WNT5_HALRO
ID WNT5_HALRO Reviewed; 363 AA.
AC O15978;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Protein Wnt-5;
DE Flags: Precursor;
GN Name=WNT5;
OS Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Pyuridae; Halocynthia.
OX NCBI_TaxID=7729;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sasakura Y., Ogasawara M., Makabe K.W.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
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}.
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DR EMBL; AB006608; BAA21878.1; -; Genomic_DNA.
DR AlphaFoldDB; O15978; -.
DR SMR; O15978; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..363
FT /note="Protein Wnt-5"
FT /id="PRO_0000041439"
FT LIPID 227
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..99
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 137..145
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 147..165
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 292..323
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 308..318
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 322..362
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 338..353
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 340..350
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 345..346
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 363 AA; 40828 MW; 79A820F8796527B9 CRC64;
MVGMTRIQSA EPVWILFVLT LYSSVLMQVK PQLWSVGIER KKLFGETNTS VHCDEIRGLS
RNQRSLCRTY NDHMYYVESG SKQGVEECQW QFRGQRWNCS LASNASPDKI IAVGSKETAF
TYAITSGGVV QSIARACKSG NLMACGCSKR ERPTGLGKDW NWGGCGDDID YAYGFAHEFI
DAQERDNSSP NDRRVKSHKA MNIHNNEAGR LSVVRASHTT CKCHGVSGSC SIKTCWLQTP
QFRTIGDKLR QRYDDALEMR VTHRGQMKTR FSSDRNPSNI DLVYIDSSPD YCKVNHKLGI
LGTSGRECQL DSLAMDGCGL MCCGRGYTTK MVEVVKSCNC KFQWCCFVKC QQCKEKVLKH
ICN