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INTU_DROME
ID   INTU_DROME              Reviewed;         869 AA.
AC   Q9VPH0; Q24144;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Protein inturned;
GN   Name=in; ORFNames=CG16993;
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], DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=8631273; DOI=10.1242/dev.122.3.961;
RA   Park W.J., Liu J., Sharp E.J., Adler P.N.;
RT   "The Drosophila tissue polarity gene inturned acts cell autonomously and
RT   encodes a novel protein.";
RL   Development 122:961-969(1996).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10570461;
RX   DOI=10.1002/(sici)1520-6408(1999)25:4<297::aid-dvg3>3.0.co;2-l;
RA   Yun U.J., Kim S.Y., Liu J., Adler P.N., Bae E., Kim J., Park W.J.;
RT   "The inturned protein of Drosophila melanogaster is a cytoplasmic protein
RT   located at the cell periphery in wing cells.";
RL   Dev. Genet. 25:297-305(1999).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15556868; DOI=10.1016/j.cub.2004.11.007;
RA   Adler P.N., Zhu C., Stone D.;
RT   "Inturned localizes to the proximal side of wing cells under the
RT   instruction of upstream planar polarity proteins.";
RL   Curr. Biol. 14:2046-2051(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=11973308; DOI=10.1093/genetics/160.4.1535;
RA   Lee H., Adler P.N.;
RT   "The function of the frizzled pathway in the Drosophila wing is dependent
RT   on inturned and fuzzy.";
RL   Genetics 160:1535-1547(2002).
RN   [8]
RP   FUNCTION.
RX   PubMed=18701542; DOI=10.1242/dev.025205;
RA   Strutt D., Warrington S.J.;
RT   "Planar polarity genes in the Drosophila wing regulate the localisation of
RT   the FH3-domain protein Multiple Wing Hairs to control the site of hair
RT   production.";
RL   Development 135:3103-3111(2008).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH MWH.
RX   PubMed=20351219; DOI=10.1534/genetics.110.114066;
RA   Lu Q., Yan J., Adler P.N.;
RT   "The Drosophila planar polarity proteins inturned and multiple wing hairs
RT   interact physically and function together.";
RL   Genetics 185:549-558(2010).
CC   -!- FUNCTION: Plays a role in the definition of cell polarity via the
CC       planar cell polarity (PCP) cascade. Acts downstream of fuz and
CC       accumulates asymmetrically in wing cells to regulate planar polarity in
CC       the wing. Probably acts by regulating ciliogenesis.
CC       {ECO:0000269|PubMed:11973308, ECO:0000269|PubMed:18701542,
CC       ECO:0000269|PubMed:20351219, ECO:0000269|PubMed:8631273}.
CC   -!- SUBUNIT: Interacts with mwh. {ECO:0000269|PubMed:20351219}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10570461}. Cell
CC       membrane {ECO:0000269|PubMed:10570461}. Note=Localizes in the vicinity
CC       of plasma membrane and the cortical actin cytoskeleton of wing disk and
CC       pupal wing cells (PubMed:10570461). Localizes to the proximal side of
CC       wing cells, fuz and frtz are required for its localization
CC       (PubMed:15556868).
CC   -!- DISRUPTION PHENOTYPE: Abnormal wing hair polarity and in many wing
CC       cells forming two or more hairs instead of the normal single hair.
CC       {ECO:0000269|PubMed:8631273}.
CC   -!- SIMILARITY: Belongs to the inturned family. {ECO:0000305}.
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DR   EMBL; U37134; AAC47004.1; -; mRNA.
DR   EMBL; AE014296; AAF51582.2; -; Genomic_DNA.
DR   EMBL; AY089567; AAL90305.1; -; mRNA.
DR   RefSeq; NP_788548.1; NM_176370.3.
DR   AlphaFoldDB; Q9VPH0; -.
DR   BioGRID; 65506; 12.
DR   IntAct; Q9VPH0; 3.
DR   STRING; 7227.FBpp0077841; -.
DR   PaxDb; Q9VPH0; -.
DR   EnsemblMetazoa; FBtr0078183; FBpp0077841; FBgn0001259.
DR   GeneID; 40246; -.
DR   KEGG; dme:Dmel_CG16993; -.
DR   UCSC; CG16993-RA; d. melanogaster.
DR   CTD; 40246; -.
DR   FlyBase; FBgn0001259; in.
