
Beta strandi229 – 2368Combined sources
Helixi239 – 25012Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi282 – 29312Combined sources
Helixi301 – 31111Combined sources
Beta strandi313 – 3153Combined sources
Helixi321 – 3233Combined sources
Helixi327 – 3359Combined sources
Beta strandi339 – 3479Combined sources
Beta strandi352 – 3609Combined sources
Helixi362 – 3643Combined sources
Helixi365 – 38218Combined sources
Helixi385 – 40218Combined sources
Helixi406 – 41914Combined sources
Helixi426 – 4349Combined sources
Helixi438 – 44811Combined sources
Turni449 – 4513Combined sources
Beta strandi455 – 4617Combined sources
Helixi462 – 4643Combined sources
Helixi468 – 4736Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCCX-ray3.16A35-480[»]
1BE3X-ray3.00A35-480[»]
1BGYX-ray3.00A/M35-480[»]
1L0LX-ray2.35A35-480[»]
1L0NX-ray2.60A35-480[»]
1NTKX-ray2.60A35-480[»]
1NTMX-ray2.40A35-480[»]
1NTZX-ray2.60A35-480[»]
1NU1X-ray3.20A35-480[»]
1PP9X-ray2.10A/N35-480[»]
1PPJX-ray2.10A/N35-480[»]
1QCRX-ray2.70A35-480[»]
1SQBX-ray2.69A1-480[»]
1SQPX-ray2.70A1-480[»]
1SQQX-ray3.00A35-480[»]
1SQVX-ray2.85A35-480[»]
1SQXX-ray2.60A35-480[»]
2A06X-ray2.10A/N35-480[»]
2BCCX-ray3.50A35-480[»]
2FYUX-ray2.26A35-480[»]
2YBBelectron microscopy19.00A/a35-480[»]
3BCCX-ray3.70A35-480[»]
ProteinModelPortaliP31800.
SMRiP31800. Positions 35-480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31800.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0612.
HOGENOMiHOG000242450.
HOVERGENiHBG006393.
InParanoidiP31800.
KOiK00414.

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.

P31800-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAASAVCRAA GAGTRVLLRT RRSPALLRSS DLRGTATYAQ ALQSVPETQV
60 70 80 90 100
SQLDNGLRVA SEQSSQPTCT VGVWIDAGSR YESEKNNGAG YFVEHLAFKG
110 120 130 140 150
TKNRPGNALE KEVESMGAHL NAYSTREHTA YYIKALSKDL PKAVELLADI
160 170 180 190 200
VQNCSLEDSQ IEKERDVILQ ELQENDTSMR DVVFNYLHAT AFQGTPLAQS
210 220 230 240 250
VEGPSENVRK LSRADLTEYL SRHYKAPRMV LAAAGGLEHR QLLDLAQKHF
260 270 280 290 300
SGLSGTYDED AVPTLSPCRF TGSQICHRED GLPLAHVAIA VEGPGWAHPD
310 320 330 340 350
NVALQVANAI IGHYDCTYGG GAHLSSPLAS IAATNKLCQS FQTFNICYAD
360 370 380 390 400
TGLLGAHFVC DHMSIDDMMF VLQGQWMRLC TSATESEVLR GKNLLRNALV
410 420 430 440 450
SHLDGTTPVC EDIGRSLLTY GRRIPLAEWE SRIAEVDARV VREVCSKYFY
460 470 480
DQCPAVAGFG PIEQLPDYNR IRSGMFWLRF
Length:480
Mass (Da):52,736
Last modified:December 1, 2000 - v2
Checksum:i4E54DD28C1905392
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59692 mRNA. Translation: CAA42213.1.
PIRiS16220. ZPBOC1.
RefSeqiNP_777054.1. NM_174629.2.
UniGeneiBt.23164.

