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WNT7B_MOUSE
ID   WNT7B_MOUSE             Reviewed;         349 AA.
AC   P28047; Q80US5;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Protein Wnt-7b;
DE   Flags: Precursor;
GN   Name=Wnt7b; Synonyms=Wnt-7b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2279700; DOI=10.1101/gad.4.12b.2319;
RA   Gavin B.J., McMahon J.A., McMahon A.P.;
RT   "Expression of multiple novel Wnt-1/int-1-related genes during fetal and
RT   adult mouse development.";
RL   Genes Dev. 4:2319-2332(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH PORCN.
RX   PubMed=10866835; DOI=10.1046/j.1432-1033.2000.01478.x;
RA   Tanaka K., Okabayashi H., Asashima M., Perrimon N., Kadowaki T.;
RT   "The evolutionarily conserved porcupine gene family is involved in the
RT   processing of the Wnt family.";
RL   Eur. J. Biochem. 267:4300-4311(2000).
RN   [4]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=11543617; DOI=10.1006/dbio.2001.0373;
RA   Parr B.A., Cornish V.A., Cybulsky M.I., McMahon A.P.;
RT   "Wnt7b regulates placental development in mice.";
RL   Dev. Biol. 237:324-332(2001).
RN   [5]
RP   FUNCTION, INTERACTION WITH FZD1; FZD4 AND FZD10, AND SUBCELLULAR LOCATION.
RX   PubMed=15923619; DOI=10.1128/mcb.25.12.5022-5030.2005;
RA   Wang Z., Shu W., Lu M.M., Morrisey E.E.;
RT   "Wnt7b activates canonical signaling in epithelial and vascular smooth
RT   muscle cells through interactions with Fzd1, Fzd10, and LRP5.";
RL   Mol. Cell. Biol. 25:5022-5030(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=28803732; DOI=10.1016/j.neuron.2017.07.031;
RA   Cho C., Smallwood P.M., Nathans J.;
RT   "Reck and Gpr124 Are Essential Receptor Cofactors for Wnt7a/Wnt7b-specific
RT   signaling in mammalian CNS angiogenesis and blood-brain barrier
RT   regulation.";
RL   Neuron 95:1056-1073(2017).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors that functions in the canonical Wnt/beta-
CC       catenin signaling pathway (PubMed:15923619, PubMed:28803732). Required
CC       for normal fusion of the chorion and the allantois during placenta
CC       development (PubMed:11543617). Required for central nervous system
CC       (CNS) angiogenesis and blood-brain barrier regulation
CC       (PubMed:28803732). {ECO:0000269|PubMed:11543617,
CC       ECO:0000269|PubMed:15923619, ECO:0000269|PubMed:28803732}.
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 FZD1 and FZD10 (PubMed:15923619).
CC       Interacts with FZD4 (in vitro) (PubMed:15923619). Interacts with PORCN
CC       (PubMed:10866835). Interacts with glypican GPC3 (By similarity).
CC       Interacts (via intrinsically disordered linker region) with RECK;
CC       interaction with RECK confers ligand selectivity for Wnt7 in brain
CC       endothelial cells and allows these cells to selectively respond to Wnt7
CC       (By similarity). {ECO:0000250|UniProtKB:P56706,
CC       ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:15923619}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P56706}. Secreted
CC       {ECO:0000269|PubMed:15923619}.
CC   -!- DEVELOPMENTAL STAGE: At 7.5 and 8.5 dpc, detected in extraembryonic
CC       membranes and cells that form the chorionic plate.
CC       {ECO:0000269|PubMed:11543617}.
CC   -!- DOMAIN: The intrinsically disordered linker region is required for
CC       recognition by RECK in brain endothelial cells.
CC       {ECO:0000250|UniProtKB:P56706}.
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; M89802; AAA40571.1; -; mRNA.
DR   EMBL; BC052018; AAH52018.2; -; mRNA.
DR   CCDS; CCDS37171.1; -.
DR   PIR; H36470; H36470.
DR   RefSeq; NP_001157105.1; NM_001163633.1.
DR   RefSeq; NP_001157106.1; NM_001163634.1.
DR   RefSeq; NP_033554.3; NM_009528.3.
DR   AlphaFoldDB; P28047; -.
DR   SMR; P28047; -.
DR   BioGRID; 204581; 7.
DR   IntAct; P28047; 1.
DR   STRING; 10090.ENSMUSP00000105051; -.
DR   GlyGen; P28047; 3 sites.
DR   iPTMnet; P28047; -.
DR   PhosphoSitePlus; P28047; -.
DR   MaxQB; P28047; -.
DR   PaxDb; P28047; -.
DR   PRIDE; P28047; -.
DR   ProteomicsDB; 297561; -.