DR   VEuPathDB; VectorBase:FBgn0001259; -.
DR   eggNOG; ENOG502QQJQ; Eukaryota.
DR   GeneTree; ENSGT00390000001301; -.
DR   HOGENOM; CLU_014223_0_0_1; -.
DR   InParanoid; Q9VPH0; -.
DR   OMA; WKEINNV; -.
DR   OrthoDB; 898612at2759; -.
DR   PhylomeDB; Q9VPH0; -.
DR   Reactome; R-DME-450728; Inhibition of actin polymerisation.
DR   Reactome; R-DME-5610787; Hedgehog 'off' state.
DR   BioGRID-ORCS; 40246; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; if; fly.
DR   GenomeRNAi; 40246; -.
DR   PRO; PR:Q9VPH0; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0001259; Expressed in capitellum (Drosophila) and 27 other tissues.
DR   Genevisible; Q9VPH0; DM.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR   GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR   GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; TAS:FlyBase.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:0035316; P:non-sensory hair organization; IMP:FlyBase.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR043987; CCZ1/INTU/HSP4_longin_1.
DR   InterPro; IPR043989; CCZ1/INTU/HSP4_longin_3.
DR   InterPro; IPR043988; CCZ1/INTU_longin_2.
DR   InterPro; IPR039151; INTU.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR21082; PTHR21082; 1.
DR   Pfam; PF19031; Intu_longin_1; 1.
DR   Pfam; PF19032; Intu_longin_2; 1.
DR   Pfam; PF19033; Intu_longin_3; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cilium biogenesis/degradation; Cytoplasm;
KW   Developmental protein; Membrane; Reference proteome.
FT   CHAIN           1..869
FT                   /note="Protein inturned"
FT                   /id="PRO_0000416287"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        170
FT                   /note="V -> L (in Ref. 1; AAC47004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="K -> Q (in Ref. 1; AAC47004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="R -> Q (in Ref. 1; AAC47004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        390
FT                   /note="R -> G (in Ref. 1; AAC47004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        440..442
FT                   /note="QLR -> HVP (in Ref. 1; AAC47004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        803
FT                   /note="V -> I (in Ref. 1; AAC47004)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   869 AA;  98133 MW;  84B5393FF4A7F21E CRC64;
     MRKSPASLPS EAFSSSNSSL SNSYSDGSDL ANWEEYVSTD GSLFYMEYVR CEKTGVSAER
     RVEFMRRSLR LGKKSSRRQP HSNNQNQSQN QNQSHGPSRL DSQTEPQEFR FSQFKTAAPD
     PKKLDLVITA ADRFRFGRRS TAVESILGFR VLPFPDQPEC LMVDGFVHDV SALQHGIKRG
     DWFRSLNGIE VYASNVDELL KQFVEPTQVC LGFQSCGAAS AVSPTDPGYN RNVREEQVCK
     VENFPMFTEK FEQMLITEGN FGIPGSSVDI RMPFAMLLLP PECYQHEQQQ DSLYYFPEIP
     DNFLFKARGS FLTLHAVLSE LHTQPLSSRL LVDQVQYHVN YRQLNGFLVL FAYAGGLCCA
     AECSLRSDEL IGYIRFSLPG LVLESFNQER EPGNSSRLKL FLRHFCEIQR TRLVARCHGH
     IRFEELLGQS RSLPLPKEAQ LRIFDALSEM EAMDYRNWND EPLTTHREFF IYGSALYYDG
     FLVASLLPPE VRVSVEGFLR CRGIFELLGA APGIKVREMY VWEEIVLPSA TGRYFLTICT
     KNHLSLAVIL KIFDAPDMAP DAVVGPSLFY IEEIQETLDH LVQCGIESLA MFWSVSNKRP
     EVLDATASES RDQEKEPNNR LESFLKQKLT VLSPSVEEEA QLCSSLGGSS IHSLTPSEDE
     SCRRRLTPIH GTAEDSDSGS DWENFAVQHP LHYGLNLGAE SHSQSQMTES MWKEINNVVP
     VKISAGWKNS VLHYVYIDIA NGSLFAPFTD SSENSNYLSE IRQACHIIHA VLQKSKHYRR
     HLSESSRAQT NSNGHSSHTV SLVKEHGMIL EVSTQPKSDG QSQSSTSSRF VVVGRLFQSP
     AKEVYVCHRS DVPQNIVEMA FRLSFFSMG
 
 
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