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Database: UniProt
Entry: Q9Y5W5
LinkDB: Q9Y5W5
Original site: Q9Y5W5 
ID   WIF1_HUMAN              Reviewed;         379 AA.
AC   Q9Y5W5; Q6UXI1; Q8WVG4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 3.
DT   13-FEB-2019, entry version 170.
DE   RecName: Full=Wnt inhibitory factor 1;
DE            Short=WIF-1;
DE   Flags: Precursor;
GN   Name=WIF1; ORFNames=UNQ191/PRO217;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10201374; DOI=10.1038/18899;
RA   Hsieh J.-C., Kodjabachian L., Rebbert M.L., Rattner A.,
RA   Smallwood P.M., 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].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH MYOC.
RX   PubMed=19188438; DOI=10.1128/MCB.01274-08;
RA   Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.;
RT   "Myocilin is a modulator of Wnt signaling.";
RL   Mol. Cell. Biol. 29:2139-2154(2009).
RN   [5]
RP   STRUCTURE BY NMR OF 32-181, AND DISULFIDE BOND.
RX   PubMed=16476441; DOI=10.1016/j.jmb.2006.01.047;
RA   Liepinsh E., Banyai L., Patthy L., Otting G.;
RT   "NMR structure of the WIF domain of the human Wnt-inhibitory factor-
RT   1.";
RL   J. Mol. Biol. 357:942-950(2006).
CC   -!- FUNCTION: Binds to WNT proteins and inhibits their activities. May
CC       be involved in mesoderm segmentation.
CC   -!- SUBUNIT: Interacts with MYOC. {ECO:0000269|PubMed:19188438}.
CC   -!- INTERACTION:
CC       P60410:KRTAP10-8; NbExp=5; IntAct=EBI-3922719, EBI-10171774;
CC       P27467:Wnt3a (xeno); NbExp=8; IntAct=EBI-3922719, EBI-2899665;
CC       P41221:WNT5A; NbExp=2; IntAct=EBI-3922719, EBI-6594545;
CC       P22725:Wnt5a (xeno); NbExp=7; IntAct=EBI-3922719, EBI-1570983;
CC       O00755:WNT7A; NbExp=3; IntAct=EBI-3922719, EBI-727198;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/WIF1ID44085ch12q14.html";
DR   EMBL; AF122922; AAD25402.1; -; mRNA.
DR   EMBL; AY358344; AAQ88710.1; -; mRNA.
DR   EMBL; BC018037; AAH18037.1; -; mRNA.
DR   CCDS; CCDS8971.1; -.
DR   PIR; A59180; A59180.
DR   RefSeq; NP_009122.2; NM_007191.4.
DR   UniGene; Hs.284122; -.
DR   PDB; 2D3J; NMR; -; A=32-181.
DR   PDB; 2YGN; X-ray; 1.85 A; A=35-178.
DR   PDB; 2YGO; X-ray; 1.85 A; A=35-210.
DR   PDB; 2YGP; X-ray; 2.22 A; A=35-210.
DR   PDB; 2YGQ; X-ray; 3.95 A; A=35-346.
DR   PDBsum; 2D3J; -.
DR   PDBsum; 2YGN; -.
DR   PDBsum; 2YGO; -.
DR   PDBsum; 2YGP; -.
DR   PDBsum; 2YGQ; -.
DR   ProteinModelPortal; Q9Y5W5; -.
DR   SMR; Q9Y5W5; -.
DR   BioGrid; 116366; 11.
DR   DIP; DIP-59097N; -.
DR   IntAct; Q9Y5W5; 15.
DR   MINT; Q9Y5W5; -.
DR   STRING; 9606.ENSP00000286574; -.
DR   iPTMnet; Q9Y5W5; -.
DR   PhosphoSitePlus; Q9Y5W5; -.
DR   BioMuta; WIF1; -.
DR   DMDM; 61252765; -.
DR   PaxDb; Q9Y5W5; -.
DR   PeptideAtlas; Q9Y5W5; -.
DR   PRIDE; Q9Y5W5; -.
DR   ProteomicsDB; 86517; -.
DR   DNASU; 11197; -.
DR   Ensembl; ENST00000286574; ENSP00000286574; ENSG00000156076.
DR   GeneID; 11197; -.
DR   KEGG; hsa:11197; -.
DR   UCSC; uc001ssk.4; human.
DR   CTD; 11197; -.
DR   DisGeNET; 11197; -.
DR   EuPathDB; HostDB:ENSG00000156076.9; -.
DR   GeneCards; WIF1; -.
DR   HGNC; HGNC:18081; WIF1.
DR   HPA; HPA039104; -.
DR   MIM; 605186; gene.
DR   neXtProt; NX_Q9Y5W5; -.
DR   OpenTargets; ENSG00000156076; -.
DR   PharmGKB; PA38291; -.
DR   eggNOG; ENOG410IQQ0; Eukaryota.
DR   eggNOG; ENOG41104IN; LUCA.
DR   GeneTree; ENSGT00940000160401; -.
DR   HOVERGEN; HBG017335; -.
DR   InParanoid; Q9Y5W5; -.
DR   KO; K01691; -.
DR   OMA; INCDKAN; -.
DR   OrthoDB; 1016037at2759; -.
DR   PhylomeDB; Q9Y5W5; -.
DR   Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR   Reactome; R-HSA-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
DR   SignaLink; Q9Y5W5; -.
DR   SIGNOR; Q9Y5W5; -.
DR   ChiTaRS; WIF1; human.
DR   EvolutionaryTrace; Q9Y5W5; -.
DR   GeneWiki; WIF1; -.
DR   GenomeRNAi; 11197; -.
DR   PRO; PR:Q9Y5W5; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000156076; Expressed in 184 organ(s), highest expression level in upper lobe of lung.
DR   ExpressionAtlas; Q9Y5W5; baseline and differential.
DR   Genevisible; Q9Y5W5; HS.
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; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; NAS:ProtInc.
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; 2.
DR   Pfam; PF02019; WIF; 1.
DR   PRINTS; PR01901; WIFPROTEIN.
DR   ProDom; PD013948; WIF; 1.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Developmental protein;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Reference proteome;
KW   Repeat; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   CHAIN        29    379       Wnt inhibitory factor 1.
FT                                /FTId=PRO_0000007775.
FT   DOMAIN       38    177       WIF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00222}.
FT   DOMAIN      178    210       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      211    242       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      243    271       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      274    306       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      307    338       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     88     88       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    245    245       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    140    177       {ECO:0000269|PubMed:16476441}.
FT   DISULFID    182    192       {ECO:0000250}.
FT   DISULFID    186    198       {ECO:0000250}.
FT   DISULFID    200    209       {ECO:0000250}.
FT   DISULFID    214    224       {ECO:0000250}.
FT   DISULFID    218    230       {ECO:0000250}.
FT   DISULFID    232    241       {ECO:0000250}.
FT   DISULFID    246    256       {ECO:0000250}.
FT   DISULFID    250    262       {ECO:0000250}.
FT   DISULFID    278    288       {ECO:0000250}.
FT   DISULFID    282    294       {ECO:0000250}.
FT   DISULFID    296    305       {ECO:0000250}.
FT   DISULFID    310    320       {ECO:0000250}.
FT   DISULFID    314    326       {ECO:0000250}.
FT   DISULFID    328    337       {ECO:0000250}.
FT   CONFLICT    166    166       Q -> K (in Ref. 3; AAH18037).
FT                                {ECO:0000305}.
FT   CONFLICT    178    178       Q -> L (in Ref. 1; AAD25402).
FT                                {ECO:0000305}.
FT   STRAND       36     40       {ECO:0000244|PDB:2YGN}.
FT   HELIX        42     49       {ECO:0000244|PDB:2YGN}.
FT   STRAND       55     59       {ECO:0000244|PDB:2YGN}.
FT   HELIX        65     67       {ECO:0000244|PDB:2YGN}.
FT   STRAND       68     70       {ECO:0000244|PDB:2YGO}.
FT   HELIX        74     76       {ECO:0000244|PDB:2YGN}.
FT   STRAND       85     93       {ECO:0000244|PDB:2YGN}.
FT   STRAND       95     97       {ECO:0000244|PDB:2YGN}.
FT   STRAND       99    109       {ECO:0000244|PDB:2YGN}.
FT   STRAND      111    113       {ECO:0000244|PDB:2D3J}.
FT   STRAND      118    121       {ECO:0000244|PDB:2YGN}.
FT   STRAND      123    126       {ECO:0000244|PDB:2YGN}.
FT   STRAND      131    137       {ECO:0000244|PDB:2YGN}.
FT   STRAND      146    158       {ECO:0000244|PDB:2YGN}.
FT   STRAND      163    165       {ECO:0000244|PDB:2YGN}.
FT   STRAND      173    177       {ECO:0000244|PDB:2YGN}.
FT   TURN        206    209       {ECO:0000244|PDB:2YGO}.
SQ   SEQUENCE   379 AA;  41528 MW;  32ADFA6644833E9D CRC64;
     MARRSAFPAA ALWLWSILLC LLALRAEAGP PQEESLYLWI DAHQARVLIG FEEDILIVSE
     GKMAPFTHDF RKAQQRMPAI PVNIHSMNFT WQAAGQAEYF YEFLSLRSLD KGIMADPTVN
     VPLLGTVPHK ASVVQVGFPC LGKQDGVAAF EVDVIVMNSE GNTILQTPQN AIFFKTCQQA
     ECPGGCRNGG FCNERRICEC PDGFHGPHCE KALCTPRCMN GGLCVTPGFC ICPPGFYGVN
     CDKANCSTTC FNGGTCFYPG KCICPPGLEG EQCEISKCPQ PCRNGGKCIG KSKCKCSKGY
     QGDLCSKPVC EPGCGAHGTC HEPNKCQCQE GWHGRHCNKR YEASLIHALR PAGAQLRQHT
     PSLKKAEERR DPPESNYIW
//
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