ID   INTU_DANRE              Reviewed;         915 AA.
AC   E7FCN8;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Protein inturned;
DE   AltName: Full=Inturned planar cell polarity effector homolog;
GN   Name=intu;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Plays a key role in ciliogenesis and embryonic development.
CC       Regulator of cilia formation by controlling the organization of the
CC       apical actin cytoskeleton and the positioning of the basal bodies at
CC       the apical cell surface, which in turn is essential for the normal
CC       orientation of elongating ciliary microtubules. Plays a key role in
CC       definition of cell polarity via its role in ciliogenesis but not via
CC       conversion extension. Has an indirect effect on hedgehog signaling (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q059U7}. Cell
CC       surface {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250|UniProtKB:Q2I0E5}. Note=Enriched at the apical surface in
CC       ciliated cells. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the inturned family. {ECO:0000305}.
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DR   EMBL; CABZ01030293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01030294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005172228.1; XM_005172171.3.
DR   AlphaFoldDB; E7FCN8; -.
DR   STRING; 7955.ENSDARP00000101586; -.
DR   PaxDb; E7FCN8; -.
DR   PeptideAtlas; E7FCN8; -.
DR   Ensembl; ENSDART00000173376; ENSDARP00000142182; ENSDARG00000077639.
DR   ZFIN; ZDB-GENE-110914-91; intu.
DR   eggNOG; ENOG502QQJQ; Eukaryota.
DR   GeneTree; ENSGT00390000001301; -.
DR   HOGENOM; CLU_014223_0_1_1; -.
DR   InParanoid; E7FCN8; -.
DR   OMA; WKEINNV; -.
DR   PhylomeDB; E7FCN8; -.
DR   TreeFam; TF323932; -.
DR   PRO; PR:E7FCN8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 7.
DR   Bgee; ENSDARG00000077639; Expressed in early embryo and 19 other tissues.
DR   ExpressionAtlas; E7FCN8; baseline.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0001736; P:establishment of planar polarity; IEA:InterPro.
DR   GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   Gene3D; 2.30.42.10; -; 1.
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; IPR001478; PDZ.
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.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Reference proteome.
FT   CHAIN           1..915
FT                   /note="Protein inturned"
FT                   /id="PRO_0000416285"
FT   DOMAIN          165..253
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          88..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          688..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   915 AA;  101132 MW;  D060480E12EA7A4B CRC64;
     MFSTCSDGRP FQSFSTNLED FDSIRSVLLY SDLEPEWLDD VQKNGQLFYL ELSDGEEEAL
     LAQVSANHSA ATNHVRFSEK EAEIITDNAK RQANSSNKSE AKLKKLTKIL RRKRRPSQRK
     AEGKDSSQRP ASILKNQAGQ RPGVVVQQQR LKDVCVYLNP KRLSSVSSSS ADRGGLLEAL
     LGVVHRPGGN TGKRGGKLII HGLIPHSPAS KCAEILIGDA LVAVDDVEVT SENIERVLSC
     IPGPMQVRLT LETVCPAGVS PESKVSASPQ VSQLVRLLWG EDTIELQMSI ADVPHIAMFL
     SLRLDSETQQ DEQEIVYQYP QSEASAQLKA VRGIFLTLCD MLENVTGGQI ISSSLWLQQQ
     LVHVGYWKEE SNLLVIAVPA SRVPLLYLQT VIEGVVRTLK VMYGSLDRGF SDVENAPRLD
     HFFCLFFQQL IQPSRLIHSS RTPDLYGSLF LDGLPAVRWL TLPPDIKVEV DTVLSDFESS
     DFGDMSEDFY GMRRLYVILG SCLFYKGYLI ANHLPKEDLL DVCLYCQHYC LLPLASEQRV
     AQLVVWREVF PQRRETRNST AHPGYCQPHA RHFLLIVGLR HFMQCVLLEA GGCASSAVGR
     PTPDSVYVDQ VKATLLQLES LDAGIEERLS APPTPCLSCA DWFLPAGGRS QQDTIGSSPI
     LNRLTAAIKP PSPGGIGRSL FGEAGTVGIR GRRASPQRSQ SDSGSEGHAD GTPASVARRD
     SLGSGGSDGS LGSAGFLKMP RLKHPNPFYL GSLRKSLSER ETEEMQNVLQ VTAGVENTLF
     HYVLMESVQG IFIAPTHTEI RHLSGSIHPQ LIHNFQHCCL SIRQAFQQSL PTRDRRGPER
     QSTAGLGPVK EHGVLFQCKP QNWTDQKKPA PTMTYWVIGR MLLEPVPQEF YVCFHDSVAE
     VPVEMAFRLS FGLAV