ID   WTIP_XENLA              Reviewed;         690 AA.
AC   A9LS46;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Wilms tumor protein 1-interacting protein homolog;
DE            Short=WT1-interacting protein homolog;
DE            Short=xWtip;
GN   Name=wtip;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=18331720; DOI=10.1016/j.devcel.2008.01.005;
RA   Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L.,
RA   Longmore G.D.;
RT   "Ajuba LIM proteins are snail/slug corepressors required for neural crest
RT   development in Xenopus.";
RL   Dev. Cell 14:424-436(2008).
RN   [2]
RP   INTERACTION WITH PRICKLE3, AND FUNCTION.
RX   PubMed=27062996; DOI=10.1038/srep24104;
RA   Chu C.W., Ossipova O., Ioannou A., Sokol S.Y.;
RT   "Prickle3 synergizes with Wtip to regulate basal body organization and
RT   cilia growth.";
RL   Sci. Rep. 6:24104-24104(2016).
CC   -!- FUNCTION: May monitor slit diaphragm protein assembly, a specialized
CC       adherens junction characteristic of podocytes. In case of podocyte
CC       injury, it shuttles into the nucleus and acts as a transcription
CC       regulator. Plays a role in the regulation of cell morphology and
CC       cytoskeletal organization (By similarity). Acts as a transcriptional
CC       corepressor for snai1 and snai2/slug and plays a role in regulating
CC       neural crest development. Involved in the organization of the basal
CC       body (PubMed:27062996). Involved in cilia growth and positioning
CC       (PubMed:27062996). {ECO:0000250, ECO:0000269|PubMed:18331720,
CC       ECO:0000269|PubMed:27062996}.
CC   -!- SUBUNIT: Interacts with prickle3 (PubMed:27062996).
CC       {ECO:0000269|PubMed:27062996}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}.
CC       Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU257484; ABX55937.1; -; mRNA.
DR   RefSeq; NP_001106366.1; NM_001112895.1.
DR   AlphaFoldDB; A9LS46; -.
DR   PRIDE; A9LS46; -.
DR   GeneID; 100127345; -.
DR   KEGG; xla:100127345; -.
DR   CTD; 100127345; -.
DR   OrthoDB; 326249at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 100127345; Expressed in internal ear and 19 other tissues.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0014032; P:neural crest cell development; IMP:UniProtKB.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00412; LIM; 3.
DR   SMART; SM00132; LIM; 3.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE   1: Evidence at protein level;
KW   Cell junction; Cilium biogenesis/degradation; LIM domain; Metal-binding;
KW   Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..690
FT                   /note="Wilms tumor protein 1-interacting protein homolog"
FT                   /id="PRO_0000328863"
FT   DOMAIN          479..540
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          544..603
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          604..673
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          151..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  75335 MW;  EEF940168E00B880 CRC64;
     MEKYDEDIAL QASKFLEDLS LCDGHSRLYG PVGDMLLSND HILVADHRGR RLNGSLTQYL
     PHSSSDKVYP LGSSQLRSMN GSRGDGYMDE GIYKSDVALP CYSGISEKNK RYSAELYRHS
     CGNSFEGVPI SAKQGGITAL YSGGKMSNSC MSATSPRSSM ASSASSSQEH SKYSSPRSSI
     SSNALSLDKF SSPRSSLVVP GQQEKYTSPR SSLGQYEGGV LSPRSSYAST TSDTSKHSSP
     RASLTSYDCG SKPSSNRTSG ISMGYDQRHI SPRSSTASQY SCTTSPRSSY SDSRYVPSGN
     PDLDGVGGHG SLVSPRSSMC LQEGRSATLG SCNPSVVSPR SSISSHSSRS SRSSRGSMGA
     YTDLTVPSPR SSMLGTSLQE ETLVQDLGEA CHYKVLTQSP PRQEQHQTIT SSHDLNSGAV
     ASYNFSSAKG SATVHRFKLP YQVTPSRESG PSQAERRLEA LTLELEKELE LHMKKEYFGI
     CIKCGKGVYG ASQACQAMGN LYHTNCFTCC SCGRRLRGKA FYNVNGKVYC EEDFLYSGFQ
     QTADKCFVCG HLIMEMILQA LGKSYHPGCF RCVVCNECLD GVPFTVDVEN NIYCVKDYHT
     VFAPKCASCN QPILPAQGSE ETIRVVSMDK DYHVECYHCE DCQLQLNDEE GRRCYPLEGH
     LLCHSCHIRR LSVNVPPHQP PSYPMHVTEL