WNT1_CHICK
ID WNT1_CHICK Reviewed; 368 AA.
AC Q91029; Q3L258; Q5QEB6; Q9PS91;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein Wnt-1;
DE Flags: Precursor;
GN Name=WNT1; Synonyms=WNT-1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-165.
RC STRAIN=White leghorn; TISSUE=Embryo;
RX PubMed=7821210; DOI=10.1242/dev.120.12.3379;
RA Bally-Cuif L., Wassef M.;
RT "Ectopic induction and reorganization of Wnt-1 expression in quail/chick
RT chimeras.";
RL Development 120:3379-3394(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-306.
RA Jensen J.L., Goode R.R., McClellan D.A., Stark M.R.;
RT "Phylogenetic analysis of the developmental gene wnt-1 suggests an
RT additional gene duplication event predating the evolution of Chordates.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-159.
RX PubMed=7577679; DOI=10.1016/0925-4773(95)00385-e;
RA Hollyday M., McMahon J.A., McMahon A.P.;
RT "Wnt expression patterns in chick embryo nervous system.";
RL Mech. Dev. 52:9-25(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-361.
RX PubMed=16258938; DOI=10.1002/dvdy.20621;
RA Fokina V.M., Frolova E.I.;
RT "Expression patterns of Wnt genes during development of an anterior part of
RT the chicken eye.";
RL Dev. Dyn. 235:496-505(2006).
RN [6]
RP PRELIMINARY CYSTEINE PALMITOYLATION, PALMITOLEOYLATION AT SER-222, AND
RP MUTAGENESIS OF CYS-91 AND SER-222.
RX PubMed=22046319; DOI=10.1371/journal.pone.0026636;
RA Galli L.M., Burrus L.W.;
RT "Differential palmit(e)oylation of Wnt1 on C93 and S224 residues has
RT overlapping and distinct consequences.";
RL PLoS ONE 6:E26636-E26636(2011).
RN [7]
RP FUNCTION, PALMITOLEOYLATION AT SER-222, INTERACTION WITH PORCN, MUTAGENESIS
RP OF SER-222, AND GLYCOSYLATION.
RX PubMed=25451226; DOI=10.1016/j.febslet.2014.11.016;
RA Miranda M., Galli L.M., Enriquez M., Szabo L.A., Gao X., Hannoush R.N.,
RA Burrus L.W.;
RT "Identification of the WNT1 residues required for palmitoylation by
RT Porcupine.";
RL FEBS Lett. 588:4815-4824(2014).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (Probable). Acts in the canonical Wnt signaling
CC pathway by promoting beta-catenin-dependent transcriptional activation
CC (PubMed:25451226). Developmental protein that promotes cell
CC proliferation in the developing spinal cord (PubMed:25451226). Has a
CC role in osteoblast function, bone development and bone homeostasis (By
CC similarity). {ECO:0000250|UniProtKB:P04628,
CC ECO:0000269|PubMed:25451226, ECO:0000305}.
CC -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC oligomerization and is required for prolonged biological activity. The
CC complex with AFM may represent the physiological form in body fluids
CC (By similarity). Interacts with PORCN (PubMed:25451226).
CC {ECO:0000250|UniProtKB:P04628, ECO:0000305|PubMed:25451226}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P04628}. Secreted
CC {ECO:0000250|UniProtKB:P04628}.
CC -!- DEVELOPMENTAL STAGE: Expression in the met-mesencephalic region.
CC -!- PTM: N-glycosylated. N-glycosylation favors subsequent
CC palmitoleoylation. {ECO:0000269|PubMed:25451226}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors. Palmitoleoylation is necessary for proper trafficking to
CC cell surface (Probable). Depalmitoleoylated by NOTUM, leading to
CC inhibit Wnt signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:P56704, ECO:0000305|PubMed:22046319,
CC ECO:0000305|PubMed:25451226}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC -!- CAUTION: A palmitoylation site was proposed at Cys-91, but it was later
CC shown that this cysteine is engaged in a disulfide bond.
CC {ECO:0000269|PubMed:22046319}.
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DR EMBL; KQ759375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X81693; CAA57341.1; -; mRNA.
DR EMBL; AY655699; AAV67340.1; -; mRNA.
DR EMBL; AY753286; AAW81988.1; -; mRNA.
DR PIR; I50729; I50729.
DR RefSeq; XP_015128668.1; XM_015273182.1.
DR AlphaFoldDB; Q91029; -.
DR SMR; Q91029; -.
DR IntAct; Q91029; 1.
DR GeneID; 396160; -.
DR KEGG; gga:396160; -.
DR CTD; 7471; -.
DR VEuPathDB; HostDB:geneid_396160; -.
DR InParanoid; Q91029; -.
DR OrthoDB; 624528at2759; -.
DR PRO; PR:Q91029; -.
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:0006915; P:apoptotic process; TAS:AgBase.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
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:0048263; P:determination of dorsal identity; TAS:AgBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; TAS:AgBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009139; Wnt1.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01841; WNT1PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Lipoprotein;
KW Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..368
FT /note="Protein Wnt-1"
FT /id="PRO_0000200601"
FT LIPID 222
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000269|PubMed:25451226,
FT ECO:0000305|PubMed:22046319"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 141..149
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 151..168
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 216..230
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 218..225
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 297..328
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 313..323
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 327..367
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 343..358
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 345..355
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 350..351
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT MUTAGEN 91
FT /note="C->A: Accumulates in the ER."
FT /evidence="ECO:0000269|PubMed:22046319"
FT MUTAGEN 222
FT /note="S->A: Accumulates in the ER. Loss of
FT palmitoleoylation."
FT /evidence="ECO:0000269|PubMed:22046319,
FT ECO:0000269|PubMed:25451226"
FT MUTAGEN 222
FT /note="S->C: Loss of palmitoleoylation by PRCN."
FT /evidence="ECO:0000269|PubMed:25451226"
FT MUTAGEN 222
FT /note="S->T: Decreases palmitoleoylation by PRCN. No effect
FT on the activation of the canonical Wnt signaling pathway."
FT /evidence="ECO:0000269|PubMed:25451226"
FT CONFLICT 36
FT /note="I -> V (in Ref. 2; CAA57341 and 3; AAV67340)"
FT CONFLICT 225
FT /note="C -> R (in Ref. 5; AAW81988)"
SQ SEQUENCE 368 AA; 40797 MW; F1D7A6C5EFB44C2B CRC64;
MRGPALLLAL RALCALSALR GTARAVNNSG RWWGIINVAS STNLLTDSGS VQLVLEPGLQ
LLSRKQRRLI RQNPGILHSV SAGLQSAVRE CQWQFRNRRW NCPTSQGPNI FGKIVNRGCR
ETAFIFAITS AGVTHSVARS CSEGSIESCT CDYRRRGPGG PDWHWGGCSD NIDFGRLFGR
EFVDSSEKGR DLRFLMNLHN NEAGRMTVFS EMRQECKCHG MSGSCTVRTC WMRLPTFRAV
GDVLKDRFDG ASRVIYGNKG SNRASRVELH HLEPENPAHK PPSPHDLVYF EKSPNFCTYS
GKMGTAGTAG RACNSSSPGL DGCELLCCGR GFRTRTQRVT ERCNCTFHWC CHVSCLNCTN
TQVLHECL
