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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.
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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
 
 
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