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VEIN_DROME
ID   VEIN_DROME              Reviewed;         623 AA.
AC   Q94918; Q9VRQ3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Protein vein;
DE   AltName: Full=Epidermal growth factor-like protein;
DE   AltName: Full=Protein defective dorsal discs;
DE   Flags: Precursor;
GN   Name=vn; Synonyms=ddd; ORFNames=CG10491;
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Embryo, and Imaginal disk;
RX   PubMed=8824589; DOI=10.1101/gad.10.18.2302;
RA   Schnepp B.C., Grumbling G.B., Donaldson T.D., Simcox A.A.;
RT   "Vein is a novel component in the Drosophila epidermal growth factor
RT   receptor pathway with similarity to the neuregulins.";
RL   Genes Dev. 10:2302-2313(1996).
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).
CC   -!- FUNCTION: Ligand for the EGF receptor. Seems to play a role in the
CC       global proliferation of wing disc cells and the larval patterning.
CC       Shows a strong synergistic genetic interaction with spi, suggesting a
CC       molecular interdependence. Required for the development of interveins
CC       cells.
CC   -!- INTERACTION:
CC       Q94918; A8JUV7: boi; NbExp=3; IntAct=EBI-869384, EBI-6895641;
CC       Q94918; Q9VM64: ihog; NbExp=2; IntAct=EBI-869384, EBI-94134;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q94918-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q94918-2; Sequence=VSP_001419;
CC   -!- DEVELOPMENTAL STAGE: Expressed in blastoderm embryos in two
CC       ventrolateral stripes that are brought to the midline as gastrulation
CC       proceeds. In the germ-band retraction stage, expression is seen in the
CC       CNS and epidermis. At late blastoderm, expression is localized in the
CC       anlagen of the amnioserosa. Expression in the head, cypeolabrum,
CC       maxillary and labial lobes, and around the stomodeum throughout embryo
CC       development. In late embryos, expression decays in all ectodermal cells
CC       and appears in the segmental muscles and the gut wall. In the larva,
CC       expression occurs in the dorsal metathoracic disc, the eye-antennal
CC       disc and the ventral thoracic disc. Found in the intervein in the pupa.
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DR   EMBL; U67935; AAC47293.1; -; mRNA.
DR   EMBL; AE014296; AAF50739.2; -; Genomic_DNA.
DR   RefSeq; NP_523942.2; NM_079218.3. [Q94918-1]
DR   AlphaFoldDB; Q94918; -.
DR   SMR; Q94918; -.
DR   BioGRID; 64117; 34.
DR   IntAct; Q94918; 3.
DR   STRING; 7227.FBpp0076790; -.
DR   GlyGen; Q94918; 9 sites.
DR   PaxDb; Q94918; -.
DR   EnsemblMetazoa; FBtr0077082; FBpp0076790; FBgn0003984. [Q94918-1]
DR   GeneID; 38657; -.
DR   KEGG; dme:Dmel_CG10491; -.
DR   CTD; 38657; -.
DR   FlyBase; FBgn0003984; vn.
DR   VEuPathDB; VectorBase:FBgn0003984; -.
DR   eggNOG; ENOG502QRNM; Eukaryota.
DR   HOGENOM; CLU_034587_0_0_1; -.
DR   InParanoid; Q94918; -.
DR   PhylomeDB; Q94918; -.
DR   SignaLink; Q94918; -.
DR   BioGRID-ORCS; 38657; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; vn; fly.
DR   GenomeRNAi; 38657; -.
DR   PRO; PR:Q94918; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0003984; Expressed in extraembryonic structure and 52 other tissues.
DR   ExpressionAtlas; Q94918; baseline and differential.
DR   Genevisible; Q94918; DM.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:FlyBase.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IDA:FlyBase.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IMP:FlyBase.
DR   GO; GO:0030031; P:cell projection assembly; IMP:FlyBase.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:FlyBase.
DR   GO; GO:0007482; P:haltere development; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0007479; P:leg disc proximal/distal pattern formation; IEP:FlyBase.
DR   GO; GO:0007494; P:midgut development; IMP:FlyBase.
DR   GO; GO:0035310; P:notum cell fate specification; IMP:FlyBase.
DR   GO; GO:0007477; P:notum development; IMP:FlyBase.
DR   GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR   GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:FlyBase.
DR   GO; GO:2000736; P:regulation of stem cell differentiation; IMP:FlyBase.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR040180; Neuregulin.
DR   PANTHER; PTHR11100; PTHR11100; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Growth factor; Immunoglobulin domain;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..623
FT                   /note="Protein vein"
FT                   /id="PRO_0000007774"
FT   DOMAIN          457..542
FT                   /note="Ig-like C2-type"
FT   DOMAIN          561..599
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          70..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..316
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        478..531
FT                   /evidence="ECO:0000250"
FT   DISULFID        566..577
FT                   /evidence="ECO:0000250"
FT   DISULFID        571..588
FT                   /evidence="ECO:0000250"
FT   DISULFID        590..599
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         609..623
FT                   /note="FVAIYGQIHTLNNDY -> SSPESCKNYQGGYY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8824589"
FT                   /id="VSP_001419"
FT   CONFLICT        149
FT                   /note="Missing (in Ref. 1; AAC47293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="S -> T (in Ref. 1; AAC47293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494
FT                   /note="E -> D (in Ref. 1; AAC47293)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   623 AA;  71698 MW;  AFD2724D5C1F56C8 CRC64;
     MYAQHLRKWS LKTKKQLMPL ILLIISYMLL LNTCVLSSSA TTQQQQQQQQ QQQHLPRLWE
     GSAEESSYYI PLSSDNGSGS SESSAESGSS SSRSSSNNID NNILSRLLSL NSNSLSSRSN
     VKLKPATVFD AGSSTPAQQE QHVAAVPEQQ QQQQQQQQSM QKVPNTLINS QIYNLLYNGM
     PSEAASSKMR RHIQPSQLPH QPESRAQLPS NYSSRPAVRS YLIESYEMPE SMLEDRSPEQ
     AARSRRDGSN TNGSRQQQRT GHRQQLQQDK RDHRRQRQDQ QKEQRQQQQQ RQHKSGNKHQ
     QQQQQRRKHQ RKHQRYNRYC SARDPAQLAF AAPTVFQGVF KSMSADRRVN FSATMKVEKV
     YKQQHDLQLP TLVRLQFALS NSSGECDIYR ERLMPRGMLR SGNDLQQASD ISYMMFVQQT
     NPGNFTILGQ PMRVTHLVVE AVETAVSENY TQNAEVTKIF SKPSKAIIKH GKKLRIVCEV
     SGQPPPKVTW FKDEKSINRK RNIYQFKHHK RRSELIVRSF NSSSDAGRYE CRAKNKASKA
     IAKRRIMIKA SPVHFPTDRS ASGIPCNFDY CFHNGTCRMI PDINEVYCRC PTEYFGNRCE
     NKWPDSRYFV AIYGQIHTLN NDY
 
 
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