Reviewed, UniProtKB/Swiss-Prot Q5RDJ5 (CYB5B_PONAB)

Names and origin

Protein names

Recommended name:
    Cytochrome b5 type B
Alternative name(s):
    Cytochrome b5 outer mitochondrial membrane isoform

Gene names

Name:	CYB5B
Synonyms:	CYB5M

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases By similarity.
Subunit structure	Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2 By similarity.
Subcellular location	Mitochondrion outer membrane By similarity.
Sequence similarities	Belongs to the cytochrome b5 family. Contains 1 cytochrome b5 heme-binding domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Ligand	Heme Iron Metal-binding
PTM	Phosphoprotein
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 outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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
	Propeptide	1 – 11	11	By similarity		PRO_0000006475
	Chain	12 – 146	135	Cytochrome b5 type B		PRO_0000006476
Regions
	Transmembrane	118 – 140	23	Potential
	Domain	20 – 96	77	Cytochrome b5 heme-binding
Sites
	Metal binding	55	1	Iron (heme axial ligand) By similarity
	Metal binding	79	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Modified residue	33	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5RDJ5-1 [UniParc]. Last modified April 12, 2005. Version 2. Checksum: 2FF7703D00E27E18	FASTA	146	16,387
	10 20 30 40 50 60 MATAEASGSD GKGQEVETSV TYYRMEEVAK RNSLKELWLV IHGRVYDVTR FLNEHPGGEE 70 80 90 100 110 120 VLLEQAGVDA SESFEDVGHS SDAREMLKQY YIGDIHPSDL KPENGSKDPS KNDTCKSCWA 130 140 YWILPIIGAV LLGFLYRYYT PESKSS

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR857913 mRNA. Translation: CAH90162.1. Different initiation.
RefSeq	NP_001125049.1.
UniGene	Pab.19345
3D structure databases
SMR	Q5RDJ5. Positions 17-102.
ModBase	Search...
Genome annotation databases
GeneID	100171930.
Phylogenomic databases
HOVERGEN	Q5RDJ5.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit.
Pfam	PF00173. Cyt-b5. 1 hit. [Graphical view]
PRINTS	PR00363. CYTOCHROMEB5.
ProDom	PD000612. Cyt_B5. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYB5B_PONAB

Accession

Primary (citable) accession number: Q5RDJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	April 12, 2005
Last modified:	June 16, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)