Genome annotation databases

GeneIDi282393.
KEGGibta:282393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59692 mRNA. Translation: CAA42213.1 .
PIRi S16220. ZPBOC1.
RefSeqi NP_777054.1. NM_174629.2.
UniGenei Bt.23164.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BCC X-ray 3.16 A 35-480 [» ]
1BE3 X-ray 3.00 A 35-480 [» ]
1BGY X-ray 3.00 A/M 35-480 [» ]
1L0L X-ray 2.35 A 35-480 [» ]
1L0N X-ray 2.60 A 35-480 [» ]
1NTK X-ray 2.60 A 35-480 [» ]
1NTM X-ray 2.40 A 35-480 [» ]
1NTZ X-ray 2.60 A 35-480 [» ]
1NU1 X-ray 3.20 A 35-480 [» ]
1PP9 X-ray 2.10 A/N 35-480 [» ]
1PPJ X-ray 2.10 A/N 35-480 [» ]
1QCR X-ray 2.70 A 35-480 [» ]
1SQB X-ray 2.69 A 1-480 [» ]
1SQP X-ray 2.70 A 1-480 [» ]
1SQQ X-ray 3.00 A 35-480 [» ]
1SQV X-ray 2.85 A 35-480 [» ]
1SQX X-ray 2.60 A 35-480 [» ]
2A06 X-ray 2.10 A/N 35-480 [» ]
2BCC X-ray 3.50 A 35-480 [» ]
2FYU X-ray 2.26 A 35-480 [» ]
2YBB electron microscopy 19.00 A/a 35-480 [» ]
3BCC X-ray 3.70 A 35-480 [» ]
ProteinModelPortali P31800.
SMRi P31800. Positions 35-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-1105N.
IntActi P31800. 3 interactions.
MINTi MINT-149960.
STRINGi 9913.ENSBTAP00000025422.

Protein family/group databases

MEROPSi M16.973.

Proteomic databases

PaxDbi P31800.
PRIDEi P31800.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 282393.
KEGGi bta:282393.

Organism-specific databases

CTDi 7384.

Phylogenomic databases

eggNOGi COG0612.
HOGENOMi HOG000242450.
HOVERGENi HBG006393.
InParanoidi P31800.
KOi K00414.

Miscellaneous databases

EvolutionaryTracei P31800.
NextBioi 20806180.

Family and domain databases

Gene3Di 3.30.830.10. 2 hits.
InterProi IPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
[Graphical view ]
Pfami PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view ]
SUPFAMi SSF63411. SSF63411. 2 hits.
ProtoNeti Search...

Publicationsi

  1. "Core I protein of bovine ubiquinol-cytochrome-c reductase; an additional member of the mitochondrial-protein-processing family. Cloning of bovine core I and core II cDNAs and primary structure of the proteins."
    Gencic S., Schaegger H., von Jagow G.
    Eur. J. Biochem. 199:123-131(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Ubiquinol-cytochrome-c reductase from human and bovine mitochondria."
    Schaegger H., Brandt U., Gencic S., von Jagow G.
    Methods Enzymol. 260:82-96(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. Cited for: PROTEIN SEQUENCE OF 35-52.
  4. "Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria."
    Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L., Deisenhofer J.
    Science 277:60-66(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  5. Erratum
    Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L., Deisenhofer J.
    Science 278:2037-2037(1997)
  6. "Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex."
    Iwata S., Lee J.W., Okada K., Lee J.K., Iwata M., Rasmussen B., Link T.A., Ramaswamy S., Jap B.K.
    Science 281:64-71(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  7. "The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition."
    Gao X., Wen X., Yu C., Esser L., Tsao S., Quinn B., Zhang L., Yu L., Xia D.
    Biochemistry 41:11692-11702(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
  8. "Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex."
    Esser L., Quinn B., Li Y.F., Zhang M., Elberry M., Yu L., Yu C.A., Xia D.
    J. Mol. Biol. 341:281-302(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
  9. "Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern."
    Huang L.S., Cobessi D., Tung E.Y., Berry E.A.
    J. Mol. Biol. 351:573-597(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  10. "Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome bc1 complex."
    Esser L., Gong X., Yang S., Yu L., Yu C.A., Xia D.
    Proc. Natl. Acad. Sci. U.S.A. 103:13045-13050(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).

Entry informationi

Entry nameiQCR1_BOVIN
AccessioniPrimary (citable) accession number: P31800
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 1, 2000
Last modified: November 26, 2014
This is version 127 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3