INTU_XENLA
ID INTU_XENLA Reviewed; 951 AA.
AC Q2I0E5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Protein inturned;
DE AltName: Full=Inturned planar cell polarity effector homolog {ECO:0000303|PubMed:16493421};
DE Short=Xint {ECO:0000303|PubMed:16493421};
GN Name=intu {ECO:0000250|UniProtKB:Q9ULD6};
GN Synonyms=in {ECO:0000303|PubMed:16493421},
GN int {ECO:0000312|EMBL:ABC75872.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC75872.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16493421; DOI=10.1038/ng1753;
RA Park T.J., Haigo S.L., Wallingford J.B.;
RT "Ciliogenesis defects in embryos lacking inturned or fuzzy function are
RT associated with failure of planar cell polarity and Hedgehog signaling.";
RL Nat. Genet. 38:303-311(2006).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=18552847; DOI=10.1038/ng.104;
RA Park T.J., Mitchell B.J., Abitua P.B., Kintner C., Wallingford J.B.;
RT "Dishevelled controls apical docking and planar polarization of basal
RT bodies in ciliated epithelial cells.";
RL Nat. Genet. 40:871-879(2008).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27158779; DOI=10.1038/ng.3558;
RA Toriyama M., Lee C., Taylor S.P., Duran I., Cohn D.H., Bruel A.L.,
RA Tabler J.M., Drew K., Kelly M.R., Kim S., Park T.J., Braun D.A.,
RA Pierquin G., Biver A., Wagner K., Malfroot A., Panigrahi I., Franco B.,
RA Al-Lami H.A., Yeung Y., Choi Y.J., Duffourd Y., Faivre L., Riviere J.B.,
RA Chen J., Liu K.J., Marcotte E.M., Hildebrandt F., Thauvin-Robinet C.,
RA Krakow D., Jackson P.K., Wallingford J.B.;
RT "The ciliopathy-associated CPLANE proteins direct basal body recruitment of
RT intraflagellar transport machinery.";
RL Nat. Genet. 48:648-656(2016).
CC -!- FUNCTION: Plays a role in the definition of cell polarity via the
CC planar cell polarity (PCP) cascade. Required for ciliogenesis by
CC controlling the organization of the apical actin cytoskeleton and the
CC positioning of the basal bodies at the apical cell surface, which in
CC turn is essential for the normal orientation of elongating ciliary
CC microtubules. Proposed to function as core component of a functional
CC module called CPLANE (ciliogenesis and planar polarity effectors)
CC involved in recruitment of peripheral IFT-A proteins to basal bodies
CC (PubMed:27158779). Controls the localization of both rhoa and
CC disheveled in multi-ciliated cells. Has an indirect effect on hedgehog
CC signaling. {ECO:0000269|PubMed:16493421, ECO:0000269|PubMed:18552847,
CC ECO:0000269|PubMed:27158779}.
CC -!- SUBUNIT: Interacts with fuz and wdpcp; fuz, intu and wdpcp probably
CC form the core CPLANE (ciliogenesis and planar polarity effectors)
CC complex. {ECO:0000250|UniProtKB:Q059U7}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16493421}. Cell
CC membrane {ECO:0000269|PubMed:16493421}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q059U7}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:27158779}. Note=Enriched at the apical surface
CC in ciliated cells. Localizes to the cell membrane in non-ciliated
CC cells. {ECO:0000269|PubMed:16493421}.
CC -!- TISSUE SPECIFICITY: Expressed in the neural plate during neural tube
CC closure with subsequent strong expression in the ventral neural tube
CC and in facial mesenchyme. {ECO:0000269|PubMed:16493421}.
CC -!- SIMILARITY: Belongs to the inturned family. {ECO:0000305}.
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DR EMBL; DQ355992; ABC75872.1; -; mRNA.
DR RefSeq; NP_001089157.1; NM_001095688.1.
DR AlphaFoldDB; Q2I0E5; -.
DR GeneID; 734193; -.
DR KEGG; xla:734193; -.
DR CTD; 734193; -.
DR Xenbase; XB-GENE-919877; intu.S.
DR OrthoDB; 898612at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 734193; Expressed in egg cell and 16 other tissues.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032053; P:ciliary basal body organization; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP: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 SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Developmental protein; Membrane; Reference proteome.
FT CHAIN 1..951
FT /note="Protein inturned"
FT /id="PRO_0000355079"
FT DOMAIN 187..269
FT /note="PDZ"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 106835 MW; F42DCFB85ACFB43A CRC64;
MEHSRGDSVE AGEEEEGRGG WDSRSAGTFS SSCTDCSSYC SSDLEPEWLD RVQKNGELFY
LELSEGEEEI LLPLSPLEPV GVNHVRFSDN EAEILPEDRK NVRKNSEPRF RKLAKMLKKK
NNKKGSAELN RQACPTSILK QNSRQKPGII VHYQYRDTCL YVNPDHLPED EHKKTSNLLQ
ALIGIVHQSS RNSKRSERQG RQESNQRLSN QEKLVVHGFI PGSPAIRCGQ VLIGDTLVAV
NDVEVHVENI ERVLSCIPGP MQLKLTFETP VLYSGMGLKN QNNQAQTSIN DLASLVWGDE
HTNSQQDLQH MPHIVMYLTL RLDSETSKEE QEILYQYPVS DASHKLKSIR GLFLTLGDML
QNVTGAPIVS SSLILNGELV HVSYWKENDK LFLISVPAQR FPLLQLKNVT ADLVRTLKFM
YSTLDRAFCQ AENISRLDHF FSLFFQRVLR VFLLSGITGY GPQFYDACSS LLVENLPGVR
WLSLPEDIKI QIDTVLSDLE ALDFAELSED YYEMRRLYMI IGTCIFYKGY LLSNHLPKED
LVDVVLYCRQ YCLLALASER IGQLIIWREV YPRYHLKHCG SPATEECSEP GGRYFLLIVG
LKHFMLCTLL EAGGCTSKAT GNPGPDYIYV DQVKATLLQL EMLDLNLEER LGSAPNPCLS
CADWFLPSAR DKLGNFTSSI VLNKLQTPKR TTSPVSKRRL FAEAASSLRT RRPSPTRSSG
GSDSGTDGAG ESVGVITHSS PDMARKFGRR ESLGSGGSDG SGGSGTLLKI NKKKYSLPNP
FSSASLRKNL SERETDDIYN TIKLTSGPEN TLFHYLYFET LQGVFISPTH KEVEQLGGSI
HPQLIKNFHR CCLSIRSVFQ QALNKKNSKH SDSKACVDVA GFDPIKEHGV LFECSPENWN
DQKKSPPTMS YWVVGRLFMH PQPQELYVCF HDSVTEISVE LAFKLSFGIP L
