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P19967

- CYB5R_DROME

UniProt

P19967 - CYB5R_DROME

Protein

Cytochrome b5-related protein

Gene

Cyt-b5-r

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    May play a role in muscle cell metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi59 – 591Iron (heme axial ligand)PROSITE-ProRule annotation
    Metal bindingi82 – 821Iron (heme axial ligand)PROSITE-ProRule annotation

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. 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 Source: InterPro

    GO - Biological processi

    1. fatty acid biosynthetic process Source: InterPro

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome b5-related protein
    Alternative name(s):
    Protein TU-36B
    Gene namesi
    Name:Cyt-b5-r
    ORF Names:CG13279
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0000406. Cyt-b5-r.

    Subcellular locationi

    GO - Cellular componenti

    1. lipid particle Source: FlyBase
    2. mitochondrion Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Cytochrome b5-related proteinPRO_0000166018Add
    BLAST

    Proteomic databases

    PaxDbiP19967.

    Expressioni

    Tissue specificityi

    Muscle.

    Gene expression databases

    BgeeiP19967.

    Interactioni

    Protein-protein interaction databases

    BioGridi61015. 3 interactions.
    IntActiP19967. 1 interaction.
    MINTiMINT-1665002.
    STRINGi7227.FBpp0080486.

    Structurei

    3D structure databases

    ProteinModelPortaliP19967.
    SMRiP19967. Positions 27-102.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 10085Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG86814.
    GeneTreeiENSGT00520000056604.
    InParanoidiP19967.
    OMAiRECNHIE.
    OrthoDBiEOG7FNC7D.
    PhylomeDBiP19967.

    Family and domain databases

    Gene3Di3.10.120.10. 1 hit.
    InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR018506. Cyt_B5_heme-BS.
    IPR012171. Fatty_acid/sphinglp_desaturase.
    IPR005804. Fatty_acid_desaturase-1.
    [Graphical view]
    PfamiPF00173. Cyt-b5. 1 hit.
    PF00487. FA_desaturase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015921. FA_sphinglp_des. 1 hit.
    SUPFAMiSSF55856. SSF55856. 1 hit.
    PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
    PS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19967-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVIEEWKKSG IATKFPTYRN SALITTHSWQ KGKRQDDGAE GLWRINDGIY    50
    DFTSFIDKHP GGPFWIRETK GTDITEAFEA HHLTTAPEKM IAKYKVRDAA 100
    EPRIYTLTLE EGGFYKTLKE RVREQLKTID KRPKKKSDLI HLGLVVSLYL 150
    LGIASAKYNS LLALVLASVA LCWTVIVSHN YFHRRDNWQM YAFNLGMMNF 200
    AAWRVSHALS HHIYPNSYFD LELSMFEPLL CWVPNPHIKS KLMRYVSWVT 250
    EPVAYALAFF IQMGTRIFYS LRHTNILYWH DLLPLTIPIA IYLGTGGSLG 300
    IWICVRQWLA MTSIASFSFC LIGLNAAHHD PEIYHEGDAN REDRDWGLFQ 350
    VDTIIDRGDL KWSQFLVLTH FGDHVLHHLF PTLDHGLLPA LYPVLYQTLD 400
    EFKGHLRECN HIEHMIGQHK QLLRIEPNPR APGAGK 436
    Length:436
    Mass (Da):50,355
    Last modified:June 21, 2005 - v2
    Checksum:i77C77E49C6218A02
    GO

    Sequence cautioni

    The sequence CAA33113.1 differs from that shown. Reason: Frameshift at position 348.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti219 – 2202FD → LN in CAA33113. (PubMed:2549511)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti202 – 2021A → P.
    Natural varianti213 – 2131I → T.
    Natural varianti344 – 3441R → G.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15008 Genomic DNA. Translation: CAA33113.1. Frameshift.
    AE014134 Genomic DNA. Translation: AAF53567.1.
    AY058287 mRNA. Translation: AAL13516.1.
    PIRiS05441.
    RefSeqiNP_001260514.1. NM_001273585.1.
    NP_477154.1. NM_057806.5.
    UniGeneiDm.4208.

    Genome annotation databases

    EnsemblMetazoaiFBtr0080932; FBpp0080486; FBgn0000406.
    FBtr0331931; FBpp0304264; FBgn0000406.
    GeneIDi35008.
    KEGGidme:Dmel_CG13279.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15008 Genomic DNA. Translation: CAA33113.1 . Frameshift.
    AE014134 Genomic DNA. Translation: AAF53567.1 .
    AY058287 mRNA. Translation: AAL13516.1 .
    PIRi S05441.
    RefSeqi NP_001260514.1. NM_001273585.1.
    NP_477154.1. NM_057806.5.
    UniGenei Dm.4208.

    3D structure databases

    ProteinModelPortali P19967.
    SMRi P19967. Positions 27-102.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61015. 3 interactions.
    IntActi P19967. 1 interaction.
    MINTi MINT-1665002.
    STRINGi 7227.FBpp0080486.

    Proteomic databases

    PaxDbi P19967.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0080932 ; FBpp0080486 ; FBgn0000406 .
    FBtr0331931 ; FBpp0304264 ; FBgn0000406 .
    GeneIDi 35008.
    KEGGi dme:Dmel_CG13279.

    Organism-specific databases

    CTDi 35008.
    FlyBasei FBgn0000406. Cyt-b5-r.

    Phylogenomic databases

    eggNOGi NOG86814.
    GeneTreei ENSGT00520000056604.
    InParanoidi P19967.
    OMAi RECNHIE.
    OrthoDBi EOG7FNC7D.
    PhylomeDBi P19967.

    Miscellaneous databases

    ChiTaRSi Cyt-b5-r. drosophila.
    GenomeRNAii 35008.
    NextBioi 791390.

    Gene expression databases

    Bgeei P19967.

    Family and domain databases

    Gene3Di 3.10.120.10. 1 hit.
    InterProi IPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR018506. Cyt_B5_heme-BS.
    IPR012171. Fatty_acid/sphinglp_desaturase.
    IPR005804. Fatty_acid_desaturase-1.
    [Graphical view ]
    Pfami PF00173. Cyt-b5. 1 hit.
    PF00487. FA_desaturase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015921. FA_sphinglp_des. 1 hit.
    SUPFAMi SSF55856. SSF55856. 1 hit.
    PROSITEi PS00191. CYTOCHROME_B5_1. 1 hit.
    PS50255. CYTOCHROME_B5_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiCYB5R_DROME
    AccessioniPrimary (citable) accession number: P19967
    Secondary accession number(s): Q9VJI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3