CRK_DROME
ID CRK_DROME Reviewed; 271 AA.
AC Q9XYM0; Q53XD2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Adapter molecule Crk;
GN Name=Crk; ORFNames=CG1587;
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 TISSUE=Embryo;
RX PubMed=10072777; DOI=10.1016/s0378-1119(99)00010-4;
RA Galletta B.J., Niu X.-P., Erickson M.R., Abmayr S.M.;
RT "Identification of a Drosophila homologue to vertebrate Crk by interaction
RT with MBC.";
RL Gene 228:243-252(1999).
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;
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adapter protein which interacts with C-terminal portion of
CC mbc, homolog of human DOCK180. May play a role in cellular processes
CC throughout development. {ECO:0000269|PubMed:10072777}.
CC -!- INTERACTION:
CC Q9XYM0; Q9VCH4: mbc; NbExp=3; IntAct=EBI-99477, EBI-177001;
CC -!- TISSUE SPECIFICITY: Embryonic zygotic expression is seen in
CC invaginating presumptive mesoderm and ectodermally derived tissues
CC during gastrulation. At stage 8, expression is also seen in anterior
CC and posterior midgut and cephalic furrow. By stage 9, expression is
CC highest in visceral mesoderm of anterior and posterior midgut, ventral
CC nerve cord and somatic mesoderm. {ECO:0000269|PubMed:10072777}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout embryogenesis, declines during larval stages and reappears
CC during pupation. {ECO:0000269|PubMed:10072777}.
CC -!- SIMILARITY: Belongs to the CRK family. {ECO:0000305}.
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DR EMBL; AF112976; AAD28428.1; -; mRNA.
DR EMBL; AE014135; AAF59362.1; -; Genomic_DNA.
DR EMBL; AE014135; AAN06519.1; -; Genomic_DNA.
DR EMBL; BT012456; AAS93727.1; -; mRNA.
DR RefSeq; NP_651908.1; NM_143651.6.
DR RefSeq; NP_726549.1; NM_166743.3.
DR AlphaFoldDB; Q9XYM0; -.
DR SMR; Q9XYM0; -.
DR BioGRID; 68612; 16.
DR DIP; DIP-21287N; -.
DR IntAct; Q9XYM0; 23.
DR MINT; Q9XYM0; -.
DR STRING; 7227.FBpp0088181; -.
DR PaxDb; Q9XYM0; -.
DR DNASU; 43775; -.
DR EnsemblMetazoa; FBtr0089112; FBpp0088181; FBgn0024811.
DR EnsemblMetazoa; FBtr0089113; FBpp0088182; FBgn0024811.
DR GeneID; 43775; -.
DR KEGG; dme:Dmel_CG1587; -.
DR UCSC; CG1587-RA; d. melanogaster.
DR CTD; 1398; -.
DR FlyBase; FBgn0024811; Crk.
DR VEuPathDB; VectorBase:FBgn0024811; -.
DR eggNOG; KOG4792; Eukaryota.
DR GeneTree; ENSGT00820000127055; -.
DR HOGENOM; CLU_060542_0_0_1; -.
DR InParanoid; Q9XYM0; -.
DR OMA; WWNAEDG; -.
DR PhylomeDB; Q9XYM0; -.
DR Reactome; R-DME-186763; Downstream signal transduction.
DR Reactome; R-DME-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DME-9027284; Erythropoietin activates RAS.
DR Reactome; R-DME-912631; Regulation of signaling by CBL.
DR SignaLink; Q9XYM0; -.
DR BioGRID-ORCS; 43775; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43775; -.
DR PRO; PR:Q9XYM0; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0024811; Expressed in cleaving embryo and 28 other tissues.
DR ExpressionAtlas; Q9XYM0; baseline and differential.
DR Genevisible; Q9XYM0; DM.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:FlyBase.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046529; P:imaginal disc fusion, thorax closure; IGI:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; TAS:FlyBase.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:FlyBase.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:FlyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:FlyBase.
DR CDD; cd11759; SH3_CRK_C; 1.
DR CDD; cd11758; SH3_CRK_N; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035458; CRK_SH3_C.
DR InterPro; IPR035457; CRK_SH3_N.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Developmental protein; Reference proteome; Repeat; SH2 domain; SH3 domain.
FT CHAIN 1..271
FT /note="Adapter molecule Crk"
FT /id="PRO_0000079350"
FT DOMAIN 12..104
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 106..166
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 199..260
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ SEQUENCE 271 AA; 31205 MW; D1B4FE43150932DC CRC64;
MDTFDVSDRN SWYFGPMSRQ DATEVLMNER ERGVFLVRDS NSIAGDYVLC VREDTKVSNY
IINKVQQQDQ IVYRIGDQSF DNLPKLLTFY TLHYLDTTPL KRPACRRVEK VIGKFDFVGS
DQDDLPFQRG EVLTIVRKDE DQWWTARNSS GKIGQIPVPY IQQYDDYMDE DAIDKNEPSI
SGSSNVFEST LKRTDLNRKL PAYARVKQSR VPNAYDKTAL KLEIGDIIKV TKTNINGQWE
GELNGKNGHF PFTHVEFVDD CDLSKNSTEI C
