WSCK_DROME
ID WSCK_DROME Reviewed; 791 AA.
AC P83097; Q8I0H1; Q95TS7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Putative inactive tyrosine-protein kinase Wsck {ECO:0000305};
DE Flags: Precursor;
GN Name=Wsck {ECO:0000312|FlyBase:FBgn0046685};
GN ORFNames=CG31127 {ECO:0000312|FlyBase:FBgn0046685};
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 [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 [2]
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 [3]
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).
RN [4]
RP IDENTIFICATION.
RA Manning G., Sudarsanam S., Plowman G.;
RT "Prediction of novel protein kinases from the Drosophila genome project and
RT EST sequences.";
RL Unpublished observations (AUG-2001).
CC -!- FUNCTION: Probably lacks tyrosine-protein kinase activity.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Gln-626 is present instead of the conserved Asp which is
CC expected to act as an active site proton acceptor therefore suggesting
CC that it has no protein kinase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13797.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAN14006.1; -; Genomic_DNA.
DR EMBL; AY058568; AAL13797.1; ALT_INIT; mRNA.
DR EMBL; BT001869; AAN71639.1; -; mRNA.
DR RefSeq; NP_733018.1; NM_170155.2.
DR AlphaFoldDB; P83097; -.
DR SMR; P83097; -.
DR STRING; 7227.FBpp0084049; -.
DR GlyGen; P83097; 3 sites.
DR PaxDb; P83097; -.
DR PRIDE; P83097; -.
DR DNASU; 318600; -.
DR EnsemblMetazoa; FBtr0084669; FBpp0084049; FBgn0046685.
DR GeneID; 318600; -.
DR KEGG; dme:Dmel_CG31127; -.
DR UCSC; CG31127-RA; d. melanogaster.
DR CTD; 318600; -.
DR FlyBase; FBgn0046685; Wsck.
DR VEuPathDB; VectorBase:FBgn0046685; -.
DR eggNOG; KOG0200; Eukaryota.
DR eggNOG; KOG4228; Eukaryota.
DR HOGENOM; CLU_021662_0_0_1; -.
DR InParanoid; P83097; -.
DR OMA; VTCVIFG; -.
DR OrthoDB; 704701at2759; -.
DR PhylomeDB; P83097; -.
DR BioGRID-ORCS; 318600; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 318600; -.
DR PRO; PR:P83097; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0046685; Expressed in embryonic/larval hemocyte (Drosophila) and 21 other tissues.
DR ExpressionAtlas; P83097; baseline and differential.
DR Genevisible; P83097; DM.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR002889; WSC_carb-bd.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01822; WSC; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00321; WSC; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS51212; WSC; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..791
FT /note="Putative inactive tyrosine-protein kinase Wsck"
FT /id="PRO_0000045275"
FT TOPO_DOM 27..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..791
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..125
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT DOMAIN 131..246
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 493..758
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 499..507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 791 AA; 88520 MW; 7287608CB2B6A1BC CRC64;
MECGSHSGHR PIPIWLSSCL VAMCLGLPLG AAVPQEAPAY YYVGCYTART DLLHESVYAK
TPQTCIEICE HQGHHYAVLA SEKCFCANVL EPQEQQDEQL CNTRCLANKA QYCGGVGVHS
YYSTILTKQP GPHHLRISNK TENSLTLSWN AYEARKLLLA GGAEAVLPNQ LLDNFLIKAQ
VLKTYSSLPA FPQPEFMVQS TETQFELTDL HPATLYNISV RAMCKDAQVG QSECGQASIE
ATTEVGLPSP VPAQPKILSR TDRTVTIELS PIRNDNGPLS KLLVIVEYVD NALSQPFDAQ
LLGSWQQAQQ DGVPYYIAAE LDYDRPEDNR TRRFVVGDGK RYGRFTNKPL DQPDAHVHIS
LGLVSTLEGV TKTMYSRGTH DQHVTSLDDF SYATFEKGQS SVVALAVTCV IFGSCLLLSL
IAYFYLRYKT CRGRRLTGGN THEMTLQTPI IERENNGYLV EDDPLPHSPE NFKQQLQQLV
EGYERIPRNA LRLNVNDVIG DGRFGEIITG KVSTNDFARD CTLHVLCLDD LNGTTQAQLL
RELRQLSQLK RQEHLLDFYG VSASPDWFYL IFEQQRMSLK RKLVESRLMA PSPRLTSLSE
QLVLQWIYEL ASAMNYLSSC QVVHRQLCSH SVFVTSDFKL KLSVFGPLPY MNIARQQPDH
NRWLAPEVLR HQHHHSTRSD VWSLACVAWE CCALGGTPYA NAVASNQQLL EAIRAAVRPA
QPAYVYGDLY QLLLNCWQLE PSERSSCEDV AFGVRQLMTS PRHALSFDRV AGGLDTLPPY
LPQLEAVATM G
