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P24958 (CYB_LOXAF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cytochrome b
Alternative name(s):
Complex III subunit 3
Complex III subunit III
Cytochrome b-c1 complex subunit 3
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Gene names
Name:MT-CYB
Synonyms:COB, CYTB, MTCYB
Encoded onMitochondrion
OrganismLoxodonta africana (African elephant) [Reference proteome]
Taxonomic identifier9785 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaAfrotheriaProboscideaElephantidaeLoxodonta

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis By similarity.

Cofactor

Binds 2 heme groups non-covalently By similarity.

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) By similarity.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein By similarity.

Miscellaneous

Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm By similarity.

Sequence similarities

Belongs to the cytochrome b family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Cytochrome b
PRO_0000061136

Regions

Transmembrane33 – 5321Helical; Potential
Transmembrane76 – 9823Helical; Potential
Transmembrane116 – 13621Helical; Potential
Transmembrane140 – 15819Helical; Potential
Transmembrane178 – 19821Helical; Potential
Transmembrane229 – 24921Helical; Potential
Transmembrane288 – 30821Helical; Potential
Transmembrane323 – 34321Helical; Potential
Transmembrane348 – 36821Helical; Potential

Sites

Metal binding831Iron 1 (heme b562 axial ligand)
Metal binding971Iron 2 (heme b566 axial ligand)
Metal binding1821Iron 1 (heme b562 axial ligand)
Metal binding1961Iron 2 (heme b566 axial ligand)

Experimental info

Sequence conflict31H → D in CAA39732. Ref.1
Sequence conflict271I → M in CAA39732. Ref.1
Sequence conflict1501F → L in CAA39732. Ref.1
Sequence conflict1551Y → C in BAA25012. Ref.2
Sequence conflict1551Y → C in BAA25013. Ref.2
Sequence conflict2121T → I in BAA25012. Ref.2
Sequence conflict2121T → I in BAA25013. Ref.2
Sequence conflict2491M → H in CAA39732. Ref.1
Sequence conflict257 – 2604MPAD → TLAN in CAA39732. Ref.1
Sequence conflict264 – 2663TPL → NPP in CAA39732. Ref.1
Sequence conflict322 – 3254QVLF → LCAYC in CAA39732. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24958 [UniParc].

Last modified January 27, 2003. Version 2.
Checksum: 05E75F539C8F9D6F

FASTA37842,740
        10         20         30         40         50         60 
MTHIRKSHPL LKIINKSFID LPTPSNISTW WNFGSLLGAC LITQILTGLF LAMHYTPDTM 

        70         80         90        100        110        120 
TAFSSMSHIC RDVNYGWIIR QLHSNGASIF FLCLYTHIGR NIYYGSYLYS ETWNTGIMLL 

       130        140        150        160        170        180 
LITMATAFMG YVLPWGQMSF WGATVITNLF SAIPYIGTNL VEWIWGGFSV DKATLNRFFA 

       190        200        210        220        230        240 
LHFILPFTMI ALAGVHLTFL HETGSNNPLG LTSDSDKIPF HPYYTIKDFL GLLILILLLL 

       250        260        270        280        290        300 
LLALLSPDML GDPDNYMPAD PLNTPLHIKP EWYFLFAYAI LRSVPNKLGG VLALLLSILI 

       310        320        330        340        350        360 
LGLMPLLHTS KHRSMMLRPL SQVLFWTLTM DLLTLTWIGS QPVEYPYIII GQMASILYFS 

       370 
IILAFLPIAG VIENYLIK 

« Hide

References

[1]"Evolution of the cytochrome b gene of mammals."
Irwin D.M., Kocher T.D., Wilson A.C.
J. Mol. Evol. 32:128-144(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular phylogenetic inference of the woolly mammoth Mammuthus primigenius, based on complete sequences of mitochondrial cytochrome b and 12S ribosomal RNA genes."
Noro M., Masuda R., Dubrovo I.A., Yoshida M.C., Kato M.
J. Mol. Evol. 46:314-326(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete mitochondrial genome sequence of the African elephant (Loxodonta africana), phylogenetic relationships of Proboscidea to other mammals and D-loop heteroplasmy."
Hauf J., Waddell P.J., Chalwatzis N., Joger U., Zimmermann F.K.
Zoology 102:184-195(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[4]"Molecular phylogeny of Elephantidae. Extreme divergence of the extant forest African elephant."
Barriel V., Thuet E., Tassy P.
C. R. Acad. Sci. III, Sci. Vie 322:447-454(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-376.
[5]"Phylogenetic resolution within the Elephantidae using fossil DNA sequence from the American mastodon (Mammut americanum) as an outgroup."
Yang H., Golenberg E.M., Shoshani J.
Proc. Natl. Acad. Sci. U.S.A. 93:1190-1194(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-106.
[6]Mueller S., Steinborn R., Mueller M.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-378.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56285 Genomic DNA. Translation: CAA39732.1.
D84150 Genomic DNA. Translation: BAA25011.1.
D84151 Genomic DNA. Translation: BAA25012.1.
D84152 Genomic DNA. Translation: BAA25013.1.
AJ224821 Genomic DNA. Translation: CAA12150.1.
AF132528 Genomic DNA. Translation: AAD44171.1.
U23741 Genomic DNA. Translation: AAA73784.1.
AF219242 Genomic DNA. Translation: AAG44238.1.
PIRS17412. T45562.
RefSeqNP_009291.1. NC_000934.1.

3D structure databases

ProteinModelPortalP24958.
SMRP24958. Positions 1-378.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSLAFT00000038069; ENSLAFP00000029503; ENSLAFG00000033303.
GeneID808783.

Organism-specific databases

CTD4519.

Phylogenomic databases

HOVERGENHBG017694.
ProtClustDBMTH00100.

Family and domain databases

InterProIPR016175. Cyt_b/b6.
IPR005798. Cyt_b/b6_C.
IPR005797. Cyt_b/b6_N.
IPR016174. Di-haem_cyt_TM.
[Graphical view]
PANTHERPTHR19271. PTHR19271. 1 hit.
PfamPF00032. Cytochrom_B_C. 1 hit.
PF13631. Cytochrom_B_N_2. 1 hit.
[Graphical view]
SUPFAMSSF81648. Cytochrome_b/b6_C. 1 hit.
SSF81342. Transmembr_di-haem_cytochrome. 1 hit.
PROSITEPS51003. CYTB_CTER. 1 hit.
PS51002. CYTB_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYB_LOXAF
AccessionPrimary (citable) accession number: P24958
Secondary accession number(s): O47887 expand/collapse secondary AC list , O48349, Q9G5G0, Q9XNF4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 27, 2003
Last modified: May 1, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families