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SCW_DROME
ID   SCW_DROME               Reviewed;         400 AA.
AC   P54631; Q8INV8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Protein screw;
DE   Flags: Precursor;
GN   Name=scw; ORFNames=CG31695;
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.
RC   STRAIN=Canton-S;
RX   PubMed=7958918; DOI=10.1101/gad.8.21.2588;
RA   Arora K., Levine M.S., O'Connor M.B.;
RT   "The screw gene encodes a ubiquitously expressed member of the TGF-beta
RT   family required for specification of dorsal cell fates in the Drosophila
RT   embryo.";
RL   Genes Dev. 8:2588-2601(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=Embryo;
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).
CC   -!- FUNCTION: Part of the signal that specifies dorsal cell fates in the
CC       embryo. Acts together with dpp. {ECO:0000269|PubMed:7958918}.
CC   -!- SUBUNIT: Heterodimers of scw/dpp are the active subunit, dpp/dpp
CC       homodimers elicit a basal response and scw/scw homodimers alone are
CC       ineffective in specifying a dorsal pattern.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed during early stages of
CC       embryogenesis, but the effect on development appears graded and is
CC       restricted to the dorsal side of the embryo.
CC       {ECO:0000269|PubMed:7958918}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Highest
CC       embryonic expression is found during syncytial blastoderm (nuclear
CC       cycles 11-12). Expression declines rapidly at cellular blastoderm stage
CC       5 and is not detected during the rest of embryonic development.
CC       {ECO:0000269|PubMed:7958918}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; U17573; AAA56872.1; -; mRNA.
DR   EMBL; AE014134; AAN11056.2; -; Genomic_DNA.
DR   EMBL; AY051793; AAK93217.1; -; mRNA.
DR   RefSeq; NP_001286088.1; NM_001299159.1.
DR   RefSeq; NP_524863.3; NM_080124.5.
DR   AlphaFoldDB; P54631; -.
DR   BioGRID; 70052; 7.
DR   DIP; DIP-59820N; -.
DR   IntAct; P54631; 2.
DR   STRING; 7227.FBpp0080802; -.
DR   GlyGen; P54631; 5 sites.
DR   PaxDb; P54631; -.
DR   DNASU; 46000; -.
DR   EnsemblMetazoa; FBtr0081261; FBpp0080802; FBgn0005590.
DR   EnsemblMetazoa; FBtr0343860; FBpp0310402; FBgn0005590.
DR   GeneID; 46000; -.
DR   KEGG; dme:Dmel_CG31695; -.
DR   UCSC; CG31695-RA; d. melanogaster.
DR   CTD; 46000; -.
DR   FlyBase; FBgn0005590; scw.
DR   VEuPathDB; VectorBase:FBgn0005590; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   HOGENOM; CLU_020515_4_1_1; -.
DR   InParanoid; P54631; -.
DR   OMA; FEAYFCG; -.
DR   OrthoDB; 1063560at2759; -.
DR   PhylomeDB; P54631; -.
DR   SignaLink; P54631; -.
DR   BioGRID-ORCS; 46000; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 46000; -.
DR   PRO; PR:P54631; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0005590; Expressed in ectoderm anlage and 15 other tissues.
DR   ExpressionAtlas; P54631; baseline and differential.
DR   Genevisible; P54631; DM.
DR   GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR   GO; GO:0007378; P:amnioserosa formation; IMP:FlyBase.
DR   GO; GO:0030509; P:BMP signaling pathway; IDA:FlyBase.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007502; P:digestive tract mesoderm development; IMP:FlyBase.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR   GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR001111; TGF-b_propeptide.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   Pfam; PF00688; TGFb_propeptide; 1.
DR   SMART; SM00204; TGFB; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS00250; TGF_BETA_1; 1.
DR   PROSITE; PS51362; TGF_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Developmental protein; Differentiation;
KW   Disulfide bond; Glycoprotein; Growth factor; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..277
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033672"
FT   CHAIN           278..400
FT                   /note="Protein screw"
FT                   /id="PRO_0000033673"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        300..365
FT                   /evidence="ECO:0000250"
FT   DISULFID        329..397
FT                   /evidence="ECO:0000250"
FT   DISULFID        333..399
FT                   /evidence="ECO:0000250"
FT   DISULFID        364
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        6
FT                   /note="F -> L (in Ref. 1; AAA56872)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  45891 MW;  2B42B7D28B9B8336 CRC64;
     MLNVFFLTSL FYAASATTYV TTNNHIEMPI YQKRPLSEQM EMIDILDLGD RPRRQAEPNL
     HNSASKFLLE VYNEISEDQE PKEVLHQRHK RSLDDDILIS NEDRQEIASC NSILTFSSRL
     KPEQLDNELD MHITFNTNDV PVDLSLVQAM LRIYKQPSLV DRRANFTVSV YRKLDNRQDF
     SYRILGSVNT TSSQRGWLEF NLTDTLRYWL HNKGLQRRNE LRISIGDSQL STFAAGLVTP
     QASRTSLEPF IVGYFNGPEL LVKIQKLRFK RDLEKRRAGG GSPPPPPPPP VDLYRPPQSC
     ERLNFTVDFK ELHMHNWVIA PKKFEAYFCG GGCNFPLGTK MNATNHAIVQ TLMHLKQPHL
     PKPCCVPTVL GAITILRYLN EDIIDLTKYQ KAVAKECGCH
 
 
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