ID   WNT16_BOVIN             Reviewed;         362 AA.
AC   Q5E9U6; Q0VD20;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Protein Wnt-16;
DE   Flags: Precursor;
GN   Name=WNT16;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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 {ECO:0000250}.
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; BT020824; AAX08841.1; -; mRNA.
DR   EMBL; BC119880; AAI19881.1; -; mRNA.
DR   RefSeq; NP_001014949.1; NM_001014949.1.
DR   AlphaFoldDB; Q5E9U6; -.
DR   SMR; Q5E9U6; -.
DR   STRING; 9913.ENSBTAP00000003825; -.
DR   PaxDb; Q5E9U6; -.
DR   GeneID; 538627; -.
DR   KEGG; bta:538627; -.
DR   CTD; 51384; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   HOGENOM; CLU_033039_1_0_1; -.
DR   InParanoid; Q5E9U6; -.
DR   OrthoDB; 745245at2759; -.
DR   TreeFam; TF105310; -.
DR   Proteomes; UP000009136; Unplaced.
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; IPR013304; Wnt16.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01895; WNT16PROTEIN.
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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..362
FT                   /note="Protein Wnt-16"
FT                   /id="PRO_0000248068"
FT   LIPID           224
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..92
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        136..144
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        146..165
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        218..232
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        220..227
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        291..322
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        307..317
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        321..361
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        337..352
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        339..349
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        344..345
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   CONFLICT        156
FT                   /note="S -> A (in Ref. 2; AAI19881)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   362 AA;  40440 MW;  24CD4FF27C664062 CRC64;
     MDRAALLGLS RLCALWAAVL ALFPCGAQGN WMWLGIASFG VPEKLGCANL PLNSRQKELC
     KRKPYLLPSI REGARLGIQE CRSQFRHERW NCLVAAASAP GTSPLFGYEL SSGTKETAFI
     YAVMAAGLVH SVTRSCSAGN MTECSCDTTL QNGGSSSEGW HWGGCSDDVQ YGMWFSRKFL
     DFPIKNTTAK ESKVLLAMNL HNNEAGRQAV AKLMSLDCRC HGVSGSCAVK TCWKTMSSFE
     KIGHLLKDKY ENSVQISDKI KRKMHRREKD QRKIPIRKDD LLYVNKSPNY CVEDKKLGIP
     GTQGRECNRT SEGADGCNLL CCGRGYNTHV VRHVERCECK FIWCCYVRCR RCESMTDVHT
     CK