DR   Antibodypedia; 27975; 102 antibodies from 22 providers.
DR   DNASU; 22422; -.
DR   Ensembl; ENSMUST00000109424; ENSMUSP00000105051; ENSMUSG00000022382.
DR   GeneID; 22422; -.
DR   KEGG; mmu:22422; -.
DR   UCSC; uc007xdf.2; mouse.
DR   CTD; 7477; -.
DR   MGI; MGI:98962; Wnt7b.
DR   VEuPathDB; HostDB:ENSMUSG00000022382; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000158861; -.
DR   InParanoid; P28047; -.
DR   OMA; NSCSERT; -.
DR   OrthoDB; 745245at2759; -.
DR   PhylomeDB; P28047; -.
DR   Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR   BioGRID-ORCS; 22422; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Wnt7b; mouse.
DR   PRO; PR:P28047; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P28047; protein.
DR   Bgee; ENSMUSG00000022382; Expressed in cortical plate and 241 other tissues.
DR   ExpressionAtlas; P28047; baseline and differential.
DR   Genevisible; P28047; MM.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:1902379; F:chemoattractant activity involved in axon guidance; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0005109; F:frizzled binding; IPI:MGI.
DR   GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR   GO; GO:0060033; P:anatomical structure regression; IMP:MGI.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0021846; P:cell proliferation in forebrain; IDA:BHF-UCL.
DR   GO; GO:0022009; P:central nervous system vasculogenesis; IGI:MGI.
DR   GO; GO:0036516; P:chemoattraction of dopaminergic neuron axon; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
DR   GO; GO:0060560; P:developmental growth involved in morphogenesis; IMP:MGI.
DR   GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR   GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
DR   GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:MGI.
DR   GO; GO:0021871; P:forebrain regionalization; IEP:UniProtKB.
DR   GO; GO:0042592; P:homeostatic process; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0072061; P:inner medullary collecting duct development; IMP:MGI.
DR   GO; GO:0060482; P:lobar bronchus development; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0060428; P:lung epithelium development; IMP:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR   GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
DR   GO; GO:0072205; P:metanephric collecting duct development; IMP:MGI.
DR   GO; GO:0072207; P:metanephric epithelium development; IMP:MGI.
DR   GO; GO:0072236; P:metanephric loop of Henle development; IMP:MGI.
DR   GO; GO:0003338; P:metanephros morphogenesis; IMP:MGI.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IDA:BHF-UCL.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
DR   GO; GO:0072060; P:outer medullary collecting duct development; IMP:MGI.
DR   GO; GO:0032364; P:oxygen homeostasis; IMP:MGI.
DR   GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
DR   GO; GO:0032536; P:regulation of cell projection size; ISO:MGI.
DR   GO; GO:0072053; P:renal inner medulla development; IMP:MGI.
DR   GO; GO:0072054; P:renal outer medulla development; IMP:MGI.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
DR   GO; GO:0048864; P:stem cell development; IDA:BHF-UCL.
DR   GO; GO:0050808; P:synapse organization; IGI:MGI.
DR   GO; GO:0060535; P:trachea cartilage morphogenesis; IMP:MGI.
DR   GO; GO:0001944; P:vasculature development; IMP:MGI.
DR   GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR013300; Wnt7.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01891; WNT7PROTEIN.
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; Glycoprotein;
KW   Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..349
FT                   /note="Protein Wnt-7b"
FT                   /id="PRO_0000041445"
FT   REGION          238..266
FT                   /note="Disordered linker"
FT                   /evidence="ECO:0000250|UniProtKB:P56706"
FT   LIPID           206
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        73..84
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        123..131
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        133..152
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        200..214
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        202..209
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        278..309
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        294..304
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        308..348
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        324..339
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        326..336
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        331..332
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   CONFLICT        33
FT                   /note="G -> V (in Ref. 2; AAH52018)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   349 AA;  39302 MW;  BDD82AB020DC680E CRC64;
     MHRNFRKWIF YVFLCFGVLY VKLGALSSVV ALGANIICNK IPGLAPRQRA ICQSRPDAII
     VIGEGAQMGI DECQHQFRFG RWNCSALGEK TVFGQELRVG SREAAFTYAI TAAGVAHAVT
     AACSQGNLSN CGCDREKQGY YNQAEGWKWG GCSADVRYGI DFSRRFVDAR EIKKNARRLM
     NLHNNEAGRK VLEDRMKLEC KCHGVSGSCT TKTCWTTLPK FREVGHLLKE KYNAAVQVEV
     VRASRLRQPT FLRIKQLRSY QKPMETDLVY IEKSPNYCEE DAATGSVGTQ GRLCNRTSPG
     ADGCDTMCCG RGYNTHQYTK VWQCNCKFHW CCFVKCNTCS ERTEVFTCK
 
 
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