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W11B1_XENTR
ID   W11B1_XENTR             Reviewed;         353 AA.
AC   Q66II0;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Protein Wnt-11b-1 {ECO:0000303|PubMed:17436276};
DE   Flags: Precursor;
GN   Name=wnt11b-1 {ECO:0000303|PubMed:17436276};
GN   Synonyms=wnt11 {ECO:0000312|EMBL:AAH81341.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAH81341.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula {ECO:0000312|EMBL:AAH81341.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NOMENCLATURE.
RX   PubMed=17436276; DOI=10.1002/dvdy.21156;
RA   Garriock R.J., Warkman A.S., Meadows S.M., D'Agostino S., Krieg P.A.;
RT   "Census of vertebrate Wnt genes: isolation and developmental expression of
RT   Xenopus Wnt2, Wnt3, Wnt9a, Wnt9b, Wnt10a, and Wnt16.";
RL   Dev. Dyn. 236:1249-1258(2007).
CC   -!- FUNCTION: Ligand for the frizzled7 transmembrane receptor. Primarily
CC       acts via non-canonical Wnt pathways mediated by either Ca(2+) and PKC,
CC       or by JNK and dvl2/dsh. Depending on the cellular context, can also
CC       signal via the canonical Wnt pathway mediated by beta-catenin and
CC       dvl2/dsh. May also inhibit canonical Wnt signaling. Maternally
CC       initiates dorsal/ventral axis formation by a canonical route, which
CC       signals via lrp6. In a complex with wnt5a, activates the canonical and
CC       non-canonical processes involved in axis formation. In the non-
CC       canonical pathway, acts through fzd7/fz7 to induce phosphorylation of
CC       dvl2/dsh. Signals through a non-canonical Wnt pathway to regulate
CC       convergent extension movements during gastrulation. Interactions with
CC       the secreted Wnt antagonist sfrp5 to coordinate foregut development,
CC       acting via a non-canonical wnt pathway whereby sfrp5 restricts wnt11b
CC       activity to prevent inappropriate foregut formation. Mediates
CC       cardiogenesis via non-canonical Wnt signaling involving JNK-activation
CC       and PKC. Acts redundantly with wnt11/wnt11r during pronephros induction
CC       (By similarity). {ECO:0000250|UniProtKB:P49893}.
CC   -!- SUBUNIT: Homodimer. Secreted homodimers form a complex with wnt5a
CC       homodimers; tyrosine sulfation of both wnt11 and wnt5a by tpst1 is
CC       required for this interaction. Interacts with the transmembrane
CC       receptor fzd7/fz7. Interacts with lrp6 and ryk. Interacts with
CC       tdgf1/frl1. Interacts weakly with frzb1 and strongly with
CC       frzb2/crescent. Interaction with frzb2/crescent antagonizes wnt11
CC       function in the neuroectoderm, but enhances it in mesodermal tissue (By
CC       similarity). {ECO:0000250|UniProtKB:P49893}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P49893}.
CC   -!- PTM: Glycosylation is required for protein secretion.
CC       {ECO:0000250|UniProtKB:P49893}.
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   -!- MISCELLANEOUS: Xenopus and other lower vertebrates contain duplicated
CC       wnt11 genes (wnt11 and wnt11b) resulting from an ancient gene
CC       duplication event, but the second copy has since been lost in mammals.
CC       In addition, X.tropicalis has two very similar wnt11b genes suggesting
CC       a further recent duplication event.
CC   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000255}.
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DR   EMBL; BC081341; AAH81341.1; -; mRNA.
DR   RefSeq; NP_001008133.1; NM_001008132.1.
DR   AlphaFoldDB; Q66II0; -.
DR   SMR; Q66II0; -.
DR   DNASU; 493495; -.
DR   GeneID; 493495; -.
DR   KEGG; xtr:493495; -.
DR   InParanoid; Q66II0; -.
DR   OrthoDB; 797177at2759; -.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000038741; Expressed in gastrula and 6 other tissues.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Gastrulation;
KW   Glycoprotein; Lipoprotein; Reference proteome; Secreted; Signal; Sulfation;
KW   Wnt signaling pathway.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..353
FT                   /note="Protein Wnt-11b-1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000397208"
FT   MOD_RES         274
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P49893"
FT   MOD_RES         281
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P49893"
FT   LIPID           214
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        78..89
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        128..136
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        138..155
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        208..222
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        210..217
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        282..313
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        298..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   353 AA;  38627 MW;  BD62EABFD1F649A9 CRC64;
     MAQIHHCVTL LLILCCSGLC GAIQWLGLTV NGSRVAWNES GHCRLLDGLV PEQSQLCKRN
     LELMQSVVNA AKQAKLTCQM TFSDMRWNCS SVENAPNFTP DLSKGTRESA FVYALASATL
     SHTIARACAS GELPTCSCGA TPAEVPGTGF RWGGCGDNLH YGLNMGSAFV DAPMKSSKSG
     GTQATKMINL HNNAVGRQVL MDSLETKCKC HGVSGSCSVK TCWKGLQDLP HIANELKSKY
     LGATKVIHRQ TGTRRQLVPR ELDIRPVRES ELVYLVSSPD YCAKNPKLGS YGTQDRVCNK
     TSVGSDSCNL MCCGRGYNAY TETIVERCQC KYYYCCYVVC KKCERTVERY VCK
 
 
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