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Wilms tumor protein 1-interacting protein (WT1-interacting protein)

 WTIP_MOUSE              Reviewed;         398 AA.
Q7TQJ8; Q8CG89;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
12-SEP-2018, entry version 115.
RecName: Full=Wilms tumor protein 1-interacting protein;
Short=WT1-interacting protein;
Name=Wtip;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND INTERACTION WITH WT1 AND CD2AP.
PubMed=14736876; DOI=10.1074/jbc.M314155200;
Srichai M.B., Konieczkowski M., Padiyar A., Konieczkowski D.J.,
Mukherjee A., Hayden P.S., Kamat S., El-Meanawy M.A., Khan S.,
Mundel P., Lee S.B., Bruggeman L.A., Schelling J.R., Sedor J.R.;
"A WT1 co-regulator controls podocyte phenotype by shuttling between
adhesion structures and nucleus.";
J. Biol. Chem. 279:14398-14408(2004).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15798086; DOI=10.1152/ajprenal.00389.2004;
Rico M., Mukherjee A., Konieczkowski M., Bruggeman L.A., Miller R.T.,
Khan S., Schelling J.R., Sedor J.R.;
"WT1-interacting protein and ZO-1 translocate into podocyte nuclei
after puromycin aminonucleoside treatment.";
Am. J. Physiol. 289:F431-F441(2005).
[5]
FUNCTION.
PubMed=17909014; DOI=10.1158/0008-5472.CAN-07-2987;
Ayyanathan K., Peng H., Hou Z., Fredericks W.J., Goyal R.K.,
Langer E.M., Longmore G.D., Rauscher F.J. III;
"The Ajuba LIM domain protein is a corepressor for SNAG domain
mediated repression and participates in nucleocytoplasmic Shuttling.";
Cancer Res. 67:9097-9106(2007).
[6]
INTERACTION WITH SNAI1; SNAI2/SLUG AND SCRT1.
PubMed=18331720; DOI=10.1016/j.devcel.2008.01.005;
Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L.,
Longmore G.D.;
"Ajuba LIM proteins are snail/slug corepressors required for neural
crest development in Xenopus.";
Dev. Cell 14:424-436(2008).
[7]
INTERACTION WITH ROR2, HOMODIMERIZATION, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=19785987; DOI=10.1016/j.bbrc.2009.09.086;
van Wijk N.V., Witte F., Feike A.C., Schambony A., Birchmeier W.,
Mundlos S., Stricker S.;
"The LIM domain protein Wtip interacts with the receptor tyrosine
kinase Ror2 and inhibits canonical Wnt signalling.";
Biochem. Biophys. Res. Commun. 390:211-216(2009).
[8]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAPK8IP3 AND DYNEIN
INTERMEDIATE CHAIN, AND TISSUE SPECIFICITY.
PubMed=20086015; DOI=10.1074/jbc.M109.061671;
Kim J.H., Konieczkowski M., Mukherjee A., Schechtman S., Khan S.,
Schelling J.R., Ross M.D., Bruggeman L.A., Sedor J.R.;
"Podocyte injury induces nuclear translocation of WTIP via
microtubule-dependent transport.";
J. Biol. Chem. 285:9995-10004(2010).
[9]
SUBCELLULAR LOCATION.
PubMed=21900451; DOI=10.1152/ajprenal.00419.2011;
Kim J.H., Mukherjee A., Madhavan S.M., Konieczkowski M., Sedor J.R.;
"WT1-interacting protein (Wtip) regulates podocyte phenotype by cell-
cell and cell-matrix contact reorganization.";
Am. J. Physiol. 302:F103-F115(2012).
-!- FUNCTION: Adapter or scaffold protein which participates in the
assembly of numerous protein complexes and is involved in several
cellular processes such as cell fate determination, cytoskeletal
organization, repression of gene transcription, cell-cell
adhesion, cell differentiation, proliferation and migration.
Positively regulates microRNA (miRNA)-mediated gene silencing.
Negatively regulates Hippo signaling pathway and antagonizes
phosphorylation of YAP1. Acts as a transcriptional corepressor for
SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin
transcription. Acts as a hypoxic regulator by bridging an
association between the prolyl hydroxylases and VHL enabling
efficient degradation of HIF1A. In podocytes, may play a role in
the regulation of actin dynamics and/or foot process
cytoarchitecture. In the course of podocyte injury, shuttles into
the nucleus and acts as a transcription regulator that represses
WT1-dependent transcription regulation, thereby translating
changes in slit diaphragm structure into altered gene expression
and a less differentiated phenotype. Involved in the organization
of the basal body (By similarity). Involved in cilia growth and
positioning (By similarity). {ECO:0000250|UniProtKB:A9LS46,
ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:15798086,
ECO:0000269|PubMed:17909014, ECO:0000269|PubMed:20086015}.
-!- SUBUNIT: Forms homodimers. Interacts with EIF4E, AGO1, AGO2, DCP2,
DDX6, LATS1, LATS2, SAV1, EGLN2/PHD1 and EGLN3/PHD3. Interacts
(via LIM domains) with VHL (By similarity). Interacts with CD2AP
and WT1. Interacts (via LIM domains) with SNAI1 (via SNAG domain),
SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain).
Interacts with ROR2. Following treatment with bacterial
lipopolysaccharide (LPS), forms a complex with MAPK8IP3 and dynein
intermediate chain. Interacts with PRICKLE3 (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:A9LS46,
ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:18331720,
ECO:0000269|PubMed:19785987, ECO:0000269|PubMed:20086015}.
