WIF1_MOUSE
ID WIF1_MOUSE Reviewed; 379 AA.
AC Q9WUA1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Wnt inhibitory factor 1;
DE Short=WIF-1;
DE Flags: Precursor;
GN Name=Wif1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10201374; DOI=10.1038/18899;
RA Hsieh J.-C., Kodjabachian L., Rebbert M.L., Rattner A., Smallwood P.M.,
RA Samos C.H., Nusse R., Dawid I.B., Nathans J.;
RT "A new secreted protein that binds to Wnt proteins and inhibits their
RT activities.";
RL Nature 398:431-436(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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).
CC -!- FUNCTION: Binds to WNT proteins and inhibits their activities. May be
CC involved in mesoderm segmentation.
CC -!- SUBUNIT: Interacts with MYOC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expression highest in heart and lung. Lower in
CC brain and eye.
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; AF122923; AAD25403.1; -; mRNA.
DR EMBL; BC013268; AAH13268.1; -; mRNA.
DR CCDS; CCDS24209.1; -.
DR RefSeq; NP_036045.1; NM_011915.2.
DR AlphaFoldDB; Q9WUA1; -.
DR BMRB; Q9WUA1; -.
DR SMR; Q9WUA1; -.
DR STRING; 10090.ENSMUSP00000020439; -.
DR GlyGen; Q9WUA1; 2 sites.
DR PhosphoSitePlus; Q9WUA1; -.
DR PaxDb; Q9WUA1; -.
DR PRIDE; Q9WUA1; -.
DR ProteomicsDB; 299979; -.
DR Antibodypedia; 29209; 505 antibodies from 33 providers.
DR DNASU; 24117; -.
DR Ensembl; ENSMUST00000020439; ENSMUSP00000020439; ENSMUSG00000020218.
DR GeneID; 24117; -.
DR KEGG; mmu:24117; -.
DR UCSC; uc007hfj.2; mouse.
DR CTD; 11197; -.
DR MGI; MGI:1344332; Wif1.
DR VEuPathDB; HostDB:ENSMUSG00000020218; -.
DR eggNOG; KOG1225; Eukaryota.
DR GeneTree; ENSGT00940000160401; -.
DR HOGENOM; CLU_041961_0_0_1; -.
DR InParanoid; Q9WUA1; -.
DR OMA; KSKCKCP; -.
DR OrthoDB; 1016037at2759; -.
DR PhylomeDB; Q9WUA1; -.
DR BioGRID-ORCS; 24117; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Wif1; mouse.
DR PRO; PR:Q9WUA1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9WUA1; protein.
DR Bgee; ENSMUSG00000020218; Expressed in molar tooth and 217 other tissues.
DR ExpressionAtlas; Q9WUA1; baseline and differential.
DR Genevisible; Q9WUA1; MM.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; ISO:MGI.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.2170; -; 1.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003306; WIF.
DR InterPro; IPR038677; WIF_sf.
DR InterPro; IPR013309; Wnt-inh.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF02019; WIF; 1.
DR PRINTS; PR01901; WIFPROTEIN.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00469; WIF; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS50814; WIF; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..379
FT /note="Wnt inhibitory factor 1"
FT /id="PRO_0000007776"
FT DOMAIN 38..177
FT /note="WIF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00222"
FT DOMAIN 178..210
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 211..242
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 243..271
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 274..306
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 307..338
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 348..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..177
FT /evidence="ECO:0000250"
FT DISULFID 182..192
FT /evidence="ECO:0000250"
FT DISULFID 186..198
FT /evidence="ECO:0000250"
FT DISULFID 200..209
FT /evidence="ECO:0000250"
FT DISULFID 214..224
FT /evidence="ECO:0000250"
FT DISULFID 218..230
FT /evidence="ECO:0000250"
FT DISULFID 232..241
FT /evidence="ECO:0000250"
FT DISULFID 246..256
FT /evidence="ECO:0000250"
FT DISULFID 250..262
FT /evidence="ECO:0000250"
FT DISULFID 278..288
FT /evidence="ECO:0000250"
FT DISULFID 282..294
FT /evidence="ECO:0000250"
FT DISULFID 296..305
FT /evidence="ECO:0000250"
FT DISULFID 310..320
FT /evidence="ECO:0000250"
FT DISULFID 314..326
FT /evidence="ECO:0000250"
FT DISULFID 328..337
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 41590 MW; E3765F2642B2BC9A CRC64;
MARRRAFPAF ALRLWSILPC LLLLRADAGQ PPEESLYLWI DAHQARVLIG FEEDILIVSE
GKMAPFTHDF RKAQQRMPAI PVNIHSMNFT WQAAGQAEYF YEFLSLRSLD KGIMADPTVN
VPLLGTVPHK ASVVQVGFPC LGKQDGVAAF EVNVIVMNSE GNTILRTPQN AIFFKTCQQA
ECPGGCRNGG FCNERRVCEC PDGFYGPHCE KALCIPRCMN GGLCVTPGFC ICPPGFYGVN
CDKANCSTTC FNGGTCFYPG KCICPPGLEG EQCELSKCPQ PCRNGGKCIG KSKCKCPKGY
QGDLCSKPVC EPGCGAHGTC HEPNKCQCRE GWHGRHCNKR YGASLMHAPR PAGAGLERHT
PSLKKAEDRR DPPESNYIW
