WNT2B_MOUSE
ID WNT2B_MOUSE Reviewed; 389 AA.
AC O70283; O88530; Q544L3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein Wnt-2b;
DE AltName: Full=Protein Wnt-13 {ECO:0000303|PubMed:9545553};
DE Flags: Precursor;
GN Name=Wnt2b; Synonyms=Wnt13 {ECO:0000303|PubMed:9545553};
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], AND DEVELOPMENTAL STAGE.
RX PubMed=9545553; DOI=10.1016/s0925-4773(98)00040-9;
RA Zakin L.D.J., Mazan S., Maury M., Martin N., Guenet J.-L., Brulet P.;
RT "Structure and expression of Wnt13, a novel mouse Wnt2 related gene.";
RL Mech. Dev. 73:107-116(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 154-389.
RC STRAIN=NIH Swiss;
RX PubMed=9584130; DOI=10.1242/dev.125.12.2315;
RA Grove E.A., Tole S., Limon J., Yip L., Ragsdale C.W.;
RT "The hem of the embryonic cerebral cortex is defined by the expression of
RT multiple Wnt genes and is compromised in Gli3-deficient mice.";
RL Development 125:2315-2325(1998).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=19686689; DOI=10.1016/j.devcel.2009.06.005;
RA Goss A.M., Tian Y., Tsukiyama T., Cohen E.D., Zhou D., Lu M.M.,
RA Yamaguchi T.P., Morrisey E.E.;
RT "Wnt2/2b and beta-catenin signaling are necessary and sufficient to specify
RT lung progenitors in the foregut.";
RL Dev. Cell 17:290-298(2009).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (Probable). Functions in the canonical
CC Wnt/beta-catenin signaling pathway (PubMed:19686689). Plays a redundant
CC role in embryonic lung development (PubMed:19686689).
CC {ECO:0000269|PubMed:19686689, ECO:0000305}.
CC -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC oligomerization and is required for prolonged biological activity. The
CC complex with AFM may represent the physiological form in body fluids
CC (By similarity). Interacts with FZD4 and FZD5 (By similarity).
CC {ECO:0000250|UniProtKB:Q93097, ECO:0000250|UniProtKB:Q98SN7}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q93097}. Secreted
CC {ECO:0000250|UniProtKB:Q93097}.
CC -!- DEVELOPMENTAL STAGE: Detected at the dorsal midline at the level of the
CC diencephalon and mesencephalon at 9.5 dpc. Detected at the level of the
CC optic and otic vesicles at 9.5 dpc (PubMed:9545553). Detected in the
CC lateral plate mesoderm surrounding the ventral aspect of the anterior
CC foregut at 9.5 dpc (PubMed:19686689). Detected in the mesothelium
CC encasing the lung, and at lower levels in the distal mesenchyme from
CC 12.5 dpc to 14.5 dpc (PubMed:19686689). {ECO:0000269|PubMed:19686689,
CC ECO:0000269|PubMed:9545553}.
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 -!- DISRUPTION PHENOTYPE: No visible phenotype at birth (PubMed:19686689).
CC Combined disruption of Wnt2 and Wnt2b leads to lung agenesis
CC (PubMed:19686689). {ECO:0000269|PubMed:19686689}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; AF070988; AAC25397.1; -; mRNA.
DR EMBL; AK035653; BAC29139.1; -; mRNA.
DR EMBL; CH466608; EDL07557.1; -; Genomic_DNA.
DR EMBL; BC119276; AAI19277.1; -; mRNA.
DR EMBL; BC119278; AAI19279.1; -; mRNA.
DR EMBL; AF038384; AAC40123.1; -; mRNA.
DR CCDS; CCDS17706.1; -.
DR RefSeq; NP_033546.2; NM_009520.3.
DR AlphaFoldDB; O70283; -.
DR SMR; O70283; -.
DR BioGRID; 204573; 1.
DR STRING; 10090.ENSMUSP00000029429; -.
DR GlyGen; O70283; 2 sites.
DR iPTMnet; O70283; -.
DR PhosphoSitePlus; O70283; -.
DR MaxQB; O70283; -.
DR PaxDb; O70283; -.
DR PRIDE; O70283; -.
DR ProteomicsDB; 299697; -.
DR Antibodypedia; 20129; 247 antibodies from 30 providers.
DR DNASU; 22414; -.
DR Ensembl; ENSMUST00000029429; ENSMUSP00000029429; ENSMUSG00000027840.
DR GeneID; 22414; -.
DR KEGG; mmu:22414; -.
DR UCSC; uc008qut.1; mouse.
DR CTD; 7482; -.
DR MGI; MGI:1261834; Wnt2b.
DR VEuPathDB; HostDB:ENSMUSG00000027840; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000159166; -.
DR HOGENOM; CLU_033039_1_0_1; -.
DR InParanoid; O70283; -.
DR OMA; IHYGIRF; -.
DR OrthoDB; 745245at2759; -.
DR PhylomeDB; O70283; -.
DR TreeFam; TF105310; -.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR BioGRID-ORCS; 22414; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Wnt2b; mouse.
DR PRO; PR:O70283; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O70283; protein.
DR Bgee; ENSMUSG00000027840; Expressed in epithelium of female urethra and 119 other tissues.
DR Genevisible; O70283; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0060070; P:canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IEP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0021871; P:forebrain regionalization; IEP:UniProtKB.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; ISO:MGI.
DR GO; GO:0060492; P:lung induction; IGI:MGI.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0060638; P:mesenchymal-epithelial cell signaling; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009140; Wnt2.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01842; WNT2PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..389
FT /note="Protein Wnt-2b"
FT /id="PRO_0000041414"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 241
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..116
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 156..164
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 166..186
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 235..249
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 237..244
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 307..338
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 323..333
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 337..377
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 353..368
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 355..365
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 360..361
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 313
FT /note="A -> S (in Ref. 1; AAC25397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43753 MW; 64F956BB9A00CEEB CRC64;
MLKLQGEDEA AQLAPRRARV PVPRPTAPDV SPSSARLGLA CLLLLLLLTL PARVDTSWWY
IGALGARVIC DNIPGLVSRQ RQLCQRYPDI MRSVGEGARE WIRECQHQFR HHRWNCTTLD
RDHTVFGRAM LRSSREAAFV YAISSAGVVH AITRACSQGE LSVCSCDPYT RGRHHDQRGD
FDWGGCSDNI HYGVRFAKAF VDAKEKRLKD ARALMNLHNN RCGRTAVRRF LKLECKCHGV
SGSCTLRTCW RALSDFRRTG DYLRRRYDGA VQVTATQDGA NFTAARQGYR HATRTDLVYF
DNSPDYCVLD KAAGSLGTAG RVCSKTSKGT DGCEIMCCGR GYDTTRVTRV TQCECKFHWC
CAVRCKECRN TVDVHTCKAP KKAEWLDQT
