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BOSS_DROME
ID   BOSS_DROME              Reviewed;         896 AA.
AC   P22815; Q9VBJ5;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Protein bride of sevenless;
DE   Flags: Precursor;
GN   Name=boss; ORFNames=CG8285;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2276620; DOI=10.1101/gad.4.11.1835;
RA   Hart A.C., Kraemer H., van Vactor D.L. Jr., Paidhungat M., Zipursky S.L.;
RT   "Induction of cell fate in the Drosophila retina: the bride of sevenless
RT   protein is predicted to contain a large extracellular domain and seven
RT   transmembrane segments.";
RL   Genes Dev. 4:1835-1847(1990).
RN   [2]
RP   SEQUENCE REVISION.
RA   Kraemer H.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=1857416; DOI=10.1038/352207a0;
RA   Kraemer H., Cagan R.L., Zipursky S.L.;
RT   "Interaction of bride of sevenless membrane-bound ligand and the sevenless
RT   tyrosine-kinase receptor.";
RL   Nature 352:207-212(1991).
CC   -!- FUNCTION: Acts as a ligand for sevenless tyrosine-kinase receptor
CC       during eye development. {ECO:0000269|PubMed:1857416}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed exclusively by R8 photoreceptor cells and
CC       is internalized in a sev-dependent manner by R7 cells.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC       {ECO:0000305}.
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DR   EMBL; X55887; CAA39373.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF56539.1; -; Genomic_DNA.
DR   RefSeq; NP_542440.1; NM_080709.3.
DR   AlphaFoldDB; P22815; -.
DR   BioGRID; 68046; 6.
DR   IntAct; P22815; 1.
DR   STRING; 7227.FBpp0084323; -.
DR   GlyGen; P22815; 4 sites.
DR   PaxDb; P22815; -.
DR   PRIDE; P22815; -.
DR   DNASU; 43146; -.
DR   EnsemblMetazoa; FBtr0084949; FBpp0084323; FBgn0000206.
DR   GeneID; 43146; -.
DR   KEGG; dme:Dmel_CG8285; -.
DR   CTD; 43146; -.
DR   FlyBase; FBgn0000206; boss.
DR   VEuPathDB; VectorBase:FBgn0000206; -.
DR   eggNOG; KOG1056; Eukaryota.
DR   HOGENOM; CLU_010513_1_0_1; -.
DR   InParanoid; P22815; -.
DR   OMA; LQQCTQY; -.
DR   OrthoDB; 671877at2759; -.
DR   PhylomeDB; P22815; -.
DR   Reactome; R-DME-418594; G alpha (i) signalling events.
DR   Reactome; R-DME-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR   SignaLink; P22815; -.
DR   BioGRID-ORCS; 43146; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 43146; -.
DR   PRO; PR:P22815; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0000206; Expressed in head capsule and 7 other tissues.
DR   ExpressionAtlas; P22815; baseline and differential.
DR   Genevisible; P22815; DM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0035997; C:rhabdomere microvillus membrane; IDA:FlyBase.
DR   GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR   GO; GO:0099530; F:G protein-coupled receptor activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR   GO; GO:0005118; F:sevenless binding; IDA:FlyBase.
DR   GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
DR   GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
DR   GO; GO:0007465; P:R7 cell fate commitment; IMP:FlyBase.
DR   GO; GO:0045470; P:R8 cell-mediated photoreceptor organization; IMP:FlyBase.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR   GO; GO:0009749; P:response to glucose; IMP:FlyBase.
DR   GO; GO:0045500; P:sevenless signaling pathway; IDA:FlyBase.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR002956; Bride_of_7less.
DR   InterPro; IPR017978; GPCR_3_C.
DR   Pfam; PF00003; 7tm_3; 1.
DR   PRINTS; PR01223; BRIDEOF7LESS.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Sensory transduction; Signal; Transducer;
KW   Transmembrane; Transmembrane helix; Vision.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..896
FT                   /note="Protein bride of sevenless"
FT                   /id="PRO_0000012971"
FT   TOPO_DOM        32..530
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        531..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        570..588
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        615..637
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        655..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        693..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        728..748
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        759..781
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        782..896
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          38..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        474
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   896 AA;  99950 MW;  580AEBC0FA208E24 CRC64;
     MKVMDALQSG RRKPLPVALL CILVTVFCVL ECHGADLTSP TKKSAPLRIT KPQPTSQQAK
     PISITTRAPT TVASTTDDEV SSSVDGQLAP LISSTTEGPS SGTTASLVPE ICLNGLQLTV
     NSADEGTVIR KQEEFVKILE GDVVLSVLTK DPDSALFVIN RVNQANLIMA DFEIGIRAIS
     IDNASLAENL LIQEVQFLQQ CTTYSMGIFV DWELYKQLES VIKDLEYNIW PIPGTRAHLF
     PKVAHLLHQM PWGEKIASVE IATETLEMYN EFMEAARQEH MCLMHFKSDD NVYIMFGNKL
     ASHFKENGTL FSVPTDRTDD EFLADLPNRA FVLMENEIDL STAVELDATP TALDEILIGK
     SVLPSRVLSF AGSIIDLMNW LRGSLSKHCK RGEEHDLYVL ESCFNFLNFI EDWRTSEYRQ
     AHDTAEILSL LLMRKLGTAM NFQMYQKKVL TLDKITGESR TELREIASQN FVTNVTTYYH
     YNRDNHTSLE LKTKFGQVFN CQYSAGDNRR YPFLFDGESV MFWRIKMDTW VATGLTAAIL
     GLIATLAILV FIVVRISLGD VFEGNPTTSI LLLLSLILVF CSFVPYSIEY VGEQRNSHVT
     FEDAQTLNTL CAVRVFIMTL VYCFVFSLLL CRAVMLASIG SEGGFLSHVN GYIQAVICAF
     SVVAQVGMSV QLLVVMHVAS ETVSCENIYY GRWLWGLLAY DFALLCCVGA LIPSIYRSQR
     NYREGILIVI GSVLIMVIWV AWIALSLFGD EWRDAAIPLG LQASGWAVLV GILIPRTFLI
     VRGIERSDIA QALPSLTSLA FAQNNQYSSE QSVYECVNPA MRHCSQDEVN HQSPSEIPTL
     PLRGGGPRRQ QFFANLRQAN ANINPQRPPP RPQQSPSRSS VSSLPPSPDH NKITRF
 
 
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