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P91682

- SMO_DROME

UniProt

P91682 - SMO_DROME

Protein

Protein smoothened

Gene

smo

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Segment polarity protein required for correct patterning of every segment. G protein-coupled receptor that associates with the patched protein (ptc) to transduce the hedgehog (hh) signal through the activation of an inhibitory G-protein. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu).

    GO - Molecular functioni

    1. G-protein coupled receptor activity Source: FlyBase
    2. hedgehog receptor activity Source: FlyBase
    3. PDZ domain binding Source: RefGenome
    4. protein binding Source: UniProtKB
    5. transmembrane signaling receptor activity Source: FlyBase
    6. Wnt-activated receptor activity Source: RefGenome
    7. Wnt-protein binding Source: RefGenome

    GO - Biological processi

    1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: FlyBase
    2. anterior/posterior lineage restriction, imaginal disc Source: FlyBase
    3. axon extension involved in axon guidance Source: RefGenome
    4. blastoderm segmentation Source: FlyBase
    5. Bolwig's organ morphogenesis Source: FlyBase
    6. canonical Wnt signaling pathway Source: RefGenome
    7. cardioblast differentiation Source: RefGenome
    8. cerebellar cortex morphogenesis Source: RefGenome
    9. ciliary receptor clustering involved in smoothened signaling pathway Source: RefGenome
    10. determination of left/right symmetry Source: RefGenome
    11. eye-antennal disc morphogenesis Source: FlyBase
    12. eye morphogenesis Source: FlyBase
    13. gonad development Source: RefGenome
    14. heart morphogenesis Source: RefGenome
    15. negative regulation of apoptotic process Source: RefGenome
    16. negative regulation of G1/S transition of mitotic cell cycle Source: FlyBase
    17. negative regulation of Notch signaling pathway Source: FlyBase
    18. neuron fate commitment Source: RefGenome
    19. neuron projection regeneration Source: RefGenome
    20. ovarian follicle cell development Source: FlyBase
    21. positive regulation of establishment of protein localization to plasma membrane Source: FlyBase
    22. positive regulation of neuroblast proliferation Source: RefGenome
    23. positive regulation of smoothened signaling pathway Source: RefGenome
    24. regulation of apoptotic process Source: FlyBase
    25. regulation of mitotic cell cycle Source: FlyBase
    26. signal transduction Source: FlyBase
    27. smoothened signaling pathway Source: FlyBase
    28. smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation Source: RefGenome
    29. somatic stem cell maintenance Source: FlyBase
    30. vasculogenesis Source: RefGenome
    31. wing disc anterior/posterior pattern formation Source: FlyBase
    32. Wnt signaling pathway Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein, G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    SignaLinkiP91682.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein smoothened
    Alternative name(s):
    SMOH
    Smooth
    dSMO
    Gene namesi
    Name:smo
    ORF Names:CG11561
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0003444. smo.

    Subcellular locationi

    GO - Cellular componenti

    1. cilium Source: RefGenome
    2. cytoplasm Source: RefGenome
    3. endosome Source: FlyBase
    4. integral component of membrane Source: FlyBase
    5. integral component of plasma membrane Source: FlyBase
    6. neuronal cell body Source: RefGenome
    7. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 10361005Protein smoothenedPRO_0000013019Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi90 ↔ 1551 PublicationPROSITE-ProRule annotation
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi100 ↔ 1481 PublicationPROSITE-ProRule annotation
    Disulfide bondi139 ↔ 1791 PublicationPROSITE-ProRule annotation
    Disulfide bondi172 ↔ 1941 PublicationPROSITE-ProRule annotation
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi218 ↔ 238PROSITE-ProRule annotation
    Disulfide bondi242 ↔ 320PROSITE-ProRule annotation
    Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi339 ↔ 413PROSITE-ProRule annotation
    Glycosylationi419 – 4191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi513 ↔ 525PROSITE-ProRule annotation
    Modified residuei658 – 6581Phosphoserine1 Publication
    Modified residuei659 – 6591Phosphoserine1 Publication
    Modified residuei667 – 6671Phosphoserine1 Publication
    Modified residuei670 – 6701Phosphoserine1 Publication
    Modified residuei673 – 6731Phosphoserine1 Publication
    Modified residuei687 – 6871Phosphoserine1 Publication
    Modified residuei690 – 6901Phosphoserine1 Publication
    Modified residuei693 – 6931Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiP91682.

    Expressioni

    Developmental stagei

    Expressed at all developmental stages, though the levels vary.

    Gene expression databases

    BgeeiP91682.

