ID   INTU_BOVIN              Reviewed;         933 AA.
AC   F1MDL2;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Protein inturned;
DE   AltName: Full=Inturned planar cell polarity effector homolog;
DE   AltName: Full=PDZ domain-containing protein 6;
GN   Name=INTU; Synonyms=PDZD6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
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). Proposed to function as core component of the CPLANE
CC       (ciliogenesis and planar polarity effectors) complex involved in the
CC       recruitment of peripheral IFT-A proteins to basal bodies (By
CC       similarity). {ECO:0000250|UniProtKB:Q059U7,
CC       ECO:0000250|UniProtKB:Q2I0E5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q059U7}. Cell
CC       surface {ECO:0000250|UniProtKB:Q2I0E5}. Cytoplasm, cytoskeleton, cilium
CC       basal body {ECO:0000250|UniProtKB:Q2I0E5}. Note=Enriched at the apical
CC       surface in ciliated cells. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the inturned family. {ECO:0000305}.
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DR   EMBL; DAAA02044649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001192784.1; NM_001205855.1.
DR   AlphaFoldDB; F1MDL2; -.
DR   STRING; 9913.ENSBTAP00000017038; -.
DR   PaxDb; F1MDL2; -.
DR   Ensembl; ENSBTAT00000017038; ENSBTAP00000017038; ENSBTAG00000012824.
DR   GeneID; 519372; -.
DR   KEGG; bta:519372; -.
DR   CTD; 27152; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012824; -.
DR   VGNC; VGNC:30235; INTU.
DR   eggNOG; ENOG502QQJQ; Eukaryota.
DR   GeneTree; ENSGT00390000001301; -.
DR   HOGENOM; CLU_014223_0_1_1; -.
DR   InParanoid; F1MDL2; -.
DR   OMA; WKEINNV; -.
DR   OrthoDB; 898612at2759; -.
DR   TreeFam; TF323932; -.
DR   Reactome; R-BTA-5610787; Hedgehog 'off' state.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000012824; Expressed in semen and 89 other tissues.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005814; C:centriole; IEA:Ensembl.
DR   GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR   GO; GO:0035869; C:ciliary transition zone; IEA:Ensembl.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR   GO; GO:0051301; P:cell division; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR   GO; GO:0001736; P:establishment of planar polarity; IEA:InterPro.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
DR   GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR   GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR   GO; GO:0044458; P:motile cilium assembly; IEA:Ensembl.
DR   GO; GO:0051782; P:negative regulation of cell division; IEA:Ensembl.
DR   GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR   GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0033365; P:protein localization to organelle; IEA:Ensembl.
DR   GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IEA:Ensembl.
DR   GO; GO:0043587; P:tongue morphogenesis; IEA:Ensembl.
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; Phosphoprotein; Reference proteome.
FT   CHAIN           1..933
FT                   /note="Protein inturned"
FT                   /id="PRO_0000416282"
FT   DOMAIN          186..264
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD6"
SQ   SEQUENCE   933 AA;  104454 MW;  0B960622E6387546 CRC64;
     MASLPLCGSV RSPEGLPGDP SSQEDRQDYD PEDPVSGSGS YSPTSTDSND LEPEWLDSVQ
     KNGELFYLEL SEDEEESLLP ETPTVNHVRF SENEIIIEED DYREGKKYEP KLKRFTKILK
     SKKLLPKRYN KKNSNASGPV SILKHQSNQK MGVIVQQRHK DVNIYVNPKK LTVTKAKEQL
     KLLEVLVGII HQTKWSWRRT GKQGGGERLV VHGLLPGGSA MKSGQVLIGD VLVAVNDVEV
     TSENIERVLS CIPGPMQVKL TFENAYAMKK ETTQPRQKKA QLNTSDLVKL LWGEEVEGIQ
     QNILNTPHIV MYLTLQLDSE TSKEEQEILY HYPVSEASQK LQSVRGIFLT LCDMLENVTG
     TQVTSSSLLL NRKQIHIAYW KETDKLLLIG LPAEEVPLPQ LRNMIEDVAQ TLKFMYGSLD
     SAFCQVENVP RLDHFFSLFF QRALQPTKLH SSASPSTQQY DASSAVLLDN LPGVRWLTLP
     QEIKLELDTA LSDLEAADFA ELSEDYYDMR RLYTILGSSL FYKGYLICSH LPKDDLIDIA
     VYCRHYCLLP LAAKQRIGQL VIWREVFPRH HLQPSADSNT EVFQEPEGRY FLLIVGLRHY
     MLCVLLEAGG CASRAIGNPG PDCIYVDQVK TTLHQLEGVD SRINERLASS PTPCLSCADW
     FLAGSHEKLD NLTTSPILSR LHGASRVATS PTCRRTLFSD YSLKTRKPSP SRSGGPDSGL
     EGEGVGLSPH TTESQGSHGS EETGALLKVT KKKSALPNPF HLGNLKKDLS EKELDIYNTV
     KLTSGPENTL FHYVALETVQ GIFITPTHEE VAQLSGSIHP QLIKNFHQCC LSIRAVFQQT
     VAKEKKKALN GKDHSGSTNS VSSLNPVKEH GVLFECSPEN WTDQRKAPPV MAYWVVGRLF
     LHPKLQELYV CFHDSVTEIA IEMAFKLFFG LTL