WTIP_DANRE
ID WTIP_DANRE Reviewed; 648 AA.
AC A8DZE6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Wilms tumor protein 1-interacting protein homolog;
DE Short=WT1-interacting protein homolog;
GN Name=wtip; ORFNames=si:ch211-79l17.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}.
CC Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; AL929392; CAP09265.1; -; Genomic_DNA.
DR RefSeq; NP_001116750.2; NM_001123278.2.
DR AlphaFoldDB; A8DZE6; -.
DR STRING; 7955.ENSDARP00000087671; -.
DR PaxDb; A8DZE6; -.
DR Ensembl; ENSDART00000157564; ENSDARP00000132856; ENSDARG00000103607.
DR GeneID; 566046; -.
DR KEGG; dre:566046; -.
DR CTD; 126374; -.
DR ZFIN; ZDB-GENE-050419-261; wtip.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000160924; -.
DR HOGENOM; CLU_001357_11_1_1; -.
DR InParanoid; A8DZE6; -.
DR OMA; MMLHAAP; -.
DR OrthoDB; 326249at2759; -.
DR PhylomeDB; A8DZE6; -.
DR TreeFam; TF320310; -.
DR Reactome; R-DRE-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR PRO; PR:A8DZE6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000103607; Expressed in pharyngeal gill and 23 other tissues.
DR ExpressionAtlas; A8DZE6; baseline.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:ZFIN.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0035844; P:cloaca development; IMP:ZFIN.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:ZFIN.
DR GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; IMP:ZFIN.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IBA:GO_Central.
DR GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IBA:GO_Central.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR GO; GO:0061032; P:visceral serous pericardium development; IMP:ZFIN.
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 3: Inferred from homology;
KW Cell junction; LIM domain; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..648
FT /note="Wilms tumor protein 1-interacting protein homolog"
FT /id="PRO_0000328862"
FT DOMAIN 437..498
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 502..561
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 562..631
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 27..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 70901 MW; EF08B1EF30DACCEF CRC64;
MDEYDEDPGR RASKLMETLS IYDVYQDGMY GEPNPDMEKT KRMNGSSSTP GNKVYSAAPV
RSVNGNRASV PLDFCSPQRE AVYPDPDVYC TKSEVALPCY SGASDRLRRY THAEVQGHRY
STGCAYDGLV LGKQVAVSGA RSNSLCMSSP DGRYTATSPR SSLASSHSSQ DQSKHTSPRS
SISSPRSSLV SPGQGEGTSV ISPRSSYAST ASDTSKHSSP RTSLNSYDCG SKPSSNRTSG
ISMGYDQRHI SPRSSTTSPR SSYSDSRFTP AGGHDPESAA VHGIPMASPR SSICSQPAVA
ANCVVSPRSS ISSHSSRSSR SSRGSMSAYP ELQLPMLGPG LPEDALLQDF TEPNGLHNNR
VHLQTFPVLE EPQQQNSEVN IGFNYCKAGA GGQRFKLPYQ VTPSRDSGPS QAERRLEALT
LELEKELEIH MKKEYFGICV KCGKGVYGAS QACQAMGNLY HTNCFTCCSC GRRLRGKAFY
NVNGKVYCEE DFLYSGFQQT AEKCFVCGHL IMEMILQALG RSYHPGCFRC VICKEGLDGV
PFTVDVENNI YCVKDYHTVF APKCASCNQP ILPAQGSEET IRVVSMDKDY HVDCYHCEDC
GLQLNDEEGH RCYPLEGHLL CHRCHLHRLK TPLAPHPPPS YPLHVTEL
