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Protein

Cytochrome b-c1 complex subunit 2, mitochondrial

Gene

UQCRC2

Organism
Bos taurus (Bovine)
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. The core protein 2 is required for the assembly of the complex.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Enzyme and pathway databases

ReactomeiR-BTA-611105. Respiratory electron transport.

Protein family/group databases

MEROPSiM16.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b-c1 complex subunit 2, mitochondrial
Alternative name(s):
Complex III subunit 2
Core protein II
Ubiquinol-cytochrome-c reductase complex core protein 2
Gene namesi
Name:UQCRC2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 25

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 14Mitochondrion2 PublicationsAdd BLAST14
ChainiPRO_000002679015 – 453Cytochrome b-c1 complex subunit 2, mitochondrialAdd BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66N6-acetyllysineBy similarity1
Modified residuei199N6-acetyllysineBy similarity1
Modified residuei250N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP23004.
PeptideAtlasiP23004.
PRIDEiP23004.

Expressioni

Gene expression databases

BgeeiENSBTAG00000021651.

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-1106N.
IntActiP23004. 2 interactors.
MINTiMINT-149969.
STRINGi9913.ENSBTAP00000028853.

Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 42Combined sources4
Beta strandi44 – 46Combined sources3
Beta strandi48 – 52Combined sources5
Beta strandi57 – 66Combined sources10
Helixi69 – 71Combined sources3
Turni74 – 78Combined sources5
Helixi79 – 85Combined sources7
Turni86 – 88Combined sources3
Beta strandi91 – 94Combined sources4
Helixi96 – 105Combined sources10
Beta strandi109 – 114Combined sources6
Beta strandi119 – 126Combined sources8
Helixi127 – 129Combined sources3
Helixi130 – 142Combined sources13
Helixi148 – 165Combined sources18
Helixi169 – 181Combined sources13
Beta strandi182 – 184Combined sources3
Helixi185 – 187Combined sources3
Helixi194 – 196Combined sources3
Turni197 – 199Combined sources3
Helixi202 – 212Combined sources11
Helixi215 – 217Combined sources3
Beta strandi218 – 225Combined sources8
Helixi227 – 237Combined sources11
Beta strandi246 – 249Combined sources4
Beta strandi256 – 261Combined sources6
Beta strandi265 – 274Combined sources10
Beta strandi278 – 280Combined sources3
Helixi281 – 293Combined sources13
Beta strandi298 – 301Combined sources4
Helixi308 – 316Combined sources9
Beta strandi321 – 330Combined sources10
Beta strandi333 – 343Combined sources11
Helixi344 – 346Combined sources3
Helixi347 – 362Combined sources16
Helixi368 – 385Combined sources18
Helixi389 – 403Combined sources15
Helixi409 – 417Combined sources9
Helixi421 – 433Combined sources13
Beta strandi436 – 442Combined sources7
Helixi444 – 446Combined sources3
Helixi450 – 452Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BCCX-ray3.16B32-453[»]
1BE3X-ray3.00B15-453[»]
1BGYX-ray3.00B/N15-453[»]
1L0LX-ray2.35B15-453[»]
1L0NX-ray2.60B15-453[»]
1NTKX-ray2.60B15-453[»]
1NTMX-ray2.40B15-453[»]
1NTZX-ray2.60B15-453[»]
1NU1X-ray3.20B15-453[»]
1PP9X-ray2.10B/O15-453[»]
1PPJX-ray2.10B/O15-453[»]
1QCRX-ray2.70B31-453[»]
1SQBX-ray2.69B1-453[»]
1SQPX-ray2.70B1-453[»]
1SQQX-ray3.00B15-453[»]
1SQVX-ray2.85B15-453[»]
1SQXX-ray2.60B15-453[»]
2A06X-ray2.10B/O15-453[»]
2BCCX-ray3.50B32-453[»]
2FYUX-ray2.26B15-453[»]
2YBBelectron microscopy19.00B/b15-453[»]
3BCCX-ray3.70B32-453[»]
4D6TX-ray3.57B/O1-453[»]
4D6UX-ray4.09B/O1-453[»]
5KLVX-ray2.65B15-453[»]
ProteinModelPortaliP23004.
SMRiP23004.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23004.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2583. Eukaryota.
COG0612. LUCA.
GeneTreeiENSGT00550000074666.
HOGENOMiHOG000046923.
HOVERGENiHBG055236.
InParanoidiP23004.
KOiK00415.
OMAiNPQAHVI.
OrthoDBiEOG091G0A7X.
TreeFamiTF105033.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 3 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P23004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLTRAGSL SRFYSLKVAP KVKATEAPAG VPPHPQDLEF TRLPNGLVIA
60 70 80 90 100
SLENYAPASR IGLFIKAGSR YENSNNLGTS HLLRLASSLT TKGASSFKIT
110 120 130 140 150
RGIEAVGGKL SVTSTRENMA YTVECLRDDV DILMEFLLNV TTAPEFRRWE
160 170 180 190 200
VAALQPQLRI DKAVALQNPQ AHVIENLHAA AYRNALANSL YCPDYRIGKV
210 220 230 240 250
TPVELHDYVQ NHFTSARMAL IGLGVSHPVL KQVAEQFLNI RGGLGLSGAK
260 270 280 290 300
AKYHGGEIRE QNGDSLVHAA LVAESAAIGS AEANAFSVLQ HVLGAGPHVK
310 320 330 340 350
RGSNATSSLY QAVAKGVHQP FDVSAFNASY SDSGLFGFYT ISQAASAGDV
360 370 380 390 400
IKAAYNQVKT IAQGNLSNPD VQAAKNKLKA GYLMSVESSE GFLDEVGSQA
410 420 430 440 450
LAAGSYTPPS TVLQQIDAVA DADVINAAKK FVSGRKSMAA SGNLGHTPFI

