INTU_HUMAN
ID INTU_HUMAN Reviewed; 942 AA.
AC Q9ULD6; A1L4N5; D6RAE6; D6RBT4; Q4W5I8; Q86V55;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
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=KIAA1284, PDZD6, PDZK6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP INTERACTION WITH NPHP4 AND DAAM1, AND SUBCELLULAR LOCATION.
RX PubMed=26644512; DOI=10.1083/jcb.201502043;
RA Yasunaga T., Hoff S., Schell C., Helmstaedter M., Kretz O., Kuechlin S.,
RA Yakulov T.A., Engel C., Mueller B., Bensch R., Ronneberger O., Huber T.B.,
RA Lienkamp S.S., Walz G.;
RT "The polarity protein Inturned links NPHP4 to Daam1 to control the
RT subapical actin network in multiciliated cells.";
RL J. Cell Biol. 211:963-973(2015).
RN [9]
RP INVOLVEMENT IN OFD17; SRTD7/20 AND SRTD20, FUNCTION, INTERACTION WITH
RP CPLANE1, VARIANT THR-452, VARIANTS SRTD20 355-GLU--LEU-942 DEL AND ALA-500,
RP VARIANT SRTD7/20 276-GLN--LEU-942 DEL, AND CHARACTERIZATION OF VARIANTS
RP SRTD20 355-GLU--LEU-942 DEL AND ALA-500.
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 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
CC (PubMed:27158779). {ECO:0000250|UniProtKB:Q059U7,
CC ECO:0000250|UniProtKB:Q2I0E5, ECO:0000305|PubMed:27158779}.
CC -!- SUBUNIT: Interacts with CPLANE1. Interacts with FUZ and WDPCP; FUZ,
CC INTU and WDPCP probably form the core CPLANE (ciliogenesis and planar
CC polarity effectors) complex (By similarity). Interacts with NPHP4 and
CC DAAM1; INTU is mediating the interaction between NPHP4 and DAAM1
CC (PubMed:26644512). {ECO:0000250|UniProtKB:Q059U7,
CC ECO:0000269|PubMed:26644512}.
CC -!- INTERACTION:
CC Q9ULD6; Q9Y4D1: DAAM1; NbExp=3; IntAct=EBI-11762696, EBI-2817289;
CC Q9ULD6; O75161: NPHP4; NbExp=2; IntAct=EBI-11762696, EBI-4281852;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q059U7}. Cell
CC surface {ECO:0000250|UniProtKB:Q2I0E5}. Cytoplasm, cytoskeleton, cilium
CC basal body {ECO:0000269|PubMed:26644512}. Note=Enriched at the apical
CC surface in ciliated cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9ULD6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULD6-2; Sequence=VSP_015073, VSP_015074;
CC Name=3;
CC IsoId=Q9ULD6-3; Sequence=VSP_042586, VSP_042587;
CC Name=4;
CC IsoId=Q9ULD6-4; Sequence=VSP_042585;
CC -!- DISEASE: Short-rib thoracic dysplasia 20 with polydactyly (SRTD20)
CC [MIM:617925]: A form of short-rib thoracic dysplasia, a group of
CC autosomal recessive ciliopathies that are characterized by a
CC constricted thoracic cage, short ribs, shortened tubular bones, and a
CC 'trident' appearance of the acetabular roof. Polydactyly is variably
CC present. Non-skeletal involvement can include cleft lip/palate as well
CC as anomalies of major organs such as the brain, eye, heart, kidneys,
CC liver, pancreas, intestines, and genitalia. Some forms of the disease
CC are lethal in the neonatal period due to respiratory insufficiency
CC secondary to a severely restricted thoracic cage, whereas others are
CC compatible with life. Disease spectrum encompasses Ellis-van Creveld
CC syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-
CC Saldino syndrome, and short rib-polydactyly syndrome.
CC {ECO:0000269|PubMed:27158779}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Orofaciodigital syndrome 17 (OFD17) [MIM:617926]: A form of
CC orofaciodigital syndrome, a group of heterogeneous disorders
CC characterized by malformations of the oral cavity, face and digits, and
CC associated phenotypic abnormalities that lead to the delineation of
CC various subtypes. OFD17 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:27158779}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Short-rib thoracic dysplasia 7/20 with polydactyly, digenic
CC (SRTD7/20) [MIM:614091]: A digenic form of short-rib thoracic dysplasia
CC caused by double heterozygosity for a mutation in the WDR35 gene and a
CC mutation in the INTU gene. Short-rib thoracic dysplasia is part of a
CC group of ciliopathies that are characterized by a constricted thoracic
CC cage, short ribs, shortened tubular bones, and a 'trident' appearance
CC of the acetabular roof. Polydactyly is variably present. Non-skeletal
CC involvement can include cleft lip/palate as well as anomalies of major
CC organs such as the brain, eye, heart, kidneys, liver, pancreas,
CC intestines, and genitalia. Some forms of the disease are lethal in the
CC neonatal period due to respiratory insufficiency secondary to a
CC severely restricted thoracic cage, whereas others are compatible with
CC life. Disease spectrum encompasses Ellis-van Creveld syndrome,
CC asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino
CC syndrome, and short rib-polydactyly syndrome. Note=The disease is
CC caused by variants affecting distinct genetic loci, including the gene
CC represented in this entry. SRTD7/20 can be caused by co-occurrence of
CC WDR35 variant p.Trp311Leu and INTU p.Gln276Ter. One such patient has
CC been reported. {ECO:0000269|PubMed:27158779}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the inturned family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86598.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB033110; BAA86598.1; ALT_INIT; mRNA.
