PATJ_DROME
ID PATJ_DROME Reviewed; 871 AA.
AC Q9NB04; Q9UA56; Q9XZ35;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Patj homolog;
GN Name=Patj; ORFNames=CG12021;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INTERACTION WITH NRX AND CRB.
RX PubMed=10102271; DOI=10.1016/s0092-8674(00)80593-0;
RA Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
RT "Discs Lost, a novel multi-PDZ domain protein, establishes and maintains
RT epithelial polarity.";
RL Cell 96:833-845(1999).
RN [2]
RP ERRATUM OF PUBMED:10102271.
RA Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
RL Cell 115:765-766(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH CRB.
RX PubMed=11076972; DOI=10.1083/jcb.151.4.891;
RA Tanentzapf G., Smith C., McGlade J., Tepass U.;
RT "Apical, lateral, and basal polarization cues contribute to the development
RT of the follicular epithelium during Drosophila oogenesis.";
RL J. Cell Biol. 151:891-904(2000).
RN [4]
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 [5]
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 [6]
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 [7]
RP IDENTIFICATION IN A SAC COMPLEX WITH CRB AND SDT.
RX PubMed=11740560; DOI=10.1038/414638a;
RA Bachmann A., Schneider M., Theilenberg E., Grawe F., Knust E.;
RT "Drosophila Stardust is a partner of Crumbs in the control of epithelial
RT cell polarity.";
RL Nature 414:638-643(2001).
RN [8]
RP INTERACTION WITH PAR-6.
RX PubMed=12900452; DOI=10.1242/dev.00648;
RA Nam S.-C., Choi K.-W.;
RT "Interaction of Par-6 and Crumbs complexes is essential for photoreceptor
RT morphogenesis in Drosophila.";
RL Development 130:4363-4372(2003).
RN [9]
RP FUNCTION.
RX PubMed=14667407; DOI=10.1016/s1534-5807(03)00358-7;
RA Pielage J., Stork T., Bunse I., Klaembt C.;
RT "The Drosophila cell survival gene discs lost encodes a cytoplasmic
RT Codanin-1-like protein, not a homolog of tight junction PDZ protein Patj.";
RL Dev. Cell 5:841-851(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Involved in cell polarity establishment. Probably
CC participates in the assembly, positioning and maintenance of adherens
CC junctions via its interaction with the SAC complex.
CC {ECO:0000269|PubMed:14667407}.
CC -!- SUBUNIT: Component of the SAC complex, a complex composed of crb, Patj
CC and sdt. Interacts directly with nrx via its third and fourth PDZ
CC domains. Interacts directly with par-6, possibly mediating a link
CC between the SAC complex and the par-6 complex, which is composed of
CC par-6, baz and aPKC. {ECO:0000269|PubMed:10102271,
CC ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:11740560,
CC ECO:0000269|PubMed:12900452}.
CC -!- INTERACTION:
CC Q9NB04; A1Z9X0: aPKC; NbExp=2; IntAct=EBI-442573, EBI-160861;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10102271,
CC ECO:0000269|PubMed:11076972}. Note=Membrane-associated. Localizes to
CC the subapical domain of cells. Sdt is required for its localization. At
CC mitotic cycles 13 and 14, during cellularization, it localizes at the
CC leading edge of the invaginating membranes. It is then exclusively
CC localized to the basal area of columnal epithelial cells. In the
CC germline, it localizes at the membrane of the nurse cells during early
CC and mid oogenesis. Later, it is found in the nuclear membrane in close
CC association with actin filaments that connect the nuclei of the nurse
CC cells with the plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed in primary and some secondary epithelial
CC cells such as ectodermal cells, salivary glands, foregut, hindgut and
CC invaginating tracheal cells. Also expressed in specific cells of the
CC peripheral nervous system. Expressed in the germline.
CC {ECO:0000269|PubMed:10102271, ECO:0000269|PubMed:11076972}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Appears
CC in mitotic cycle 11 when the furrows made by the imprint of the
CC embryonic nuclei become apparent. {ECO:0000269|PubMed:10102271}.
CC -!- SIMILARITY: Belongs to the Patj family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the Disks lost (Dlt) protein.
CC However, PubMed:14667407 showed that it is not the case and renamed it
CC Patj. This drastically changes the first conclusions drawn about its
CC essential function, since the mutant used contained defects for another
CC protein, which is now called Dlt. If its association with proteins
CC involved in cell polarization complexes is clear, Patj is not essential
CC since its absence apparently does not lead to important defects.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43031.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF103942; AAD43031.1; ALT_INIT; mRNA.
DR EMBL; AF274350; AAF81829.1; -; mRNA.
DR EMBL; AE014296; AAN11498.1; -; Genomic_DNA.
DR EMBL; AF132193; AAD34781.1; -; mRNA.
DR RefSeq; NP_477342.1; NM_057994.5.
DR RefSeq; NP_599144.1; NM_134317.4.
DR RefSeq; NP_728674.1; NM_167917.4.
DR AlphaFoldDB; Q9NB04; -.
DR SMR; Q9NB04; -.
DR BioGRID; 68832; 25.
DR IntAct; Q9NB04; 6.
DR MINT; Q9NB04; -.
DR STRING; 7227.FBpp0072662; -.
