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Protein Wnt-5a

 WNT5A_RAT               Reviewed;         380 AA.
Q9QXQ7; Q5PY99;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 2.
23-MAY-2018, entry version 116.
RecName: Full=Protein Wnt-5a;
Flags: Precursor;
Name=Wnt5a; Synonyms=Wnt-5a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
PubMed=15309358; DOI=10.1007/s00221-004-1887-0;
Peters S., Mix E., Bauer P., Weinelt S., Schubert B., Knoblich R.,
Boettcher T., Strauss U., Pahnke J., Cattaneo E., Wree A., Rolfs A.;
"Wnt-5a expression in the rat neuronal progenitor cell line ST14A.";
Exp. Brain Res. 158:189-195(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Corpus luteum;
Lacher M.D., Walther P.R., Lareu R.R., Dharmarajan A.M., Friis R.R.;
"Coexpression of Wnt-5a, Wnt-4, frizzled-4, and DDC4 (frpAP, a
secreted Frizzled, AF012891) in the pregnant ovary.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Ligand for members of the frizzled family of seven
transmembrane receptors. Can activate or inhibit canonical Wnt
signaling, depending on receptor context. In the presence of FZD4,
activates beta-catenin signaling. In the presence of ROR2,
inhibits the canonical Wnt pathway by promoting beta-catenin
degradation through a GSK3-independent pathway which involves
down-regulation of beta-catenin-induced reporter gene expression
(By similarity). Suppression of the canonical pathway allows
chondrogenesis to occur and inhibits tumor formation. Stimulates
cell migration. Decreases proliferation, migration, invasiveness
and clonogenicity of carcinoma cells and may act as a tumor
suppressor. Mediates motility of melanoma cells (By similarity).
Required during embryogenesis for extension of the primary
anterior-posterior axis and for outgrowth of limbs and the genital
tubercle. Inhibits type II collagen expression in chondrocytes (By
similarity). {ECO:0000250|UniProtKB:P22725,
ECO:0000250|UniProtKB:P41221, ECO:0000250|UniProtKB:Q27Q52}.
-!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
oligomerization and is required for prolonged biological activity.
The complex with AFM may represent the physiological form in body
fluids (By similarity). Homooligomer; disulfide-linked, leading to
inactivation. Interacts with PORCN. Interacts with WLS (By
similarity). {ECO:0000250|UniProtKB:P22725,
ECO:0000250|UniProtKB:P41221}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250|UniProtKB:P41221}. Secreted
{ECO:0000250|UniProtKB:P41221}.
-!- PTM: Glycosylation is necessary for secretion but not for
activity. {ECO:0000250|UniProtKB:P22725}.
-!- PTM: Palmitoleoylation is required for efficient binding to
frizzled receptors. Depalmitoleoylation leads to Wnt signaling
pathway inhibition. {ECO:0000250|UniProtKB:P27467,
ECO:0000250|UniProtKB:P56704}.
-!- PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation
and formation of large disulfide-bond oligomers, leading to
inactivation of WNT5A. {ECO:0000250|UniProtKB:P22725}.
-!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY819646; AAV69750.1; -; mRNA.
EMBL; AF188333; AAF15588.1; -; mRNA.
UniGene; Rn.48749; -.
SMR; Q9QXQ7; -.
STRING; 10116.ENSRNOP00000021164; -.
PaxDb; Q9QXQ7; -.
PRIDE; Q9QXQ7; -.
UCSC; RGD:69250; rat.
RGD; 69250; Wnt5a.
eggNOG; KOG3913; Eukaryota.
eggNOG; ENOG410XQZ1; LUCA.
HOGENOM; HOG000039529; -.
HOVERGEN; HBG001595; -.
InParanoid; Q9QXQ7; -.
PhylomeDB; Q9QXQ7; -.
PRO; PR:Q9QXQ7; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEP:RGD.
GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
GO; GO:0044849; P:estrous cycle; IEP:RGD.
GO; GO:0048286; P:lung alveolus development; IEP:RGD.
GO; GO:0030182; P:neuron differentiation; IEP:RGD.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:RGD.
GO; GO:0150012; P:positive regulation of neuron projection arborization; IGI:ARUK-UCL.
GO; GO:0030850; P:prostate gland development; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0033574; P:response to testosterone; IEP:RGD.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:MGI.
InterPro; IPR005817; Wnt.
InterPro; IPR026538; Wnt5a.
InterPro; IPR018161; Wnt_CS.
PANTHER; PTHR12027; PTHR12027; 1.
PANTHER; PTHR12027:SF33; PTHR12027:SF33; 1.
Pfam; PF00110; wnt; 1.
PRINTS; PR01349; WNTPROTEIN.
SMART; SM00097; WNT1; 1.
PROSITE; PS00246; WNT1; 1.
2: Evidence at transcript level;
Chondrogenesis; Complete proteome; Developmental protein;
Differentiation; Disulfide bond; Extracellular matrix; Glycoprotein;
Lipoprotein; Reference proteome; Secreted; Signal;
Wnt signaling pathway.
SIGNAL 1 37 {ECO:0000255}.
PROPEP 38 61 {ECO:0000250}.
/FTId=PRO_0000352798.
CHAIN 62 380 Protein Wnt-5a.
/FTId=PRO_0000041429.
LIPID 244 244 O-palmitoleoyl serine; by PORCN.
{ECO:0000250|UniProtKB:P56704}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 326 326 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 104 115 {ECO:0000250|UniProtKB:P28026}.
DISULFID 154 162 {ECO:0000250|UniProtKB:P28026}.
DISULFID 164 182 {ECO:0000250|UniProtKB:P28026}.
DISULFID 238 252 {ECO:0000250|UniProtKB:P28026}.
DISULFID 240 247 {ECO:0000250|UniProtKB:P28026}.
DISULFID 325 340 {ECO:0000250|UniProtKB:P28026}.
DISULFID 355 370 {ECO:0000250|UniProtKB:P28026}.
DISULFID 357 367 {ECO:0000250|UniProtKB:P28026}.
DISULFID 362 363 {ECO:0000250|UniProtKB:P28026}.
CONFLICT 42 42 E -> K (in Ref. 2; AAF15588).
{ECO:0000305}.
CONFLICT 50 50 G -> S (in Ref. 2; AAF15588).
{ECO:0000305}.
CONFLICT 61 61 H -> Y (in Ref. 2; AAF15588).
{ECO:0000305}.
CONFLICT 168 168 Missing (in Ref. 2; AAF15588).
{ECO:0000305}.
SEQUENCE 380 AA; 42283 MW; 9716401010072224 CRC64;
MKKPIGILSP GVALGTAGGA MSSKFFLMAL ATFFSFAQVV IEANSWWSLG MNNPVQMSEV
HIIGAQPLCS QLAGLSQGQK KLCHLYQDHM QYIGEGAKTG IKECQYQFRH RRWNCSTVDN
TSVFGRVMQI GSRETAFTYA VSAAGVVNAM SRACREGELS TCGCSRAARP KDLPRDWLWG
GCGDNIDYGY RFAKEFVDAR ERERIHAKGS YESARILMNL HNNEAGRRTV YNLADVACKC
HGVSGSCSLK TCWLQLADFR KVGDALKEKY DSAAAMRLNS RGKLVQVNSR FNSPTTQDLV
YIDPSPDYCV RNESTGSLGT QGRLCNKTSE GMDGCELMCC GRGYDQFKTV QTERCHCKFH
WCCYVKCKKC TEIVDQFVCK


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