ID Q7KVT3_DROME Unreviewed; 1367 AA. AC Q7KVT3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 08-NOV-2023, entry version 169. DE SubName: Full=Stardust, isoform E {ECO:0000313|EMBL:AAS65284.1}; DE EC=2.7.4.8 {ECO:0000313|EMBL:AAS65284.1}; GN Name=sdt {ECO:0000313|EMBL:AAS65284.1, GN ECO:0000313|FlyBase:FBgn0261873}; GN Synonyms=anon-EST:fe2E6 {ECO:0000313|EMBL:AAS65284.1}, BP1063 GN {ECO:0000313|EMBL:AAS65284.1}, CG12657 {ECO:0000313|EMBL:AAS65284.1}, GN CG12658 {ECO:0000313|EMBL:AAS65284.1}, CG15339 GN {ECO:0000313|EMBL:AAS65284.1}, CG15340 {ECO:0000313|EMBL:AAS65284.1}, GN CG15341 {ECO:0000313|EMBL:AAS65284.1}, CG15342 GN {ECO:0000313|EMBL:AAS65284.1}, CG1617 {ECO:0000313|EMBL:AAS65284.1}, GN cGUK1 {ECO:0000313|EMBL:AAS65284.1}, cMAGUK1 GN {ECO:0000313|EMBL:AAS65284.1}, Dmel\CG32717 GN {ECO:0000313|EMBL:AAS65284.1}, l(1)7Ef {ECO:0000313|EMBL:AAS65284.1}, GN pal1 {ECO:0000313|EMBL:AAS65284.1}, PALS1 GN {ECO:0000313|EMBL:AAS65284.1}, Pals1 {ECO:0000313|EMBL:AAS65284.1}, GN SDT {ECO:0000313|EMBL:AAS65284.1}, Sdt {ECO:0000313|EMBL:AAS65284.1}, GN Std {ECO:0000313|EMBL:AAS65284.1}, std {ECO:0000313|EMBL:AAS65284.1}; GN ORFNames=CG32717 {ECO:0000313|EMBL:AAS65284.1, GN ECO:0000313|FlyBase:FBgn0261873}, Dmel_CG32717 GN {ECO:0000313|EMBL:AAS65284.1}; 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 {ECO:0000313|EMBL:AAS65284.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAS65284.1, 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., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., 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., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., 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:AAS65284.1, 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 melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAS65284.1, 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., 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] {ECO:0000313|EMBL:AAS65284.1, 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., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AAS65284.1, 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 assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAS65284.1, 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 [7] {ECO:0000313|EMBL:AAS65284.1, 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 heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:AAS65284.1, 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). CC -!- SIMILARITY: Belongs to the MAGUK family. CC {ECO:0000256|ARBA:ARBA00007014}. 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; AE014298; AAS65284.1; -; Genomic_DNA. DR RefSeq; NP_996376.1; NM_206653.3. DR SMR; Q7KVT3; -. DR DNASU; 44861; -. DR EnsemblMetazoa; FBtr0089974; FBpp0088912; FBgn0261873. DR GeneID; 44861; -. DR UCSC; CG32717-RE; d. melanogaster. DR AGR; FB:FBgn0261873; -. DR CTD; 44861; -. DR FlyBase; FBgn0261873; sdt. DR VEuPathDB; VectorBase:FBgn0261873; -. DR OrthoDB; 2873706at2759; -. DR BioGRID-ORCS; 44861; 0 hits in 1 CRISPR screen. DR ChiTaRS; sdt; fly. DR GenomeRNAi; 44861; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0261873; Expressed in spermathecum and 33 other tissues. DR ExpressionAtlas; Q7KVT3; baseline and differential. DR GO; GO:0005912; C:adherens junction; IBA:GO_Central. DR GO; GO:0045179; C:apical cortex; IDA:FlyBase. DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase. DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005918; C:septate junction; TAS:FlyBase. DR GO; GO:0035003; C:subapical complex; IPI:FlyBase. DR GO; GO:0004385; F:guanylate kinase activity; ISS:FlyBase. DR GO; GO:0045176; P:apical protein localization; IMP:FlyBase. DR GO; GO:0007043; P:cell-cell junction assembly; NAS:FlyBase. DR GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:FlyBase. DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:FlyBase. DR GO; GO:0048699; P:generation of neurons; IBA:GO_Central. DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; TAS:FlyBase. DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IBA:GO_Central. DR GO; GO:0002009; P:morphogenesis of an epithelium; NAS:FlyBase. DR GO; GO:0042461; P:photoreceptor cell development; IMP:FlyBase. DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central. DR GO; GO:0045186; P:zonula adherens assembly; IMP:FlyBase. DR CDD; cd00071; GMPK; 1. DR CDD; cd00992; PDZ_signaling; 1. DR CDD; cd12036; SH3_MPP5; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR014775; L27_C. DR InterPro; IPR004172; L27_dom. DR InterPro; IPR035601; MPP5_SH3. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1. DR PANTHER; PTHR23122:SF14; PROTEIN PALS1; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF02828; L27; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF07653; SH3_2; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS51022; L27; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW Cell junction {ECO:0000256|ARBA:ARBA00022949}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q7KVT3}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}; KW Transferase {ECO:0000313|EMBL:AAS65284.1}. FT DOMAIN 762..818 FT /note="L27" FT /evidence="ECO:0000259|PROSITE:PS51022" FT DOMAIN 911..990 FT /note="PDZ" FT /evidence="ECO:0000259|PROSITE:PS50106" FT DOMAIN 1016..1087 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT DOMAIN 1166..1346 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000259|PROSITE:PS50052" FT REGION 102..126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 203..270 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 321..439 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 478..505 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 550..603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 812..832 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 214..270 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 321..422 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 485..505 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 588..603 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1367 AA; 148311 MW; 1D7E0610B05DF6EE CRC64; MRILKQWNRR RSGSSIVVLD GDDLKPCLPD DYISGQHHLN HQQQLQLQQQ LQQQHPLQQQ HYRTHSGDIR EIDQEMLTML SVNQDNGPHR EMAVDCPDTF IARNKTPPRY PPPRPPQKHK KSTNTTTTTT ITALTNNDHA NKMLIVAYHS SHQHEQLQQQ HPSKTSTTTT TIALDVATQN LYNQKQQNKL EQIENYENCL QSERNEQHEQ QFEQQKQHQA TTAMAATQVA QQQTPSHKLQ ATLSSDPNGN SNSNNNSHIV GISSSSSSNN SSITDDFLCV VDGLYQGRKD TASPSSSAFD EVMSKHTLDS FGSIAYRHLH QQHQATSNGN SSSNTSNTNS NTNSNTNSNS NTNGNTSNNT AVSTKTATVT KTGVSSSNSN SNSLNSSNSS MHTSSSSSGH SSNIASATSS SSATSSSTVP DDLSLAPPGY EVSQQQQQQH LVATPVTMLL PPMAKHRELP VDVPDSFIEM VKTTPRYPPP AHLSSRGSLL SNGSASTAHT TLSSMGVAPS PVTATAAAAA SASAACATTA VAAAAVSGVA DGDARRVADE LNGNAKPVPP PRDHLRVEKD GRLVNCSPAP QLPDRRAPGN ASSGSSGATT HPLQHQQIAQ IVEPTLEQLD SIKKYQEQLR RRREEEERIA QQNEFLRNSL RGSRKLKALQ DTATPGKAVA QQQQQATLAT QVVGVENEAY LPDEDQPQAE QIDGYGELIA ALTRLQNQLS KSGLSTLAGR VSAAHSVLAS ASVAHVLAAR TAVLQRRRSR VSGPLHHSSL GLQKDIVELL TQSNTAAAIE LGNLLTSHEM EGLLLAHDRI ANHTDGTPSP TPTPTPAIGA ATGSTLSSPV AGPKRNLGMV VPPPVVPPPL AQRGAMPLPR GESPPPVPMP PLATMPMSMP VNLPMSACFG TLNDQNDNIR IIQIEKSTEP LGATVRNEGE AVVIGRIVRG GAAEKSGLLH EGDEILEVNG QELRGKTVNE VCALLGAMQG TLTFLIVPAG SPPSVGVMGG TTGSQLAGLG GAHRDTAVLH VRAHFDYDPE DDLYIPCREL GISFQKGDVL HVISREDPNW WQAYREGEED QTLAGLIPSQ SFQHQRETMK LAIAEEAGLA RSRGKDGSGS KGATLLCARK GRKKKKKASS EAGYPLYATT APDETDPEEI LTYEEVALYY PRATHKRPIV LIGPPNIGRH ELRQRLMADS ERFSAAVPHT SRARREGEVP GVDYHFITRQ AFEADILARR FVEHGEYEKA YYGTSLEAIR TVVASGKICV LNLHPQSLKL LRASDLKPYV VLVAPPSLDK LRQKKLRNGE PFKEEELKDI IATARDMEAR WGHLFDMIII NNDTERAYHQ LLAEINSLER EPQWVPAQWV HNNRDES //