Reviewed, UniProtKB/Swiss-Prot Q9V4N3 (CYB5_DROME)

Names and origin

Protein names

Recommended name:
    Cytochrome b5
      Short name=CYTB5

Gene names

Name:	Cyt-b5
ORF Names:	CG2140

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	134 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side By similarity. Microsome membrane; Single-pass membrane protein; Cytoplasmic side 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	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Ligand	Heme Iron Metal-binding
Technical term	Complete 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	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lipid particle Inferred from direct assay. Source: FlyBase microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform B (identifier: Q9V4N3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform A (identifier: Q9V4N3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: MSSEETKTFTRAEVAKHNTNKDTWLLIHNNIYDVTAFLNE → MVQSKRNFARVLRIKVSVTLLAYKCQIKS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 134	134	Cytochrome b5		PRO_0000166016
Regions
	Transmembrane	111 – 131	21	Potential
	Domain	6 – 82	77	Cytochrome b5 heme-binding
Sites
	Metal binding	41	1	Iron (heme axial ligand) By similarity
	Metal binding	65	1	Iron (heme axial ligand) By similarity
Natural variations
	Alternative sequence	1 – 40	40	MSSEE…AFLNE → MVQSKRNFARVLRIKVSVTL LAYKCQIKS in isoform A.		VSP_008871

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 11D1FB03EFAB40DC	FASTA	134	15,206
	10 20 30 40 50 60 MSSEETKTFT RAEVAKHNTN KDTWLLIHNN IYDVTAFLNE HPGGEEVLIE QAGKDATENF 70 80 90 100 110 120 EDVGHSNDAR DMMKKYKIGE LVESERTSVA QKSEPTWSTE QQTEESSVKS WLVPLVLCLV 130 ATLFYKFFFG GAKQ
	Isoform A. Checksum: DF79BC1E406497B1	FASTA	123	13,904
	10 20 30 40 50 60 MVQSKRNFAR VLRIKVSVTL LAYKCQIKSH PGGEEVLIEQ AGKDATENFE DVGHSNDARD 70 80 90 100 110 120 MMKKYKIGEL VESERTSVAQ KSEPTWSTEQ QTEESSVKSW LVPLVLCLVA TLFYKFFFGG AKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Strain: Berkeley. Tissue: Head.
[4]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Strain: Berkeley. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013599 Genomic DNA. Translation: AAF59233.3. AE013599 Genomic DNA. Translation: AAG22305.2. BT001378 mRNA. Translation: AAN71133.1. BT004852 mRNA. Translation: AAO45208.1. BT015196 mRNA. Translation: AAT94425.1.
RefSeq	NP_610294.1. NP_724575.1.
UniGene	Dm.6903
3D structure databases
HSSP	HSSP built from PDB template 1EHB based on UniProtKB P00171.
SMR	Q9V4N3. Positions 3-88.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:22488N.
IntAct	Q9V4N3. 2 interactions.
Proteomic databases
PRIDE	Q9V4N3.
Genome annotation databases
Ensembl	FBgn0033189. Drosophila melanogaster. [Contig view]
GeneID	35688.
KEGG	dme:Dmel_CG2140.
NMPDR	fig|7227.3.peg.3676.
Organism-specific databases
FlyBase	FBgn0033189. Cyt-b5.
Phylogenomic databases
HOGENOM	Q9V4N3.
OMA	Q9V4N3. TAFLNEH.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-003239-MON.
Gene expression databases
ArrayExpress	Q9V4N3.
GermOnline	CG2140. Drosophila melanogaster.
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...
Other Resources
NextBio	794735.

Entry information

Entry name

CYB5_DROME

Accession

Primary (citable) accession number: Q9V4N3
Secondary accession number(s): Q6AWQ2, Q8IH75, Q9I7E0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project