DEL
Length:453
Mass (Da):48,149
Last modified:July 1, 1993 - v2
Checksum:iB7C600DA71CD34CF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti41T → R.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59693 mRNA. Translation: CAA42214.1.
BT020993 mRNA. Translation: AAX09010.1.
BC102337 mRNA. Translation: AAI02338.1.
PIRiS16221. ZPBOC2.
RefSeqiNP_777055.1. NM_174630.2.
UniGeneiBt.27799.

Genome annotation databases

EnsembliENSBTAT00000028853; ENSBTAP00000028853; ENSBTAG00000021651.
GeneIDi282394.
KEGGibta:282394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59693 mRNA. Translation: CAA42214.1.
BT020993 mRNA. Translation: AAX09010.1.
BC102337 mRNA. Translation: AAI02338.1.
PIRiS16221. ZPBOC2.
RefSeqiNP_777055.1. NM_174630.2.
UniGeneiBt.27799.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BCCX-ray3.16B32-453[»]
1BE3X-ray3.00B15-453[»]
1BGYX-ray3.00B/N15-453[»]
1L0LX-ray2.35B15-453[»]
1L0NX-ray2.60B15-453[»]
1NTKX-ray2.60B15-453[»]
1NTMX-ray2.40B15-453[»]
1NTZX-ray2.60B15-453[»]
1NU1X-ray3.20B15-453[»]
1PP9X-ray2.10B/O15-453[»]
1PPJX-ray2.10B/O15-453[»]
1QCRX-ray2.70B31-453[»]
1SQBX-ray2.69B1-453[»]
1SQPX-ray2.70B1-453[»]
1SQQX-ray3.00B15-453[»]
1SQVX-ray2.85B15-453[»]
1SQXX-ray2.60B15-453[»]
2A06X-ray2.10B/O15-453[»]
2BCCX-ray3.50B32-453[»]
2FYUX-ray2.26B15-453[»]
2YBBelectron microscopy19.00B/b15-453[»]
3BCCX-ray3.70B32-453[»]
4D6TX-ray3.57B/O1-453[»]
4D6UX-ray4.09B/O1-453[»]
5KLVX-ray2.65B15-453[»]
ProteinModelPortaliP23004.
SMRiP23004.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-1106N.
IntActiP23004. 2 interactors.
MINTiMINT-149969.
STRINGi9913.ENSBTAP00000028853.

Protein family/group databases

MEROPSiM16.974.

Proteomic databases

PaxDbiP23004.
PeptideAtlasiP23004.
PRIDEiP23004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000028853; ENSBTAP00000028853; ENSBTAG00000021651.
GeneIDi282394.
KEGGibta:282394.

Organism-specific databases

CTDi7385.

Phylogenomic databases

eggNOGiKOG2583. Eukaryota.
COG0612. LUCA.
GeneTreeiENSGT00550000074666.
HOGENOMiHOG000046923.
HOVERGENiHBG055236.
InParanoidiP23004.
KOiK00415.
OMAiNPQAHVI.
OrthoDBiEOG091G0A7X.
TreeFamiTF105033.

Enzyme and pathway databases

ReactomeiR-BTA-611105. Respiratory electron transport.

Miscellaneous databases

EvolutionaryTraceiP23004.

Gene expression databases

BgeeiENSBTAG00000021651.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 3 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQCR2_BOVIN
AccessioniPrimary (citable) accession number: P23004
Secondary accession number(s): Q3ZCG7, Q5E9C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 143 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

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.