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
junction, adherens junction. Nucleus. Cytoplasm, cytosol. Cell
membrane. Note=In adherent but isolated podocytes, targets to
focal adhesions and then shifts to adherens junctions after cells
make homotypic contacts. Following podocyte injury, caused by
treatment with LPS, puromycin aminonucleoside, ultraviolet or
hydrogen peroxide, translocates from sites of cell-cell contacts
into the cytosol and nucleus. Maximal nuclear localization is
achieved 6 hours after LPS treatment. Nuclear translocation
requires dynein motor activity and intact microtubule network (By
similarity). Returns to cell-cell contacts several hours after LPS
stimulation. In the presence of ROR2, localizes to the plasma
membrane. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in kidney, lung, eye and ovary. In
kidney, restricted to podocytes. {ECO:0000269|PubMed:14736876,
ECO:0000269|PubMed:20086015}.
-!- DEVELOPMENTAL STAGE: From 9.5 to 11.5 dpc, expressed in the
branchial arches, otic vesicle, limb buds, somites, craniofacial
mesenchyme and tail buds. At 14.5 dpc, expressed in the developing
tongue, nasal cavity, palate, adrenal gland, in the forebrain,
dorsal root ganglia and in the somites. At 14.5 dpc, also detected
in lung, rib cartilage, kidney and intestine (at protein level).
In the kidney, expression peaks at 15 to 16 dpc and decreases
thereafter, but persists in adulthood.
{ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:19785987}.
-!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; BX539331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC042762; AAH42762.1; -; mRNA.
EMBL; BC054125; AAH54125.1; -; mRNA.
CCDS; CCDS21135.1; -.
RefSeq; NP_997095.1; NM_207212.2.
UniGene; Mm.422738; -.
ProteinModelPortal; Q7TQJ8; -.
SMR; Q7TQJ8; -.
BioGrid; 221684; 1.
DIP; DIP-59507N; -.
IntAct; Q7TQJ8; 5.
MINT; Q7TQJ8; -.
STRING; 10090.ENSMUSP00000047623; -.
iPTMnet; Q7TQJ8; -.
PhosphoSitePlus; Q7TQJ8; -.
MaxQB; Q7TQJ8; -.
PaxDb; Q7TQJ8; -.
PeptideAtlas; Q7TQJ8; -.
PRIDE; Q7TQJ8; -.
Ensembl; ENSMUST00000038537; ENSMUSP00000047623; ENSMUSG00000036459.
GeneID; 101543; -.
KEGG; mmu:101543; -.
UCSC; uc009gis.2; mouse.
CTD; 126374; -.
MGI; MGI:2141920; Wtip.
eggNOG; KOG1701; Eukaryota.
eggNOG; ENOG410Y3GP; LUCA.
GeneTree; ENSGT00760000119039; -.
HOGENOM; HOG000007533; -.
HOVERGEN; HBG108679; -.
InParanoid; Q7TQJ8; -.
KO; K16682; -.
OMA; GICVTCG; -.
OrthoDB; EOG091G057U; -.
PhylomeDB; Q7TQJ8; -.
TreeFam; TF320310; -.
Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
PRO; PR:Q7TQJ8; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000036459; Expressed in 235 organ(s), highest expression level in aorta.
ExpressionAtlas; Q7TQJ8; baseline and differential.
Genevisible; Q7TQJ8; MM.
GO; GO:0005912; C:adherens junction; IBA:GO_Central.
GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
GO; GO:0035195; P:gene silencing by miRNA; ISO:MGI.
GO; GO:0035329; P:hippo signaling; IBA:GO_Central.
GO; GO:0035331; P:negative regulation of hippo signaling; ISS:UniProtKB.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0001666; P:response to hypoxia; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR001781; Znf_LIM.
Pfam; PF00412; LIM; 3.
SMART; SM00132; LIM; 3.
PROSITE; PS00478; LIM_DOMAIN_1; 2.
PROSITE; PS50023; LIM_DOMAIN_2; 3.
1: Evidence at protein level;
Cell junction; Cell membrane; Cilium biogenesis/degradation;
Complete proteome; Cytoplasm; LIM domain; Membrane; Metal-binding;
Nucleus; Reference proteome; Repeat; Repressor;
RNA-mediated gene silencing; Transcription; Transcription regulation;
Zinc.
CHAIN 1 398 Wilms tumor protein 1-interacting
protein.
/FTId=PRO_0000328861.
DOMAIN 191 252 LIM zinc-binding 1. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 256 315 LIM zinc-binding 2. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 316 385 LIM zinc-binding 3. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
COMPBIAS 48 134 Gly-rich.
COMPBIAS 130 157 Pro-rich.
SEQUENCE 398 AA; 42254 MW; 6677EE0A882D1E40 CRC64;
MQRSRTAADD AALLLAGLGL RESEPTAGSP GRVRRGPRAV DEAAPASGRR GKGGCGGPEA
APDVPSRPER GPRASLAGSD GGSARSSGIS LGYDQRHGPG PGPPSGGSAR SSVSSLGSRG
SAGACADLLP PGVGPAPARS PEPAQFPFPL PSLPLPPGRE GGPSAAERRL EALTRELERA
LEARTARDYF GICIKCGLGI YGARQACQAM GSLYHTDCFI CDSCGRRLRG KAFYNVGEKV
YCQEDFLYSG FQQTADKCSV CGHLIMEMIL QALGKSYHPG CFRCSVCNEC LDGVPFTVDV
DNNIYCVRDY HTVFAPKCAS CARPILPAQG CETTIRVVSM DRDYHVECYH CEDCGLQLSG
EEGRRCYPLE GHLLCRRCHL RRLGQGPLPS PAVHVTEL


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