DR EMBL; AK291481; BAF84170.1; -; mRNA.
DR EMBL; AC093591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC097462; AAY41002.1; -; Genomic_DNA.
DR EMBL; AC110797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX05202.1; -; Genomic_DNA.
DR EMBL; BC051698; AAH51698.1; -; mRNA.
DR EMBL; BC130611; AAI30612.1; -; mRNA.
DR CCDS; CCDS34061.1; -. [Q9ULD6-1]
DR RefSeq; NP_056508.2; NM_015693.3. [Q9ULD6-1]
DR RefSeq; XP_011530148.1; XM_011531846.1. [Q9ULD6-4]
DR PDB; 7Q3D; EM; 3.35 A; B=2-942.
DR PDBsum; 7Q3D; -.
DR AlphaFoldDB; Q9ULD6; -.
DR BioGRID; 118034; 48.
DR ComplexPortal; CPX-5001; CPLANE complex.
DR IntAct; Q9ULD6; 43.
DR STRING; 9606.ENSP00000334003; -.
DR iPTMnet; Q9ULD6; -.
DR PhosphoSitePlus; Q9ULD6; -.
DR BioMuta; INTU; -.
DR DMDM; 73621379; -.
DR EPD; Q9ULD6; -.
DR MassIVE; Q9ULD6; -.
DR MaxQB; Q9ULD6; -.
DR PaxDb; Q9ULD6; -.
DR PeptideAtlas; Q9ULD6; -.
DR PRIDE; Q9ULD6; -.
DR ProteomicsDB; 84999; -. [Q9ULD6-1]
DR ProteomicsDB; 85000; -. [Q9ULD6-2]
DR ProteomicsDB; 85001; -. [Q9ULD6-3]
DR ProteomicsDB; 85002; -. [Q9ULD6-4]
DR Antibodypedia; 26899; 82 antibodies from 17 providers.
DR DNASU; 27152; -.
DR Ensembl; ENST00000335251.11; ENSP00000334003.5; ENSG00000164066.13. [Q9ULD6-1]
DR Ensembl; ENST00000503626.5; ENSP00000426287.1; ENSG00000164066.13. [Q9ULD6-2]
DR Ensembl; ENST00000503952.5; ENSP00000421995.1; ENSG00000164066.13. [Q9ULD6-3]
DR GeneID; 27152; -.
DR KEGG; hsa:27152; -.
DR MANE-Select; ENST00000335251.11; ENSP00000334003.5; NM_015693.4; NP_056508.2.
DR UCSC; uc003ifk.3; human. [Q9ULD6-1]
DR CTD; 27152; -.
DR DisGeNET; 27152; -.
DR GeneCards; INTU; -.
DR HGNC; HGNC:29239; INTU.
DR HPA; ENSG00000164066; Tissue enhanced (retina).
DR MalaCards; INTU; -.
DR MIM; 610621; gene.
DR MIM; 614091; phenotype.
DR MIM; 617925; phenotype.
DR MIM; 617926; phenotype.
DR neXtProt; NX_Q9ULD6; -.
DR OpenTargets; ENSG00000164066; -.
DR PharmGKB; PA162392193; -.
DR VEuPathDB; HostDB:ENSG00000164066; -.
DR eggNOG; ENOG502QQJQ; Eukaryota.
DR GeneTree; ENSGT00390000001301; -.
DR HOGENOM; CLU_014223_0_1_1; -.
DR InParanoid; Q9ULD6; -.
DR OMA; WKEINNV; -.
DR OrthoDB; 898612at2759; -.
DR PhylomeDB; Q9ULD6; -.
DR TreeFam; TF323932; -.
DR PathwayCommons; Q9ULD6; -.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR SignaLink; Q9ULD6; -.
DR BioGRID-ORCS; 27152; 8 hits in 1080 CRISPR screens.
DR ChiTaRS; INTU; human.
DR GenomeRNAi; 27152; -.
DR Pharos; Q9ULD6; Tbio.
DR PRO; PR:Q9ULD6; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9ULD6; protein.
DR Bgee; ENSG00000164066; Expressed in right uterine tube and 159 other tissues.
