ID Q9W3H8_DROME Unreviewed; 1269 AA.
AC Q9W3H8;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 4.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=MAGUK p55 subfamily member 5 {ECO:0000256|ARBA:ARBA00032294};
GN Name=sdt {ECO:0000313|EMBL:AAF46349.4,
GN ECO:0000313|FlyBase:FBgn0261873};
GN Synonyms=anon-EST:fe2E6 {ECO:0000313|EMBL:AAF46349.4}, BP1063
GN {ECO:0000313|EMBL:AAF46349.4}, CG12657 {ECO:0000313|EMBL:AAF46349.4},
GN CG12658 {ECO:0000313|EMBL:AAF46349.4}, CG15339
GN {ECO:0000313|EMBL:AAF46349.4}, CG15340 {ECO:0000313|EMBL:AAF46349.4},
GN CG15341 {ECO:0000313|EMBL:AAF46349.4}, CG15342
GN {ECO:0000313|EMBL:AAF46349.4}, CG1617 {ECO:0000313|EMBL:AAF46349.4},
GN cGUK1 {ECO:0000313|EMBL:AAF46349.4}, cMAGUK1
GN {ECO:0000313|EMBL:AAF46349.4}, Dmel\CG32717
GN {ECO:0000313|EMBL:AAF46349.4}, l(1)7Ef {ECO:0000313|EMBL:AAF46349.4},
GN pal1 {ECO:0000313|EMBL:AAF46349.4}, PALS1
GN {ECO:0000313|EMBL:AAF46349.4}, Pals1 {ECO:0000313|EMBL:AAF46349.4},
GN SDT {ECO:0000313|EMBL:AAF46349.4}, Sdt {ECO:0000313|EMBL:AAF46349.4},
GN Std {ECO:0000313|EMBL:AAF46349.4}, std {ECO:0000313|EMBL:AAF46349.4};
GN ORFNames=CG32717 {ECO:0000313|EMBL:AAF46349.4,
GN ECO:0000313|FlyBase:FBgn0261873}, Dmel_CG32717
GN {ECO:0000313|EMBL:AAF46349.4};
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:AAF46349.4, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AAF46349.4, 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:AAF46349.4, 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:AAF46349.4, 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:AAF46349.4, 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:AAF46349.4, 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:AAF46349.4, 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:AAF46349.4, 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:AAF46349.4, 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 -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004184}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR EMBL; AE014298; AAF46349.4; -; Genomic_DNA.
DR RefSeq; NP_572464.4; NM_132236.6.
DR AlphaFoldDB; Q9W3H8; -.
DR SMR; Q9W3H8; -.
DR IntAct; Q9W3H8; 7.
DR DNASU; 44861; -.
DR EnsemblMetazoa; FBtr0308217; FBpp0300537; FBgn0261873.
DR GeneID; 44861; -.
DR UCSC; CG32717-RA; d. melanogaster.
DR AGR; FB:FBgn0261873; -.
DR CTD; 44861; -.
DR FlyBase; FBgn0261873; sdt.
DR VEuPathDB; VectorBase:FBgn0261873; -.
DR GeneTree; ENSGT00940000156087; -.
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 cell types or tissues.
DR ExpressionAtlas; Q9W3H8; 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:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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 projection {ECO:0000256|ARBA:ARBA00023273};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9W3H8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:AAF46349.4}.
FT DOMAIN 664..720
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 813..892
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 918..989
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1068..1248
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 101..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 136937 MW; 51ABB9F30FC9DA31 CRC64;
MRILKQWNRR RSGSSIVVLD GDDLKPCLPD DYISGQHHLN HQQQLQLQQQ LQQQHPLQQQ
HYRTHSGDIR EIDQEMLTML SVNQDNGPHR EMAVDCPDTF IARNKTPPRY PPPRPPQKQH
QATTAMAATQ VAQQQTPSHK LQATLSSDPN GNSNSNNNSH IVGISSSSSS NNSSITDDFL
CVVDGLYQGR KDTASPSSSA FDEVMSKHTL DSFGSIAYRH LHQQHQATSN GNSSSNTSNT
NSNTNSNTNS NSNTNGNTSN NTAVSTKTAT VTKTGVSSSN SNSNSLNSSN SSMHTSSSSS
GHSSNIASAT SSSSATSSST VPDDLSLAPP GYEVSQQQQQ QHLVATPVTM LLPPMAKHRE
LPVDVPDSFI EMVKTTPRYP PPAHLSSRGS LLSNGSASTA HTTLSSMGVA PSPVTATAAA
AASASAACAT TAVAAAAVSG VADGDARRVA DELNGNAKPV PPPRDHLRVE KDGRLVNCSP
APQLPDRRAP GNASSGSSGA TTHPLQHQQI AQIVEPTLEQ LDSIKKYQEQ LRRRREEEER
IAQQNEFLRN SLRGSRKLKA LQDTATPGKA VAQQQQQATL ATQVVGVENE AYLPDEDQPQ
AEQIDGYGEL IAALTRLQNQ LSKSGLSTLA GRVSAAHSVL ASASVAHVLA ARTAVLQRRR
SRVSGPLHHS SLGLQKDIVE LLTQSNTAAA IELGNLLTSH EMEGLLLAHD RIANHTDGTP
SPTPTPTPAI GAATGSTLSS PVAGPKRNLG MVVPPPVVPP PLAQRGAMPL PRGESPPPVP
MPPLATMPMS MPVNLPMSAC FGTLNDQNDN IRIIQIEKST EPLGATVRNE GEAVVIGRIV
RGGAAEKSGL LHEGDEILEV NGQELRGKTV NEVCALLGAM QGTLTFLIVP AGSPPSVGVM
GGTTGSQLAG LGGAHRDTAV LHVRAHFDYD PEDDLYIPCR ELGISFQKGD VLHVISREDP
NWWQAYREGE EDQTLAGLIP SQSFQHQRET MKLAIAEEAG LARSRGKDGS GSKGATLLCA
RKGRKKKKKA SSEAGYPLYA TTAPDETDPE EILTYEEVAL YYPRATHKRP IVLIGPPNIG
RHELRQRLMA DSERFSAAVP HTSRARREGE VPGVDYHFIT RQAFEADILA RRFVEHGEYE
KAYYGTSLEA IRTVVASGKI CVLNLHPQSL KLLRASDLKP YVVLVAPPSL DKLRQKKLRN
GEPFKEEELK DIIATARDME ARWGHLFDMI IINNDTERAY HQLLAEINSL EREPQWVPAQ
WVHNNRDES
//
