WIF1_XENLA
ID WIF1_XENLA Reviewed; 374 AA.
AC Q9W6F8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Wnt inhibitory factor 1;
DE Short=WIF-1;
DE Flags: Precursor;
GN Name=wif1;
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].
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).
CC -!- FUNCTION: Binds to WNT proteins and inhibits their activities. May be
CC involved in mesoderm segmentation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: During somatogenesis, expressed predominantly in
CC unsegmented paraxial presomitic mesoderm and, to a much lesser extent,
CC in newly segmented somites.
CC -!- DEVELOPMENTAL STAGE: First expressed at neurula stages.
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; AF122924; AAD25404.1; -; mRNA.
DR RefSeq; NP_001084220.1; NM_001090751.1.
DR AlphaFoldDB; Q9W6F8; -.
DR SMR; Q9W6F8; -.
DR GeneID; 399375; -.
DR KEGG; xla:399375; -.
DR CTD; 399375; -.
DR Xenbase; XB-GENE-865617; wif1.S.
DR OrthoDB; 1016037at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 399375; Expressed in testis and 8 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR013111; EGF_extracell.
DR InterPro; IPR003306; WIF.
DR InterPro; IPR038677; WIF_sf.
DR InterPro; IPR013309; Wnt-inh.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF12661; hEGF; 2.
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; 5.
DR PROSITE; PS50026; EGF_3; 4.
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..374
FT /note="Wnt inhibitory factor 1"
FT /id="PRO_0000007778"
FT DOMAIN 33..172
FT /note="WIF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00222"
FT DOMAIN 173..205
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 208..237
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 237..269
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 270..301
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 302..333
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 343..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 135..172
FT /evidence="ECO:0000250"
FT DISULFID 177..187
FT /evidence="ECO:0000250"
FT DISULFID 181..193
FT /evidence="ECO:0000250"
FT DISULFID 195..204
FT /evidence="ECO:0000250"
FT DISULFID 209..219
FT /evidence="ECO:0000250"
FT DISULFID 213..225
FT /evidence="ECO:0000250"
FT DISULFID 227..236
FT /evidence="ECO:0000250"
FT DISULFID 241..251
FT /evidence="ECO:0000250"
FT DISULFID 245..257
FT /evidence="ECO:0000250"
FT DISULFID 259..268
FT /evidence="ECO:0000250"
FT DISULFID 273..283
FT /evidence="ECO:0000250"
FT DISULFID 277..289
FT /evidence="ECO:0000250"
FT DISULFID 291..300
FT /evidence="ECO:0000250"
FT DISULFID 305..315
FT /evidence="ECO:0000250"
FT DISULFID 309..321
FT /evidence="ECO:0000250"
FT DISULFID 323..332
FT /evidence="ECO:0000250"
SQ SEQUENCE 374 AA; 41071 MW; E26F973B0F00ACF8 CRC64;
MSLTGYFAAP LCSIFLFILA HADAGQQEDS LYMWIDAHQA RVLIGFEEDI LIVAEGKMAP
FTHDFRKAQQ RMPAIPVNIH AMNFTWQATG QAEYFYEFLS LRSLDKGIMA DPTVNMPLLG
TVPHKATVIQ VGFPCLGNQD GVAAFEVNVI VMNSEGNVIL QTPQNAIFFK TCQQAKCTGG
CRNGGFCNDR HVCECPDGFY GPHCEKALCM PRCMNGGLCV TPGLCICPPG YYGINCDKVN
CTTHCLNGGT CFYPGKCICP SGYEGEQCET SKCQQPCRNG GKCSGKNKCK CSKGYQGDLC
SKPVCEPSCG AHGTCIEPNK CQCKEGWNGR YCNKKYGSNL MNALRPTGSR NRQHTPSPKR
TEDRQALPES NYIW