DR iPTMnet; Q9NB04; -.
DR PaxDb; Q9NB04; -.
DR DNASU; 44100; -.
DR EnsemblMetazoa; FBtr0072779; FBpp0072662; FBgn0067864.
DR EnsemblMetazoa; FBtr0072781; FBpp0072664; FBgn0067864.
DR EnsemblMetazoa; FBtr0301625; FBpp0290839; FBgn0067864.
DR GeneID; 44100; -.
DR KEGG; dme:Dmel_CG12021; -.
DR CTD; 10207; -.
DR FlyBase; FBgn0067864; Patj.
DR VEuPathDB; VectorBase:FBgn0067864; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000167964; -.
DR HOGENOM; CLU_006771_1_0_1; -.
DR InParanoid; Q9NB04; -.
DR OMA; SEIVRKW; -.
DR OrthoDB; 532163at2759; -.
DR PhylomeDB; Q9NB04; -.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9NB04; -.
DR BioGRID-ORCS; 44100; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 44100; -.
DR PRO; PR:Q9NB04; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0067864; Expressed in second segment of antenna (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q9NB04; baseline and differential.
DR Genevisible; Q9NB04; DM.
DR GO; GO:0005912; C:adherens junction; IDA:FlyBase.
DR GO; GO:0045179; C:apical cortex; NAS:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; TAS:FlyBase.
DR GO; GO:0005635; C:nuclear envelope; NAS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; NAS:FlyBase.
DR GO; GO:0005918; C:septate junction; TAS:FlyBase.
DR GO; GO:0035003; C:subapical complex; IDA:FlyBase.
DR GO; GO:0032033; F:myosin II light chain binding; IDA:FlyBase.
DR GO; GO:0005080; F:protein kinase C binding; IPI:FlyBase.
DR GO; GO:0034334; P:adherens junction maintenance; IGI:FlyBase.
DR GO; GO:0034332; P:adherens junction organization; IMP:FlyBase.
DR GO; GO:0045176; P:apical protein localization; TAS:FlyBase.
DR GO; GO:0007043; P:cell-cell junction assembly; NAS:FlyBase.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:FlyBase.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; TAS:FlyBase.
DR GO; GO:0016334; P:establishment or maintenance of polarity of follicular epithelium; IPI:FlyBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; TAS:FlyBase.
DR GO; GO:0016333; P:morphogenesis of follicular epithelium; IMP:FlyBase.
DR GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IGI:FlyBase.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:FlyBase.
DR GO; GO:0035209; P:pupal development; IMP:FlyBase.
DR Gene3D; 2.30.42.10; -; 4.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 4.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 4.
DR SUPFAM; SSF50156; SSF50156; 4.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 4.
PE 1: Evidence at protein level;
KW Developmental protein; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..871
FT /note="Patj homolog"
FT /id="PRO_0000094591"
FT DOMAIN 3..67
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 149..229
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 318..403
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 559..648
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 728..814
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 100..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 349
FT /note="S -> N (in Ref. 3; AAF81829)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="S -> N (in Ref. 3; AAF81829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 871 AA; 92852 MW; CE41E80AA2925B4D CRC64;
MHLSADISSA LQQIEAVKKG IDESDDPKLQ MQTAESLSTI LGILQDPVFR TIVHVQDSLS
ELNAQLAQHP SMLPNDFDID VAGNLVLSLN GGEVMYDFDE QRSSSHSHSA PGSPDKSGGV
GEEPRPQSQN SKGAGVADLY ATDYAQIQAI ELVNDGTGLG FGIIGARNSG VIVKTILPGG
VADKDGRLRS GDHILQIGDV NLHEMVSEQV AAVLRQSGTH VRLVVARPVE QSVPTPQYAL
EPGTAVVPTR VLVDPAELER YLISTGYPEI FGESSTASTP QTTTEDDRFV YRGETSMLID
PNIDLEELLA LPETEKLQVE LKKDANGLGI TIAGYVCEKE ELSGIFVKSV SPGSAADLSG
RIRVNDRIIE VDGQSLQGYS NHQAVELLKK SGQVVNLRLE RYLRGPKFEQ LQQAIAANDK
LPSSAPGTPS RAPMPTPVAT TSSATTTPSR SITRELEEEA LPAPEAFMTT PPSVTTMTTT
TLSSFGAGKQ LVAVRDSLDG STKIIPTEVV PLADKTEAKN SGVITRHKYY TDPELSDDAE
TEIIRKWQKI VGSDVEVIVA QIKKFAVGGL GISLEGTVDV EGGREVRPHH YIRSILPDGP
VGVNGVLRSG DELLEVNGER LLGMNHLEVV AILKELPLDV RMVCGRNRNS SLLPFSDDTL
KKLSNNFENL LPATDRLVKA KSDGSLATAG SVADGDSVAA AAASFSKLKS RSLEPLTGLA
MWSSQPQIIE LVKGDRGLGF SILDYQDPLD PNDTLIVIRS LVPGGVAQLD GRLIPGDRLL
FVNSINLENA SLDQAVQALK GASKGVVRIG VAKPLPMTDN SLKACSNAST TSEETLDAQP
SPPALPTVAP PAMPPSASMG AEPDLIPDWR N
