Cytochrome c1, heme protein, mitochondrial precursor

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P00125 (CY1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytochrome c1, heme protein, mitochondrial

Alternative name(s):
Complex III subunit 4
Complex III subunit IV
Cytochrome b-c1 complex subunit 4
Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit
Short name=Cytochrome c-1

Gene names

Name:

CYC1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	325 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 the heme-containing component of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain.
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; Single-pass membrane protein; Intermembrane side.
Post-translational modification	Binds 1 heme group per subunit.
Sequence similarities	Belongs to the cytochrome c family. Contains 1 cytochrome c domain.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
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 transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from sequence or structural similarity. Source: AgBase respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding 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 – 84

Mitochondrion Ref.2

Chain

85 – 325

241

Cytochrome c1, heme protein, mitochondrial

PRO_0000108416

Regions

Transmembrane

292 – 306

Helical; Note=Anchors to the membrane; Potential

Domain

108 – 209

102

Cytochrome c

Sites

Metal binding

125

Iron (heme axial ligand)

Metal binding

244

Iron (heme axial ligand) By similarity

Binding site

121

Heme (covalent)

Binding site

124

Heme (covalent)

Secondary structure

325

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00125 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: 588ED1DEFEAABD6D
Show »

FASTA

325

35,297

        10         20         30         40         50         60 
MAAAAATLRG AMVGPRGAGL PGARARGLLC GARPGQLPLR TPQAVSLSSK SGLSRGRKVI 

        70         80         90        100        110        120 
LSALGMLAAG GAGLAVALHS AVSASDLELH PPSYPWSHRG LLSSLDHTSI RRGFQVYKQV 

       130        140        150        160        170        180 
CSSCHSMDYV AYRHLVGVCY TEDEAKALAE EVEVQDGPNE DGEMFMRPGK LSDYFPKPYP 

       190        200        210        220        230        240 
NPEAARAANN GALPPDLSYI VRARHGGEDY VFSLLTGYCE PPTGVSLREG LYFNPYFPGQ 

       250        260        270        280        290        300 
AIGMAPPIYN EVLEFDDGTP ATMSQVAKDV CTFLRWAAEP EHDHRKRMGL KMLLMMGLLL 

       310        320 
PLVYAMKRHK WSVLKSRKLA YRPPK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver.
[2]	"Structural studies of bovine heart cytochrome c1." Wakabayashi S., Matsubara H., Kim C.H., King T.E. J. Biol. Chem. 257:9335-9344(1982) [PubMed: 6286615] [Abstract] Cited for: PROTEIN SEQUENCE OF 85-325. Tissue: Heart.
[3]	"Partial genomic sequence of the bovine cytochrome c1 gene." Band M., Ron M. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-194. Strain: Holstein-Friesian.
[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: 9204897] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 85-321.
[5]	"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: 9651245] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 85-321.
[6]	"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: 12269811] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
[7]	"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: 15312779] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
[8]	"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: 16024040] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]	"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: 16924113] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BC109917 mRNA. Translation: AAI09918.1.
U97172 Genomic DNA. Translation: AAB57834.1.

IPI

IPI00908005.

PIR

CCBO1. A00118.

RefSeq

NP_001033179.1. NM_001038090.1.

UniGene

Bt.1808.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BCC	X-ray	3.16	D	85-325	[»]
1BE3	X-ray	3.00	D	85-325	[»]
1BGY	X-ray	3.00	D/P	85-325	[»]
1L0L	X-ray	2.35	D	85-325	[»]
1L0N	X-ray	2.60	D	85-325	[»]
1NTK	X-ray	2.60	D	85-325	[»]
1NTM	X-ray	2.40	D	85-325	[»]
1NTZ	X-ray	2.60	D	85-325	[»]
1NU1	X-ray	3.20	D	85-325	[»]
1PP9	X-ray	2.10	D/Q	85-325	[»]
1PPJ	X-ray	2.10	D/Q	85-325	[»]
1QCR	X-ray	2.70	D	251-325	[»]
1SQB	X-ray	2.69	D	85-325	[»]
1SQP	X-ray	2.70	D	85-325	[»]
1SQQ	X-ray	3.00	D	85-325	[»]
1SQV	X-ray	2.85	D	85-325	[»]
1SQX	X-ray	2.60	D	85-325	[»]
2A06	X-ray	2.10	D/Q	85-325	[»]
2BCC	X-ray	3.50	D	85-325	[»]
2FYU	X-ray	2.26	D	85-325	[»]
2YBB	electron microscopy	19.00	D/d	85-325	[»]
3BCC	X-ray	3.70	D	85-325	[»]

ProteinModelPortal

P00125.

SMR

P00125. Positions 85-325.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00125. 9 interactions.

STRING

P00125.

Protein family/group databases

TCDB

3.D.3.2.1. proton-translocating quinol:cytochrome c reductase (QCR) superfamily.

Proteomic databases

PRIDE

P00125.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000016224; ENSBTAP00000016224; ENSBTAG00000012232.

GeneID

512500.

KEGG

bta:512500.

Organism-specific databases

CTD

1537.

Phylogenomic databases

eggNOG

maNOG14316.

HOVERGEN

HBG001239.

PhylomeDB

P00125.

Family and domain databases

InterPro

IPR002326. Cyt_c1.
IPR021157. Cyt_c1_TM_anchor_C.
IPR009056. Cyt_c_dom.
[Graphical view]

Gene3D

G3DSA:1.20.5.100. Cyt_c1_TM_anchor_C. 1 hit.
G3DSA:1.10.760.10. Cytochrome_c_R. 1 hit.

K00413.

PANTHER

PTHR10266. Cyt_C1. 1 hit.

Pfam

PF02167. Cytochrom_C1. 1 hit.
[Graphical view]

PRINTS

PR00603. CYTOCHROMEC1.

SUPFAM

SSF81496. Cyt_c1_TM_anchor_C. 1 hit.
SSF46626. Cytochrome_c. 1 hit.

PROSITE

PS51007. CYTC. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CY1_BOVIN

Accession

Primary (citable) accession number: P00125
Secondary accession number(s): Q2TBM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 27, 2006
Last modified:	December 14, 2011
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents