ID   WNT6_MOUSE              Reviewed;         364 AA.
AC   P22727; Q80ZM9;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   24-JAN-2024, entry version 169.
DE   RecName: Full=Protein Wnt-6;
DE   Flags: Precursor;
GN   Name=Wnt6; Synonyms=Wnt-6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2279700; DOI=10.1101/gad.4.12b.2319;
RA   Gavin B.J., McMahon J.A., McMahon A.P.;
RT   "Expression of multiple novel Wnt-1/int-1-related genes during fetal and
RT   adult mouse development.";
RL   Genes Dev. 4:2319-2332(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
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).
RN   [5]
RP   INTERACTION WITH PORCN.
RX   PubMed=10866835; DOI=10.1046/j.1432-1033.2000.01478.x;
RA   Tanaka K., Okabayashi H., Asashima M., Perrimon N., Kadowaki T.;
RT   "The evolutionarily conserved porcupine gene family is involved in the
RT   processing of the Wnt family.";
RL   Eur. J. Biochem. 267:4300-4311(2000).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=22370641; DOI=10.1038/onc.2012.40;
RA   Yuan G., Regel I., Lian F., Friedrich T., Hitkova I., Hofheinz R.D.,
RA   Stroebel P., Langer R., Keller G., Roecken C., Zimmermann W., Schmid R.M.,
RA   Ebert M.P.A., Burgermeister E.;
RT   "WNT6 is a novel target gene of caveolin-1 promoting chemoresistance to
RT   epirubicin in human gastric cancer cells.";
RL   Oncogene 32:375-387(2013).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. Probable developmental protein. May be a
CC       signaling molecule which affects the development of discrete regions of
CC       tissues. Is likely to signal over only few cell diameters.
CC   -!- SUBUNIT: Interacts with PORCN. {ECO:0000269|PubMed:10866835}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- TISSUE SPECIFICITY: Detected in ileum, colon and stomach (at protein
CC       level). {ECO:0000269|PubMed:22370641}.
CC   -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC       receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC       inhibition. {ECO:0000250|UniProtKB:P27467,
CC       ECO:0000250|UniProtKB:P56704}.
CC   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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; M89800; AAA40569.1; -; mRNA.
DR   EMBL; AK133954; BAE21949.1; -; mRNA.
DR   EMBL; CH466548; EDL00351.1; -; Genomic_DNA.
DR   EMBL; BC048700; AAH48700.1; -; mRNA.
DR   CCDS; CCDS15056.1; -.
DR   PIR; F36470; F36470.
DR   RefSeq; NP_033552.2; NM_009526.3.
DR   RefSeq; XP_006495950.1; XM_006495887.3.
DR   RefSeq; XP_006495951.1; XM_006495888.3.
DR   AlphaFoldDB; P22727; -.
DR   SMR; P22727; -.
DR   BioGRID; 204579; 1.
DR   IntAct; P22727; 1.
DR   STRING; 10090.ENSMUSP00000006716; -.
DR   GlyCosmos; P22727; 2 sites, No reported glycans.
DR   GlyGen; P22727; 2 sites.
DR   PhosphoSitePlus; P22727; -.
DR   SwissPalm; P22727; -.
DR   MaxQB; P22727; -.
DR   PaxDb; 10090-ENSMUSP00000006716; -.
DR   ProteomicsDB; 299774; -.
DR   Antibodypedia; 34291; 272 antibodies from 34 providers.
DR   DNASU; 22420; -.
DR   Ensembl; ENSMUST00000006716.8; ENSMUSP00000006716.7; ENSMUSG00000033227.8.
DR   GeneID; 22420; -.
DR   KEGG; mmu:22420; -.
DR   UCSC; uc007bne.1; mouse.
DR   AGR; MGI:98960; -.
DR   CTD; 7475; -.
DR   MGI; MGI:98960; Wnt6.
DR   VEuPathDB; HostDB:ENSMUSG00000033227; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000159281; -.
DR   HOGENOM; CLU_033039_1_3_1; -.
DR   InParanoid; P22727; -.
DR   OMA; EWTNCNC; -.
DR   OrthoDB; 2874082at2759; -.
DR   PhylomeDB; P22727; -.
DR   TreeFam; TF105310; -.
DR   Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR   BioGRID-ORCS; 22420; 2 hits in 80 CRISPR screens.
DR   PRO; PR:P22727; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P22727; Protein.
DR   Bgee; ENSMUSG00000033227; Expressed in lumbar dorsal root ganglion and 190 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
DR   GO; GO:0009798; P:axis specification; IDA:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:MGI.
DR   GO; GO:0060684; P:epithelial-mesenchymal cell signaling; IDA:MGI.
DR   GO; GO:0072080; P:nephron tubule development; IDA:MGI.
DR   GO; GO:0072079; P:nephron tubule formation; IDA:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR   GO; GO:0070172; P:positive regulation of tooth mineralization; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR   CDD; cd19338; Wnt_Wnt6; 1.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR009143; Wnt6.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027:SF72; PROTEIN WNT-6; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01845; WNT6PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
DR   Genevisible; P22727; MM.
PE   1: Evidence at protein level;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..364
FT                   /note="Protein Wnt-6"
FT                   /id="PRO_0000041441"
FT   REGION          140..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           227
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        123..131
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        133..171
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        221..235
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        223..230
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        293..324
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        309..319
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        323..363
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        339..354
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        341..351
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        346..347
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   CONFLICT        233
FT                   /note="R -> S (in Ref. 1; AAA40569)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  39656 MW;  6F28CE191F98A0AC CRC64;
     MLPPVPSRLG LLLLLLCPAH VDGLWWAVGS PLVMDPTSIC RKARRLAGRQ AELCQAEPEV
     VAELARGARL GVRECQFQFR FRRWNCSSHS KAFGRVLQQD IRETAFVFAI TAAGASHAVT
     QACSMGELLQ CGCQAPRGRA PPRPSGLLGT PGPPGPTGSP DASAAWEWGG CGDDVDFGDE
     KSRLFMDAQH KRGRGDIRAL VQLHNNEAGR LAVRSHTRTE CKCHGLSGSC ALRTCWQKLP
     PFREVGARLL ERFHGASRVM GTNDGKALLP AVRTLKPPGR ADLLYAADSP DFCAPNRRTG
     SPGTRGRACN SSAPDLSGCD LLCCGRGHRQ ESVQLEENCL CRFHWCCVVQ CHRCRVRKEL
     SLCL
//