WNT9A_CHICK
ID WNT9A_CHICK Reviewed; 354 AA.
AC O42280;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein Wnt-9a;
DE AltName: Full=Wnt-14 {ECO:0000303|PubMed:9441749};
DE Flags: Precursor;
GN Name=WNT9A; Synonyms=WNT14 {ECO:0000303|PubMed:9441749};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9441749; DOI=10.1006/geno.1997.5041;
RA Bergstein I., Eisenberg L.M., Bhalerao J., Jenkins N.A., Copeland N.G.,
RA Osborne M.P., Bowcock A.M., Brown A.M.C.;
RT "Isolation of two novel WNT genes, WNT14 and WNT15, one of which (WNT15) is
RT closely linked to WNT3 on human chromosome 17q21.";
RL Genomics 46:450-458(1997).
RN [2]
RP FUNCTION.
RX PubMed=16818445; DOI=10.1242/dev.02471;
RA Spaeter D., Hill T.P., O'sullivan R.J., Gruber M., Conner D.A.,
RA Hartmann C.;
RT "Wnt9a signaling is required for joint integrity and regulation of Ihh
RT during chondrogenesis.";
RL Development 133:3039-3049(2006).
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:16818445). Plays a role in
CC embryonic chondrocyte maturation and in embryonic bone mineralization
CC (By similarity). {ECO:0000250|UniProtKB:Q8R5M2,
CC ECO:0000269|PubMed:16818445, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:O14904}. Secreted
CC {ECO:0000250|UniProtKB:O14904}.
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; AF031168; AAC41248.1; -; mRNA.
DR AlphaFoldDB; O42280; -.
DR SMR; O42280; -.
DR STRING; 9031.ENSGALP00000008661; -.
DR PaxDb; O42280; -.
DR VEuPathDB; HostDB:geneid_395829; -.
DR eggNOG; KOG3913; Eukaryota.
DR InParanoid; O42280; -.
DR PhylomeDB; O42280; -.
DR Proteomes; UP000000539; Unplaced.
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:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0061303; P:cornea development in camera-type eye; IEP:BHF-UCL.
DR GO; GO:0072498; P:embryonic skeletal joint development; IMP:BHF-UCL.
DR GO; GO:0061072; P:iris morphogenesis; IEP:BHF-UCL.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:1902764; P:positive regulation of embryonic skeletal joint development; TAS:AgBase.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR013303; Wnt9a.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF75; PTHR12027:SF75; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01894; WNT14PROTEIN.
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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..354
FT /note="Protein Wnt-9a"
FT /id="PRO_0000041457"
FT REGION 246..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 213
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..96
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 133..141
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 143..160
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 207..221
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 209..216
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 288..313
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 302..308
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 312..352
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 328..343
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 330..340
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 335..336
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 354 AA; 39814 MW; 044BB0539CFD8669 CRC64;
MALLRALLGL LACTPRPSAA YFGLTGNEAL TILPLTSEME EAAVKAHYKV CDRLKLEKKQ
RRMCRRDPGG AETLMEAISM SALECQYQFR FERWNCTLEG RYRASLLKRG FKETAFLYAI
SSAGLTHAMA KACSAGRMER CTCDEAPDLE NREAWQWGGC GDNLKYSNKF VKEFLGRKPN
KDLRARVDFH NNLVGMKVIK AGVETTCKCH GVSGSCTVRT CWRQLSPFHE IGKQLKQKYE
TSLKVGSTTN EATGEGDISP PKKSIPGHSD QIPRTTDLVY IDDSPSFCLM SRYSPGTSGR
KCYKDKNCDS ICCGRGHNTQ SRVVTRPCQC QVRWCCYVEC KQCTQREEVY TCKD
