ID Q9VZI9_DROME Unreviewed; 903 AA. AC Q9VZI9; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 16-OCT-2019, entry version 182. DE RecName: Full=Receptor protein serine/threonine kinase {ECO:0000256|SAAS:SAAS00138132}; DE EC=2.7.11.30 {ECO:0000256|SAAS:SAAS00138132}; GN Name=wit {ECO:0000313|EMBL:AAF47832.1, GN ECO:0000313|FlyBase:FBgn0024179}; GN Synonyms=1262 {ECO:0000313|EMBL:AAF47832.1}, 15 GN {ECO:0000313|EMBL:AAF47832.1}, ALK3 {ECO:0000313|EMBL:AAF47832.1}, BMP GN {ECO:0000313|EMBL:AAF47832.1}, BMPRII {ECO:0000313|EMBL:AAF47832.1}, GN Dmel\CG10776 {ECO:0000313|EMBL:AAF47832.1}, l(3)64Aa GN {ECO:0000313|EMBL:AAF47832.1}, l(3)S126215 GN {ECO:0000313|EMBL:AAF47832.1}, l(3)SH12 {ECO:0000313|EMBL:AAF47832.1}, GN SE20 {ECO:0000313|EMBL:AAF47832.1}, STK-D GN {ECO:0000313|EMBL:AAF47832.1}, Stk-D {ECO:0000313|EMBL:AAF47832.1}, GN WIT {ECO:0000313|EMBL:AAF47832.1}, Wit {ECO:0000313|EMBL:AAF47832.1}, GN Wit-C {ECO:0000313|EMBL:AAF47832.1}; GN ORFNames=CG10776 {ECO:0000313|EMBL:AAF47832.1, GN ECO:0000313|FlyBase:FBgn0024179}, Dmel_CG10776 GN {ECO:0000313|EMBL:AAF47832.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF47832.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF47832.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., RA Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF47832.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAF47832.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAF47832.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002). RN [5] {ECO:0000313|EMBL:AAF47832.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAM50168.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley {ECO:0000313|EMBL:AAM50168.1}; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., RA Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., RA Celniker S.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:AAF47832.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [8] {ECO:0000313|EMBL:AAF47832.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:AAF47832.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., RA Yu C., Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:AAF47832.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [11] {ECO:0000313|EMBL:AAF47832.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [12] {ECO:0000313|EMBL:AAF47832.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109357; DOI=.1534/g3.115.018929; RG FlyBase Consortium; RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., RA St Pierre S.E., Gramates L.S., Zhou P., Schroeder A.J., Falls K., RA Strelets V., Russo S.M., Gelbart W.M.; RT "Gene Model Annotations for Drosophila melanogaster: Impact of High- RT Throughput Data."; RL G3 (Bethesda) 5:1721-1736(2015). RN [13] {ECO:0000313|EMBL:AAF47832.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109356; DOI=.1534/g3.115.018937; RG FlyBase Consortium; RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., RA St Pierre S.E., Zhou P., Schroeder A.J., Falls K., Emmert D.B., RA Russo S.M., Gelbart W.M.; RT "Gene Model Annotations for Drosophila melanogaster: The Rule- RT Benders."; RL G3 (Bethesda) 5:1737-1749(2015). RN [14] {ECO:0000313|EMBL:AAF47832.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O- CC phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA- CC COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, CC ChEBI:CHEBI:456216; EC=2.7.11.30; CC Evidence={ECO:0000256|SAAS:SAAS01128400}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[receptor-protein]-L-threonine + ATP = [receptor- CC protein]-O-phospho-L-threonine + ADP + H(+); CC Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA- CC COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.30; Evidence={ECO:0000256|SAAS:SAAS01128404}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. TGFB receptor subfamily. CC {ECO:0000256|SAAS:SAAS00595019}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014296; AAF47832.1; -; Genomic_DNA. DR