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STAR_DROME
ID   STAR_DROME              Reviewed;         597 AA.
AC   P42519; Q9VPW0;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Protein Star;
GN   Name=S; ORFNames=CG4385;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=7924981; DOI=10.1242/dev.120.7.1731;
RA   Kolodkin A.L., Pickup A.T., Lin D., Goodman C.S., Banerjee U.;
RT   "Characterization of Star and its interactions with sevenless and EGF
RT   receptor during photoreceptor cell development in Drosophila.";
RL   Development 120:1731-1745(1994).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Testis;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=11672524; DOI=10.1016/s0092-8674(01)00526-8;
RA   Lee J.R., Urban S., Garvey C.F., Freeman M.;
RT   "Regulated intracellular ligand transport and proteolysis control EGF
RT   signal activation in Drosophila.";
RL   Cell 107:161-171(2001).
RN   [6]
RP   REVIEW.
RX   PubMed=11790319; DOI=10.1016/s0960-9822(01)00642-x;
RA   Klaembt C.;
RT   "EGF receptor signalling: roles of Star and Rhomboid revealed.";
RL   Curr. Biol. 12:R21-R23(2002).
CC   -!- FUNCTION: Involved in EGF receptor signaling. Has an early role in
CC       photoreceptor development. Interacts with the receptor torpedo in the
CC       eye. {ECO:0000269|PubMed:11672524, ECO:0000269|PubMed:7924981}.
CC   -!- SUBUNIT: Interacts with Spitz via the lumenal domain and mediates its
CC       transport to the Golgi.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC       II membrane protein. Golgi apparatus membrane; Single-pass type II
CC       membrane protein. Cell membrane; Single-pass type II membrane protein.
CC   -!- TISSUE SPECIFICITY: In the larval eye disk, expression is first seen at
CC       the morphogenetic furrow, then in the developing R2, R5, and R8 cells
CC       as well as in the posterior clusters of the disk in additional R cells.
CC       {ECO:0000269|PubMed:7924981}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos and larvae.
CC       {ECO:0000269|PubMed:7924981}.
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DR   EMBL; L31886; AAB04161.1; -; mRNA.
DR   EMBL; AE014134; AAF51425.1; -; Genomic_DNA.
DR   EMBL; AY113201; AAM29206.1; -; mRNA.
DR   RefSeq; NP_523450.1; NM_078726.4.
DR   RefSeq; NP_722674.1; NM_164403.2.
DR   AlphaFoldDB; P42519; -.
DR   BioGRID; 59534; 52.
DR   DIP; DIP-22174N; -.
DR   IntAct; P42519; 5.
DR   MINT; P42519; -.
DR   STRING; 7227.FBpp0077658; -.
DR   PaxDb; P42519; -.
DR   DNASU; 33281; -.
DR   EnsemblMetazoa; FBtr0077993; FBpp0077658; FBgn0003310.
DR   EnsemblMetazoa; FBtr0077994; FBpp0077659; FBgn0003310.
DR   GeneID; 33281; -.
DR   KEGG; dme:Dmel_CG4385; -.
DR   CTD; 33281; -.
DR   FlyBase; FBgn0003310; S.
DR   VEuPathDB; VectorBase:FBgn0003310; -.
DR   eggNOG; ENOG502S385; Eukaryota.
DR   HOGENOM; CLU_457313_0_0_1; -.
DR   InParanoid; P42519; -.
DR   OMA; YDETDHV; -.
DR   OrthoDB; 696505at2759; -.
DR   PhylomeDB; P42519; -.
DR   SignaLink; P42519; -.
DR   BioGRID-ORCS; 33281; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 33281; -.
DR   PRO; PR:P42519; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0003310; Expressed in cleaving embryo and 73 other tissues.
DR   ExpressionAtlas; P42519; baseline and differential.
DR   Genevisible; P42519; DM.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:FlyBase.
DR   GO; GO:0031902; C:late endosome membrane; IDA:FlyBase.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR   GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IMP:FlyBase.
DR   GO; GO:0046667; P:compound eye retinal cell programmed cell death; IMP:FlyBase.
DR   GO; GO:0048263; P:determination of dorsal identity; IMP:FlyBase.
DR   GO; GO:0035225; P:determination of genital disc primordium; IMP:FlyBase.
DR   GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:FlyBase.
DR   GO; GO:0016197; P:endosomal transport; IDA:FlyBase.
DR   GO; GO:0038004; P:epidermal growth factor receptor ligand maturation; IDA:FlyBase.
DR   GO; GO:0061331; P:epithelial cell proliferation involved in Malpighian tubule morphogenesis; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR   GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR   GO; GO:0043703; P:photoreceptor cell fate determination; IGI:FlyBase.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IDA:FlyBase.
DR   GO; GO:0042749; P:regulation of circadian sleep/wake cycle; IGI:FlyBase.
DR   GO; GO:0048865; P:stem cell fate commitment; IMP:FlyBase.
DR   GO; GO:0007421; P:stomatogastric nervous system development; IMP:FlyBase.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
PE   2: Evidence at transcript level;
KW   Cell membrane; Developmental protein; Endoplasmic reticulum;
KW   Golgi apparatus; Membrane; Reference proteome; Sensory transduction;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Vision.
FT   CHAIN           1..597
FT                   /note="Protein Star"
FT                   /id="PRO_0000072241"
FT   TOPO_DOM        1..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..597
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..243
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  65818 MW;  46B0A2F18B14486B CRC64;
     MSQQVFSAHP ALAVDQLQQA EQEEHNTSSN HHQQRSATQS RRHTKAAPKK FTLSRSCAGG
     GSGTLSGVHQ QVKPSPSNPA ISPECRKTLP VRTNYAAVDD DDDIECEDVD EVNFGQQEKE
     RERETRQPTK DCGTDETDHV QQRHKNTMTT SATAASRHHH QDGGGGDQSD LSSVISSPSV
     STVSSPLSTP TRLPQALQQQ LHCCQKSTGM ESRARTSPQQ IQHPHRQHHQ QQHHHHHHHH
     HLTAAGCTGG GGGGGGSGGS GSCKAKKLDP RLNPSPYRQL LPIALCLLSF AAVFATLIVY
     MDTTEIRHQQ FRLNMSRDYE LNGVAQDDPA LIDFLRQIHM GKYLGKASPK VAAAASVGVG
     PPPNSPRLAA AGSTFGSGNS SGSGADQLAH YVADLVGGKM NGAVIQSLSG PLAHLITAPW
     LSEQLNWMGV LVEPEPRWYF TLRKQNAQRA RMQVVHACVS PNTYPKEITI HNEDVRINSL
     HDEETSWFNS RVKCFPLYTI MLACERTEYD LLSLGVQGHE LEILQTLPFD KVKIDVISIH
     LLEDHEDVAD YVLDITRFLA GKSYKLQRKI GRNYFYQRLN ASASRTRKKD ILLLKTP
 
 
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