    Interactioni

    Subunit structurei

    Interacts with cos.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    cosO168445EBI-142245,EBI-102069

    Protein-protein interaction databases

    BioGridi59452. 17 interactions.
    DIPiDIP-19956N.
    IntActiP91682. 3 interactions.
    MINTiMINT-811118.

    Structurei

    Secondary structure

    1
    1036
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi94 – 963
    Beta strandi108 – 1103
    Helixi112 – 1143
    Helixi120 – 13112
    Helixi132 – 1354
    Helixi137 – 1404
    Helixi146 – 1516
    Beta strandi156 – 1605
    Beta strandi162 – 1654
    Helixi169 – 1768
    Helixi180 – 1823
    Helixi189 – 1924

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MAHNMR-A85-202[»]
    ProteinModelPortaliP91682.
    SMRiP91682. Positions 76-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 258227ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini280 – 2878CytoplasmicSequence Analysis
    Topological domaini309 – 33931ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini361 – 38121CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini403 – 42119ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini443 – 46927CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini491 – 53242ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini554 – 1036483CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei259 – 27921Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei288 – 30821Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei340 – 36021Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei382 – 40221Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei422 – 44221Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei470 – 49021Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei533 – 55321Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini85 – 206122FZPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi816 – 8194Poly-Ser

    Sequence similaritiesi

    Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG312505.
    GeneTreeiENSGT00750000117492.
    InParanoidiP91682.
    KOiK06226.
    OMAiNANKYPA.
    OrthoDBiEOG74J972.
    PhylomeDBiP91682.

    Family and domain databases

    Gene3Di1.10.2000.10. 1 hit.
    InterProiIPR000539. Frizzled.
    IPR015526. Frizzled/SFRP.
    IPR020067. Frizzled_dom.
    IPR017981. GPCR_2-like.
    IPR026544. SMO.
    [Graphical view]
    PANTHERiPTHR11309. PTHR11309. 1 hit.
    PTHR11309:SF35. PTHR11309:SF35. 1 hit.
    PfamiPF01534. Frizzled. 1 hit.
    PF01392. Fz. 1 hit.
    [Graphical view]
    PRINTSiPR00489. FRIZZLED.
    SMARTiSM00063. FRI. 1 hit.
    [Graphical view]
    SUPFAMiSSF63501. SSF63501. 1 hit.
    PROSITEiPS50038. FZ. 1 hit.
    PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P91682-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQYLNFPRMP NIMMFLEVAI LCLWVVADAS ASSAKFGSTT PASAQQSDVE     50
    LEPINGTLNY RLYAKKGRDD KPWFDGLDSR HIQCVRRARC YPTSNATNTC 100
    FGSKLPYELS SLDLTDFHTE KELNDKLNDY YALKHVPKCW AAIQPFLCAV 150
    FKPKCEKING EDMVYLPSYE MCRITMEPCR ILYNTTFFPK FLRCNETLFP 200
    TKCTNGARGM KFNGTGQCLS PLVPTDTSAS YYPGIEGCGV RCKDPLYTDD 250
    EHRQIHKLIG WAGSICLLSN LFVVSTFFID WKNANKYPAV IVFYINLCFL 300
    IACVGWLLQF TSGSREDIVC RKDGTLRHSE PTAGENLSCI VIFVLVYYFL 350
    TAGMVWFVFL TYAWHWRAMG HVQDRIDKKG SYFHLVAWSL PLVLTITTMA 400
    FSEVDGNSIV GICFVGYINH SMRAGLLLGP LCGVILIGGY FITRGMVMLF 450
    GLKHFANDIK STSASNKIHL IIMRMGVCAL LTLVFILVAI ACHVTEFRHA 500
    DEWAQSFRQF IICKISSVFE EKSSCRIENR PSVGVLQLHL LCLFSSGIVM 550
    STWCWTPSSI ETWKRYIRKK CGKEVVEEVK MPKHKVIAQT WAKRKDFEDK 600
    GRLSITLYNT HTDPVGLNFD VNDLNSSETN DISSTWAAYL PQCVKRRMAL 650
    TGAATGNSSS HGPRKNSLDS EISVSVRHVS VESRRNSVDS QVSVKIAEMK 700
    TKVASRSRGK HGGSSSNRRT QRRRDYIAAA TGKSSRRRES STSVESQVIA 750
    LKKTTYPNAS HKVGVFAHHS SKKQHNYTSS MKRRTANAGL DPSILNEFLQ 800
    KNGDFIFPFL QNQDMSSSSE EDNSRASQKI QDLNVVVKQQ EISEDDHDGI 850
    KIEELPNSKQ VALENFLKNI KKSNESNSNR HSRNSARSQS KKSQKRHLKN 900
    PAADLDFRKD CVKYRSNDSL SCSSEELDVA LDVGSLLNSS FSGISMGKPH 950
    SRNSKTSCDV GIQANPFELV PSYGEDELQQ AMRLLNAASR QRTEAANEDF 1000
    GGTELQGLLG HSHRHQREPT FMSESDKLKM LLLPSK 1036
    Length:1,036
    Mass (Da):116,552
    Last modified:May 1, 1997 - v1
    Checksum:i7797FC71A539A87A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U87613 Genomic DNA. Translation: AAC33180.1.
    AF030334 Genomic DNA. Translation: AAB84275.1.
    AE014134 Genomic DNA. Translation: AAF51518.2.
    BT053691 mRNA. Translation: ACK77608.1.
    PIRiS71804.
    RefSeqiNP_523443.1. NM_078719.3.
    UniGeneiDm.244.

