P19967 (CYB5R_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome b5-related protein

Alternative name(s):
Protein TU-36B

Gene names

Name:	Cyt-b5-r
ORF Names:	CG13279

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May play a role in muscle cell metabolism.
Tissue specificity	Muscle.
Sequence similarities	Contains 1 cytochrome b5 heme-binding domain.
Sequence caution	The sequence CAA33113.1 differs from that shown. Reason: Frameshift at position 348.

Ontologies

Keywords
Ligand	Heme Iron Metal-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	lipid particle Inferred from direct assay PubMed 16543254. Source: FlyBase mitochondrion Inferred from direct assay PubMed 10899459. Source: FlyBase
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 436	436	Cytochrome b5-related protein		PRO_0000166018
Regions
	Domain	16 – 100	85	Cytochrome b5 heme-binding
Sites
	Metal binding	59	1	Iron (heme axial ligand) By similarity
	Metal binding	82	1	Iron (heme axial ligand) By similarity
Natural variations
	Natural variant	202	1	A → P.
	Natural variant	213	1	I → T.
	Natural variant	344	1	R → G.
Experimental info
	Sequence conflict	219 – 220	2	FD → LN in CAA33113. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P19967 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: 77C77E49C6218A02	FASTA	436	50,355
	10 20 30 40 50 60 MVIEEWKKSG IATKFPTYRN SALITTHSWQ KGKRQDDGAE GLWRINDGIY DFTSFIDKHP 70 80 90 100 110 120 GGPFWIRETK GTDITEAFEA HHLTTAPEKM IAKYKVRDAA EPRIYTLTLE EGGFYKTLKE 130 140 150 160 170 180 RVREQLKTID KRPKKKSDLI HLGLVVSLYL LGIASAKYNS LLALVLASVA LCWTVIVSHN 190 200 210 220 230 240 YFHRRDNWQM YAFNLGMMNF AAWRVSHALS HHIYPNSYFD LELSMFEPLL CWVPNPHIKS 250 260 270 280 290 300 KLMRYVSWVT EPVAYALAFF IQMGTRIFYS LRHTNILYWH DLLPLTIPIA IYLGTGGSLG 310 320 330 340 350 360 IWICVRQWLA MTSIASFSFC LIGLNAAHHD PEIYHEGDAN REDRDWGLFQ VDTIIDRGDL 370 380 390 400 410 420 KWSQFLVLTH FGDHVLHHLF PTLDHGLLPA LYPVLYQTLD EFKGHLRECN HIEHMIGQHK 430 QLLRIEPNPR APGAGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of a muscle specific gene which is adjacent to the Drosophila myosin heavy-chain gene and can encode a cytochrome b related protein." Levin R.J., Boychuk P.L., Croniger C.M., Kazzaz J.A., Rozek C.E. Nucleic Acids Res. 17:6349-6367(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15008 Genomic DNA. Translation: CAA33113.1. Frameshift. AE014134 Genomic DNA. Translation: AAF53567.1. AY058287 mRNA. Translation: AAL13516.1.
PIR	S05441.
RefSeq	NP_001260514.1. NM_001273585.1. NP_477154.1. NM_057806.5.
UniGene	Dm.4208.
3D structure databases
ProteinModelPortal	P19967.
SMR	P19967. Positions 26-102.
ModBase	Search...
Protein-protein interaction databases
IntAct	P19967. 1 interaction.
MINT	MINT-1665002.
STRING	7227.FBpp0080486.
Proteomic databases
PaxDb	P19967.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0080932; FBpp0080486; FBgn0000406. FBtr0331931; FBpp0304264; FBgn0000406.
GeneID	35008.
KEGG	dme:Dmel_CG13279.
Organism-specific databases
CTD	35008.
FlyBase	FBgn0000406. Cyt-b5-r.
Phylogenomic databases
eggNOG	NOG86814.
GeneTree	ENSGT00520000056604.
InParanoid	P19967.
OMA	TEAFEAH.
OrthoDB	EOG40K6F4.
PhylomeDB	P19967.
Gene expression databases
Bgee	P19967.
GermOnline	CG13279. Drosophila melanogaster.
Family and domain databases
Gene3D	3.10.120.10. 1 hit.
InterPro	IPR001199. Cyt_B5-like_heme/steroid-bd. IPR018506. Cyt_B5_heme-BS. IPR012171. Fatty_acid/sphinglp_desaturase. IPR005804. Fatty_acid_desaturase-1. [Graphical view]
Pfam	PF00173. Cyt-b5. 1 hit. PF00487. FA_desaturase. 1 hit. [Graphical view]
PIRSF	PIRSF015921. FA_sphinglp_des. 1 hit.
SUPFAM	SSF55856. Cyt_B5. 1 hit.
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Cyt-b5-r. drosophila.
GenomeRNAi	35008.
NextBio	791390.

Entry information

Entry name

CYB5R_DROME

Accession

Primary (citable) accession number: P19967
Secondary accession number(s): Q9VJI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	June 21, 2005
Last modified:	April 3, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project