DR ExpressionAtlas; Q9ULD6; baseline and differential.
DR Genevisible; Q9ULD6; HS.
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; IDA:UniProtKB.
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; IDA:UniProtKB.
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; IMP:GO_Central.
DR GO; GO:0001736; P:establishment of planar polarity; IC:ComplexPortal.
DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
DR GO; GO:0042073; P:intraciliary transport; IC:ComplexPortal.
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; IC:ComplexPortal.
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:1902017; P:regulation of cilium assembly; IC:ComplexPortal.
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; IMP:GO_Central.
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; IMP:GO_Central.
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.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Developmental protein; Disease variant; Phosphoprotein; Reference proteome.
FT CHAIN 1..942
FT /note="Protein inturned"
FT /id="PRO_0000058296"
FT DOMAIN 185..263
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4ACE5"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..49
FT /note="MASVASCDSRPSSDELPGDPSSQEEDEDYDFEDRVSDSGSYSSASSDYD ->
FT MFQVGRSSIPKPAPRSLEDLDSVQRVLLHS (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_042585"
FT VAR_SEQ 395..408
FT /note="VPLPRLRNMIENVI -> IELPSSAHTHGERN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015073"
FT VAR_SEQ 409..942
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015074"
FT VAR_SEQ 421..435
FT /note="AFCQIENVPRLDHFF -> IMKEFSVIVSSGKII (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042586"
FT VAR_SEQ 436..942
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042587"
FT VARIANT 276..942
FT /note="Missing (in SRTD7/20; in an SRTD7/20 patient who
FT also carries variant WDR35 L-311)"
FT /evidence="ECO:0000269|PubMed:27158779"
FT /id="VAR_080710"
FT VARIANT 355..942
FT /note="Missing (in SRTD20; loss of subcellular location to
FT cilium basal body, when tested in a heterologous system)"
FT /evidence="ECO:0000269|PubMed:27158779"
FT /id="VAR_080711"
FT VARIANT 452
FT /note="A -> T (in dbSNP:rs150681845)"
FT /evidence="ECO:0000269|PubMed:27158779"
FT /id="VAR_076782"
FT VARIANT 500
FT /note="E -> A (in SRTD20; unknown pathological
FT significance; impairs recruitment of IFT43 to the basal
FT body, but no effect on subcellular location, when tested in
FT a heterologous system; dbSNP:rs1360128571)"
FT /evidence="ECO:0000269|PubMed:27158779"
FT /id="VAR_076783"
SQ SEQUENCE 942 AA; 105648 MW; F21BF6BC0EF7A8F8 CRC64;
MASVASCDSR PSSDELPGDP SSQEEDEDYD FEDRVSDSGS YSSASSDYDD LEPEWLDSVQ
KNGELFYLEL SEDEEESLLP ETPTVNHVRF SENEIIIEDD YKERKKYEPK LKQFTKILRR
KRLLPKRCNK KNSNDNGPVS ILKHQSNQKT GVIVQQRYKD VNVYVNPKKL TVIKAKEQLK
LLEVLVGIIH QTKWSWRRTG KQGDGERLVV HGLLPGGSAM KSGQVLIGDV LVAVNDVDVT
TENIERVLSC IPGPMQVKLT FENAYDVKRE TSHPRQKKTQ SNTSDLVKLL WGEEVEGIQQ
SGLNTPHIIM YLTLQLDSET SKEEQEILYH YPMSEASQKL KSVRGIFLTL CDMLENVTGT
QVTSSSLLLN GKQIHVAYWK ESDKLLLIGL PAEEVPLPRL RNMIENVIQT LKFMYGSLDS
AFCQIENVPR LDHFFNLFFQ RALQPAKLHS SASPSAQQYD ASSAVLLDNL PGVRWLTLPL
EIKMELDMAL SDLEAADFAE LSEDYYDMRR LYTILGSSLF YKGYLICSHL PKDDLIDIAV
YCRHYCLLPL AAKQRIGQLI IWREVFPQHH LRPLADSSTE VFPEPEGRYF LLVVGLKHYM
LCVLLEAGGC ASKAIGSPGP DCVYVDQVKT TLHQLDGVDS RIDERLASSP VPCLSCADWF
LTGSREKTDS LTTSPILSRL QGTSKVATSP TCRRTLFGDY SLKTRKPSPS CSSGGSDNGC
EGGEDDGFSP HTTPDAVRKQ RESQGSDGLE ESGTLLKVTK KKSTLPNPFH LGNLKKDLPE
KELEIYNTVK LTSGPENTLF HYVALETVQG IFITPTLEEV AQLSGSIHPQ LIKNFHQCCL
SIRAVFQQTL VEEKKKGLNS GDHSDSAKSV SSLNPVKEHG VLFECSPGNW TDQKKAPPVM
AYWVVGRLFL HPKPQELYVC FHDSVTEIAI EIAFKLFFGL TL