EMBL; AY119514; AAM50168.1; -; mRNA. DR RefSeq; NP_524692.3; NM_079953.4. DR SMR; Q9VZI9; -. DR IntAct; Q9VZI9; 2. DR PRIDE; Q9VZI9; -. DR EnsemblMetazoa; FBtr0073279; FBpp0073135; FBgn0024179. DR GeneID; 44096; -. DR UCSC; CG10776-RA; d. melanogaster. DR CTD; 44096; -. DR FlyBase; FBgn0024179; wit. DR eggNOG; KOG3653; Eukaryota. DR eggNOG; ENOG410XS2Z; LUCA. DR OMA; CFTLWNQ; -. DR OrthoDB; 390511at2759; -. DR ChiTaRS; wit; fly. DR GenomeRNAi; 44096; -. DR Proteomes; UP000000803; Chromosome 3L. DR Bgee; FBgn0024179; Expressed in 9 organ(s), highest expression level in head. DR ExpressionAtlas; Q9VZI9; baseline and differential. DR GO; GO:0005769; C:early endosome; IDA:FlyBase. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0055037; C:recycling endosome; IDA:FlyBase. DR GO; GO:0045202; C:synapse; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IBA:GO_Central. DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central. DR GO; GO:0048813; P:dendrite morphogenesis; NAS:FlyBase. DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase. DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase. DR GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IMP:FlyBase. DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central. DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase. DR InterPro; IPR000472; Activin_recp. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR000333; TGFB_receptor. DR PANTHER; PTHR23255; PTHR23255; 1. DR Pfam; PF01064; Activin_recp; 1. DR Pfam; PF00069; Pkinase; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|SAAS:SAAS00138218}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Kinase {ECO:0000256|SAAS:SAAS00138139}; KW Membrane {ECO:0000256|SAAS:SAAS00138203, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00138212}; KW Receptor {ECO:0000256|SAAS:SAAS00138179}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00138186}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|SAAS:SAAS00138167}; KW Transmembrane {ECO:0000256|SAAS:SAAS00138220, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00488859, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 903 Receptor protein serine/threonine kinase. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015100862. FT TRANSMEM 167 190 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 224 531 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT REGION 36 66 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 748 771 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 793 837 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 855 878 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 793 810 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 822 837 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 855 869 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. SQ SEQUENCE 903 AA; 100269 MW; ADA949206BA6CC3F CRC64; MNWAIYLLLA LISLGRATPV PNRQYSCMSY QEDDNSFHDD DGDQDSSGEL QEQQVESTPI PSEPHRRTCP DGYTFCFTIW NQTANGARVV KQGCWKDNTD RTSICSQSEC TSSAPTSKTS SLYYCCCSGG VCNAQYSVVE PAPLELGSNE GRTSITNRAT EKQHQSFLAS TMLGLAGGLT ALTIGIFLAV QYCRTAKEKP EPEESPLAPS GPGYSSNLRN VDNMNLIGML GSGKYGTVMK GLLHDQEVAV KIYPEEHHQY YVNERNIYAL PLMECPALLS YFGYDERCTM DGRMEYQLVL SLAPLGCLQD WLIANTLTFS ECCGMLRSIT RGISHLHTEL RLGDQHKPCV AHRDINTRNV LVQADLSCCI ADFGFALKVF GSKYEYKGEV AMAETKSINE VGTLRYMAPE LLEGAVNLRD CETSLKQMDV YALGLVLWEV ATRCSDFYAP GQATPPYKAP YEQEVGSHPS FDQMQALVVR HKARPLFPTG WGGGAAAKVV RDTCEDCWDH DADARLTSLC AEERMQEMST LRPRAQAQPS SPLLNTNNLV ASPTAEQGIN IIATTTTAAA VHHQMSSDTT GLIQPPPNQQ IPLAALEREK NHLSYPQQQL QPYQGRNPCQ ERNLAPLTMR TPPVLVERSK KHSFQTQPQE NSLSCLEHDV SVEELIASHQ HQQQKNTIVS TGGNGNSCLG QGFPKQQNTD QKLRGWHGVR ALIHKKLFRK EHAEELCRQL QLGEEKSNLV TALRRPNNLD LNPRLDKPPP DQLRSAEQRM GTPAHIVPRS LSSSLIKHIN GTTNNNSIQS HGSELQTLTR PASKRRPGHL RTNSLMATTG QGPPTEQQMR RQHSLEVFRE VFSGRGSSER LRDPSERVKT PGDVPPSVRK ARASKTLSLY DDRMMDSSLL NIL //