WNT2_DASNO
ID WNT2_DASNO Reviewed; 360 AA.
AC Q07E44;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Protein Wnt-2;
DE Flags: Precursor;
GN Name=WNT2;
OS Dasypus novemcinctus (Nine-banded armadillo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Xenarthra; Cingulata; Dasypodidae; Dasypus.
OX NCBI_TaxID=9361;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Functions in the canonical Wnt signaling
CC pathway that results in activation of transcription factors of the
CC TCF/LEF family (By similarity). {ECO:0000250|UniProtKB:P09544,
CC ECO:0000250|UniProtKB:P21552}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P09544}. Secreted
CC {ECO:0000250|UniProtKB:P09544}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC inhibition. {ECO:0000250|UniProtKB:P09544}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; DP000181; ABI93632.1; -; Genomic_DNA.
DR RefSeq; NP_001268692.1; NM_001281763.1.
DR AlphaFoldDB; Q07E44; -.
DR SMR; Q07E44; -.
DR Ensembl; ENSDNOT00000009298; ENSDNOP00000007200; ENSDNOG00000009309.
DR GeneID; 101432213; -.
DR KEGG; dnm:101432213; -.
DR CTD; 7472; -.
DR HOGENOM; CLU_033039_1_4_1; -.
DR OMA; PKSADWT; -.
DR OrthoDB; 745245at2759; -.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IEA:Ensembl.
DR GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
DR GO; GO:1904954; P:canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; IEA:Ensembl.
DR GO; GO:0033278; P:cell proliferation in midbrain; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0061180; P:mammary gland epithelium development; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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 3: Inferred from homology;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..360
FT /note="Protein Wnt-2"
FT /id="PRO_0000260341"
FT LIPID 212
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..87
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 127..135
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 137..157
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 206..220
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 208..215
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 278..309
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 294..304
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 308..348
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 324..339
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 326..336
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 331..332
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 360 AA; 40426 MW; D85C3C7FB9516E77 CRC64;
MNAPLGGIWL WLPLLLTWLT PEVSSSWWYM RATGGSSRVM CDNVPGLVSR QRQLCHRHPD
VMRAIGLGVA EWTAECQHQF RQHRWNCNTL DRDHSLFGRV LLRSSRESAF VYAISSAGVV
FAITRACSQG ELKSCSCDPK KKGTAKDSKG TFDWGGCSDN IDHGIKFARA FVDAKERKGK
DARALMNLHN NRAGRKAVKR FLKQECKCHG VSGSCTLRTC WLAMADFRKT GDYLWRKYNG
AIQVVMNQDG TGFTVANKRF KKPTKNDLVY FENSPDYCIR DRDAGSLGTA GRVCNLTSRG
MDSCEVMCCG RGYDTSHVTR MTKCECKFHW CCAVRCQDCL EALDVHTCKA PKSADWAVPT
