INTU_RAT
ID INTU_RAT Reviewed; 942 AA.
AC D4ACE5;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 AlphaFoldDB; D4ACE5; -.
DR SMR; D4ACE5; -.
DR iPTMnet; D4ACE5; -.
DR PhosphoSitePlus; D4ACE5; -.
DR PRIDE; D4ACE5; -.
DR UCSC; RGD:1309446; rat.
DR RGD; 1309446; Intu.
DR InParanoid; D4ACE5; -.
DR PhylomeDB; D4ACE5; -.
DR TreeFam; TF323932; -.
DR Reactome; R-RNO-5610787; Hedgehog 'off' state.
DR PRO; PR:D4ACE5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0035869; C:ciliary transition zone; ISO:RGD.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:InterPro.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; ISO:RGD.
DR GO; GO:0051782; P:negative regulation of cell division; ISO:RGD.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0021915; P:neural tube development; ISO:RGD.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISO:RGD.
DR GO; GO:0033365; P:protein localization to organelle; ISO:RGD.
DR GO; GO:0030278; P:regulation of ossification; ISO:RGD.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0021513; P:spinal cord dorsal/ventral patterning; ISO:RGD.
DR GO; GO:0043587; P:tongue morphogenesis; ISO:RGD.
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 Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Developmental protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..942
FT /note="Protein inturned"
FT /id="PRO_0000416284"
FT DOMAIN 189..267
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 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD6"
SQ SEQUENCE 942 AA; 105142 MW; 938478970E98D63B CRC64;
MADPARRDPR GRAPELPGDL SSQEEEEEES DSDAGASSLG SCSSASSDTD LEPEWLDSVQ
RNGELFYLEL SEDEEESLLP ETQTVNHVNH VRFSEKEVII EEDDSRERKK YEPKLRRFTK
ILKSKSLLPK RHHKKKSSNT GPVSILKHQS TQRTGVTVQQ RYKDVTVYIN PKKLTAIKAR
EQAKLLEVLV GVIHQTKWSW KRSGKQADGE RLVVHGLVPG GSAMKSGQVL VGDVLVAVND
VDVTSENIER VLSCIPGPMQ VKLTFENAYA VKKETAQPKK KKAQSSTNDL VKLLCGSEAD
ATQHSTLSIP HITMYLTLQL QSEVAREEQE MLYHYPVSEA SQKLKSVRGI FLTLCDMLES
VTGTQVTSSS LHVNGKQIHV AYLKESDKLL LIGLPAEEVP LPQLRNMTED VAQTLKFMYG
SLDSAFCQVE NTPRLDHFFS LFFERALRPG KLHLSASPSA QQYDAASAVL LDNLPGVRWL
LLPQELKVEL DTALSDLEAA DFQELSEDYY DMRRLYTILG SSLFYKGYMV CSHLPKDDVV
EIAAYCRQYC LLPLAAQQRI GQLIIWREVF PQHHLQPATD SDPEAFQEPE GRYFLLIVGL
RHYMLCVLLE AGGCASKATG NPGPDCIYVD QARATLHQLE GVESRIEEQL AATPGPCLSC
ADWFLAAPRE KADSLTTSPI LGRLQGPSKT AASPTCRRTF FSDYSFKARK PSPSRIGGGR
EPGEGEENVG LSPHTTPDTV RKQRESEGSD DNVALLKLAR KKSTLPNPFH LGTSKKELSE
KELEVYNMMK LTSGPENTLF HYVALETVQG IFITPTHEEV AQLGGSVHSQ LIKNFHRCCL
TIRAVFQQTL KVEKKKALSD GDHLESANSV SSLSPVKEHG VLFECSPENW TDQKKTPPVM
SYWVVGRLFL NPKPQELYVC FHDSVSEIAI EMAFRLFFGL TL
