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WIF1_DANRE
ID   WIF1_DANRE              Reviewed;         378 AA.
AC   Q9W6F9;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Wnt inhibitory factor 1;
DE            Short=WIF-1;
DE   Flags: Precursor;
GN   Name=wif1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
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: Highly expressed in unsegmented paraxial mesoderm.
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DR   EMBL; AF122925; AAD25405.1; -; mRNA.
DR   PIR; B59180; B59180.
DR   RefSeq; NP_571304.1; NM_131229.1.
DR   AlphaFoldDB; Q9W6F9; -.
DR   SMR; Q9W6F9; -.
DR   STRING; 7955.ENSDARP00000019818; -.
DR   PaxDb; Q9W6F9; -.
DR   GeneID; 30476; -.
DR   KEGG; dre:30476; -.
DR   CTD; 11197; -.
DR   ZFIN; ZDB-GENE-990712-17; wif1.
DR   eggNOG; KOG1225; Eukaryota.
DR   InParanoid; Q9W6F9; -.
DR   OrthoDB; 1016037at2759; -.
DR   PhylomeDB; Q9W6F9; -.
DR   PRO; PR:Q9W6F9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:ZFIN.
DR   GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:ZFIN.
DR   GO; GO:0048794; P:swim bladder development; IMP:ZFIN.
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; 1.
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; 4.
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..378
FT                   /note="Wnt inhibitory factor 1"
FT                   /id="PRO_0000007779"
FT   DOMAIN          36..175
FT                   /note="WIF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00222"
FT   DOMAIN          176..205
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          208..240
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          243..272
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          272..304
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          305..336
FT                   /note="EGF-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          343..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        138..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        180..190
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..196
FT                   /evidence="ECO:0000250"
FT   DISULFID        212..222
FT                   /evidence="ECO:0000250"
FT   DISULFID        216..228
FT                   /evidence="ECO:0000250"
FT   DISULFID        230..239
FT                   /evidence="ECO:0000250"
FT   DISULFID        244..254
FT                   /evidence="ECO:0000250"
FT   DISULFID        248..260
FT                   /evidence="ECO:0000250"
FT   DISULFID        262..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        276..286
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..292
FT                   /evidence="ECO:0000250"
FT   DISULFID        294..303
FT                   /evidence="ECO:0000250"
FT   DISULFID        308..318
FT                   /evidence="ECO:0000250"
FT   DISULFID        312..324
FT                   /evidence="ECO:0000250"
FT   DISULFID        326..335
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  41312 MW;  42FE9F70D948D1D8 CRC64;
     MAFRTPAVQL HLKACVLLLL GGLLEAAYQE RGTMYMWIDA NQARILIGFE EDILIVSEGK
     MAPFTHDFRK AQQRMPAIPV NIHHVNFTWQ ATDQAEYFYE FQTLRSLDKD IMDDPTVNVP
     LLGSVPHKAS VVQVGFPCRG DQDGVAAFEV TILVMDAGGN IILRTPHNAI FFKTCQRAKC
     PGGCRNGGYC NERQVCECQD GFYGVHCEKA LCSPRCLNGG LCMSPGVCIC PPGYFGSSCE
     RANCSTTCLN GGTCFHPGKC ICAVSFEGVR CELSKCRQPC RNGGKCTGRN KCKCSKGYHG
     DLCSKAVCEP SCGAHGTCVE PNRCQCREGW HGRHCNKRFR GGVSNSQRVS PSKHKSPSVA
     AAKEAPETSQ PSETNYVV
 
 
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