    Genome annotation databases

    EnsemblMetazoaiFBtr0078129; FBpp0077788; FBgn0003444.
    GeneIDi33196.
    KEGGidme:Dmel_CG11561.
    UCSCiCG11561-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U87613 Genomic DNA. Translation: AAC33180.1 .
    AF030334 Genomic DNA. Translation: AAB84275.1 .
    AE014134 Genomic DNA. Translation: AAF51518.2 .
    BT053691 mRNA. Translation: ACK77608.1 .
    PIRi S71804.
    RefSeqi NP_523443.1. NM_078719.3.
    UniGenei Dm.244.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MAH NMR - A 85-202 [» ]
    ProteinModelPortali P91682.
    SMRi P91682. Positions 76-202.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 59452. 17 interactions.
    DIPi DIP-19956N.
    IntActi P91682. 3 interactions.
    MINTi MINT-811118.

    Protein family/group databases

    GPCRDBi Search...

    Proteomic databases

    PRIDEi P91682.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0078129 ; FBpp0077788 ; FBgn0003444 .
    GeneIDi 33196.
    KEGGi dme:Dmel_CG11561.
    UCSCi CG11561-RA. d. melanogaster.

    Organism-specific databases

    CTDi 6608.
    FlyBasei FBgn0003444. smo.

    Phylogenomic databases

    eggNOGi NOG312505.
    GeneTreei ENSGT00750000117492.
    InParanoidi P91682.
    KOi K06226.
    OMAi NANKYPA.
    OrthoDBi EOG74J972.
    PhylomeDBi P91682.

    Enzyme and pathway databases

    SignaLinki P91682.

    Miscellaneous databases

    GenomeRNAii 33196.
    NextBioi 782367.
    PROi P91682.

    Gene expression databases

    Bgeei P91682.

    Family and domain databases

    Gene3Di 1.10.2000.10. 1 hit.
    InterProi IPR000539. Frizzled.
    IPR015526. Frizzled/SFRP.
    IPR020067. Frizzled_dom.
    IPR017981. GPCR_2-like.
    IPR026544. SMO.
    [Graphical view ]
    PANTHERi PTHR11309. PTHR11309. 1 hit.
    PTHR11309:SF35. PTHR11309:SF35. 1 hit.
    Pfami PF01534. Frizzled. 1 hit.
    PF01392. Fz. 1 hit.
    [Graphical view ]
    PRINTSi PR00489. FRIZZLED.
    SMARTi SM00063. FRI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF63501. SSF63501. 1 hit.
    PROSITEi PS50038. FZ. 1 hit.
    PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Drosophila smoothened gene encodes a seven-pass membrane protein, a putative receptor for the hedgehog signal."
      Alcedo J., Ayzenzon M., von Ohlen T., Noll M., Hooper J.E.
      Cell 86:221-232(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "smoothened encodes a receptor-like serpentine protein required for hedgehog signalling."
      van den Heuvel M., Ingham P.W.
      Nature 382:547-551(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
    6. "Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus."
      Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.
      Dev. Cell 8:267-278(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COS.
    7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658; SER-659; SER-667; SER-670; SER-673; SER-687; SER-690 AND SER-693, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.
    8. "Structural insights into the role of the Smoothened cysteine-rich domain in Hedgehog signalling."
      Rana R., Carroll C.E., Lee H.J., Bao J., Marada S., Grace C.R., Guibao C.D., Ogden S.K., Zheng J.J.
      Nat. Commun. 4:2965-2974(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 85-202, DISULFIDE BONDS.

    Entry informationi

    Entry nameiSMO_DROME
    AccessioniPrimary (citable) accession number: P91682
    Secondary accession number(s): B7FNK1, Q9VPM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Caution

    It is uncertain whether Met-1, Met-9, Met-13 or Met-14 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3