P23004 (QCR2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

UQCRC2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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).
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence similarities	Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
Caution	Does not seem to have a protease activity as it lack the zinc-binding site.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metal ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 14

14

Mitochondrion Ref.4 Ref.5

Chain

15 – 453

439

Cytochrome b-c1 complex subunit 2, mitochondrial

PRO_0000026790

Amino acid modifications

Modified residue

250

1

N6-acetyllysine By similarity

Natural variations

Natural variant

41

1

T → R.

Secondary structure

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453

Helix Strand Turn

Details...

Beta strand

39 – 42

4

Beta strand

44 – 46

3

Beta strand

48 – 52

5

Beta strand

57 – 66

10

Helix

69 – 71

3

Turn

74 – 78

5

Helix

79 – 85

7

Turn

86 – 88

3

Beta strand

91 – 94

4

Helix

96 – 105

10

Beta strand

109 – 114

6

Beta strand

119 – 126

8

Helix

127 – 129

3

Helix

130 – 142

13

Helix

148 – 165

18

Helix

169 – 181

13

Beta strand

182 – 184

3

Helix

185 – 187

3

Helix

194 – 196

3

Turn

197 – 199

3

Helix

202 – 212

11

Helix

215 – 217

3

Beta strand

218 – 225

8

Helix

227 – 237

11

Beta strand

246 – 249

4

Beta strand

256 – 261

6

Beta strand

265 – 274

10

Beta strand

278 – 280

3

Helix

281 – 293

13

Beta strand

298 – 301

4

Helix

308 – 316

9

Beta strand

321 – 330

10

Beta strand

333 – 343

11

Helix

344 – 346

3

Helix

347 – 362

16

Helix

368 – 385

18

Helix

389 – 403

15

Helix

409 – 417

9

Helix

421 – 433

13

Beta strand

436 – 442

7

Helix

444 – 446

3

Helix

450 – 452

3

Sequences

	Sequence		Length	Mass (Da)
	P23004 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: B7C600DA71CD34CF	FASTA	453	48,149
	10 20 30 40 50 60 MKLLTRAGSL SRFYSLKVAP KVKATEAPAG VPPHPQDLEF TRLPNGLVIA SLENYAPASR 70 80 90 100 110 120 IGLFIKAGSR YENSNNLGTS HLLRLASSLT TKGASSFKIT RGIEAVGGKL SVTSTRENMA 130 140 150 160 170 180 YTVECLRDDV DILMEFLLNV TTAPEFRRWE VAALQPQLRI DKAVALQNPQ AHVIENLHAA 190 200 210 220 230 240 AYRNALANSL YCPDYRIGKV TPVELHDYVQ NHFTSARMAL IGLGVSHPVL KQVAEQFLNI 250 260 270 280 290 300 RGGLGLSGAK AKYHGGEIRE QNGDSLVHAA LVAESAAIGS AEANAFSVLQ HVLGAGPHVK 310 320 330 340 350 360 RGSNATSSLY QAVAKGVHQP FDVSAFNASY SDSGLFGFYT ISQAASAGDV IKAAYNQVKT 370 380 390 400 410 420 IAQGNLSNPD VQAAKNKLKA GYLMSVESSE GFLDEVGSQA LAAGSYTPPS TVLQQIDAVA 430 440 450 DADVINAAKK FVSGRKSMAA SGNLGHTPFI DEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.
[4]	"Complexity and tissue specificity of the mitochondrial respiratory chain." Capaldi R.A., Gonzalez-Halphen D., Zhang Y.-Z., Yanamura W. J. Bioenerg. Biomembr. 20:291-311(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 15-46.
[5]	"Subunit arrangement in beef heart complex III." Gonzalez-Halphen D., Lindorfer M.A., Capaldi R.M. Biochemistry 27:7021-7031(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 15-43.
[6]	"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).
[7]	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)
[8]	"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).
[9]	"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).
[10]	"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).
[11]	"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).
[12]	"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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59693 mRNA. Translation: CAA42214.1.
BT020993 mRNA. Translation: AAX09010.1.
BC102337 mRNA. Translation: AAI02338.1.

IPI

IPI00697827.

PIR

ZPBOC2. S16221.

RefSeq

NP_777055.1. NM_174630.2.

UniGene

Bt.27799.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BCC	X-ray	3.16	B	32-453	[»]
1BE3	X-ray	3.00	B	15-453	[»]
1BGY	X-ray	3.00	B/N	15-453	[»]
1L0L	X-ray	2.35	B	15-453	[»]
1L0N	X-ray	2.60	B	15-453	[»]
1NTK	X-ray	2.60	B	15-453	[»]
1NTM	X-ray	2.40	B	15-453	[»]
1NTZ	X-ray	2.60	B	15-453	[»]
1NU1	X-ray	3.20	B	15-453	[»]
1PP9	X-ray	2.10	B/O	15-453	[»]
1PPJ	X-ray	2.10	B/O	15-453	[»]
1QCR	X-ray	2.70	B	31-453	[»]
1SQB	X-ray	2.69	B	1-453	[»]
1SQP	X-ray	2.70	B	1-453	[»]
1SQQ	X-ray	3.00	B	15-453	[»]
1SQV	X-ray	2.85	B	15-453	[»]
1SQX	X-ray	2.60	B	15-453	[»]
2A06	X-ray	2.10	B/O	15-453	[»]
2FYU	X-ray	2.26	B	15-453	[»]
2YBB	electron microscopy	19.00	B/b	15-453	[»]
3BCC	X-ray	3.70	B	32-453	[»]

ProteinModelPortal

P23004.

SMR

P23004. Positions 29-453.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1106N.

IntAct

P23004. 2 interactions.

Protein family/group databases

MEROPS

M16.974.

Proteomic databases

PaxDb

P23004.

PRIDE

P23004.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000028853; ENSBTAP00000028853; ENSBTAG00000021651.

GeneID

282394.

KEGG

bta:282394.

Organism-specific databases

CTD

7385.

Phylogenomic databases

eggNOG

COG0612.

GeneTree

ENSGT00550000074666.

HOGENOM

HOG000046923.

HOVERGEN

HBG055236.

InParanoid

P23004.

KO

K00415.

OMA

FVSGQKS.

OrthoDB

EOG4QRH45.

Family and domain databases

Gene3D

3.30.830.10. 2 hits.

InterPro

IPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]

Pfam

PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]

SUPFAM

SSF63411. Metalloenz_metal-bd. 2 hits.

PROSITE

PS00143. INSULINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23004.

NextBio

20806181.

Entry information

Entry name

QCR2_BOVIN

Accession

Primary (citable) accession number: P23004
Secondary accession number(s): Q3ZCG7, Q5E9C7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	July 1, 1993
Last modified:	April 3, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program