WIF1_RAT
ID WIF1_RAT Reviewed; 379 AA.
AC Q6IN38; Q924Y6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Wnt inhibitory factor 1;
DE Short=WIF-1;
DE Flags: Precursor;
GN Name=Wif1;
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 [MRNA] (ISOFORM 2), AND INDUCTION.
RX PubMed=12065666; DOI=10.1046/j.1471-4159.2002.00847.x;
RA De Smet C., Nishimori H., Furnari F.B., Boegler O., Huang H.-J.S.,
RA Cavenee W.K.;
RT "A novel seven transmembrane receptor induced during the early steps of
RT astrocyte differentiation identified by differential expression.";
RL J. Neurochem. 81:575-588(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6IN38-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IN38-2; Sequence=VSP_013172;
CC -!- INDUCTION: Induced during the differentiation of CG-4 cells.
CC {ECO:0000269|PubMed:12065666}.
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DR EMBL; AY030278; AAK51134.1; -; mRNA.
DR EMBL; BC072473; AAH72473.1; -; mRNA.
DR RefSeq; NP_446190.1; NM_053738.1. [Q6IN38-2]
DR RefSeq; XP_006241457.1; XM_006241395.3. [Q6IN38-1]
DR AlphaFoldDB; Q6IN38; -.
DR SMR; Q6IN38; -.
DR STRING; 10116.ENSRNOP00000006426; -.
DR GlyGen; Q6IN38; 2 sites.
DR PhosphoSitePlus; Q6IN38; -.
DR PaxDb; Q6IN38; -.
DR Ensembl; ENSRNOT00000006426; ENSRNOP00000006426; ENSRNOG00000004476. [Q6IN38-1]
DR GeneID; 114557; -.
DR KEGG; rno:114557; -.
DR CTD; 11197; -.
DR RGD; 619774; Wif1.
DR eggNOG; KOG1225; Eukaryota.
DR GeneTree; ENSGT00940000160401; -.
DR HOGENOM; CLU_041961_0_0_1; -.
DR InParanoid; Q6IN38; -.
DR OMA; KSKCKCP; -.
DR OrthoDB; 1016037at2759; -.
DR PhylomeDB; Q6IN38; -.
DR PRO; PR:Q6IN38; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004476; Expressed in lung and 16 other tissues.
DR Genevisible; Q6IN38; RN.
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:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:RGD.
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 Alternative splicing; Developmental protein; Disulfide bond;
KW EGF-like domain; Glycoprotein; Reference proteome; Repeat; Secreted;
KW 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_0000007777"
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..274
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 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 264..273
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"
FT VAR_SEQ 293..308
FT /note="KCKCPKGYQGDLCSKP -> KS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12065666"
FT /id="VSP_013172"
SQ SEQUENCE 379 AA; 41585 MW; 55229F6FDCC1021C CRC64;
MARRRAFPAF VLRLWSILPC LLLLRADAGQ PPEESLYLWI DAHQARVLIG FEEDILIVSE
GKMAPFTHDF RKAQQRMPAI PVNIHSMNFT WQASGQAEYF YEFLSLRSLD KGIMADPTVN
VPRLGTVPHK ASVVQVGFPC LGKQDGVAAF EVNVIVMNSE GNPILRTPQN AIFFKTCQQA
ECPGGCRNGG FCNERRVCEC PDGFYGPHCE KALCIPRCMN GGLCVTPGFC ICPPGFYGVN
CDKANCSATC FNGGTCFYPG KCICPPGLEG EQCELSKCPQ PCRNGGKCIG KSKCKCPKGY
QGDLCSKPVC EPGCGAHGTC HEPNKCQCRE GWHGRHCNKR YGASLMHAPR PAGAGLERHT
PSLKKAEGRR DPPESNYIW
