WNT7B_HUMAN
ID WNT7B_HUMAN Reviewed; 349 AA.
AC P56706; B8A596; Q96Q12;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein Wnt-7b;
DE Flags: Precursor;
GN Name=WNT7B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11562755; DOI=10.3892/ijo.19.4.779;
RA Kirikoshi H., Sekihara H., Katoh M.;
RT "Molecular cloning and characterization of human WNT7B.";
RL Int. J. Oncol. 19:779-783(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim N.-S., Kim J.-M., Oh J.-H., Sohn H.-Y., Hahn Y., Kim Y.S.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 204-327.
RC TISSUE=Mammary gland;
RX PubMed=8168088;
RA Huguet E.L., McMahon J.A., McMahon A.P., Bicknell R., Harris A.L.;
RT "Differential expression of human Wnt genes 2, 3, 4, and 7B in human breast
RT cell lines and normal and disease states of human breast tissue.";
RL Cancer Res. 54:2615-2621(1994).
RN [6]
RP INTERACTION WITH GPC3.
RX PubMed=16227623; DOI=10.1074/jbc.m507004200;
RA Capurro M.I., Shi W., Sandal S., Filmus J.;
RT "Processing by convertases is not required for glypican-3-induced
RT stimulation of hepatocellular carcinoma growth.";
RL J. Biol. Chem. 280:41201-41206(2005).
RN [7]
RP INTERACTION WITH AFM, AND SUBCELLULAR LOCATION.
RX PubMed=26902720; DOI=10.7554/elife.11621;
RA Mihara E., Hirai H., Yamamoto H., Tamura-Kawakami K., Matano M.,
RA Kikuchi A., Sato T., Takagi J.;
RT "Active and water-soluble form of lipidated Wnt protein is maintained by a
RT serum glycoprotein afamin/alpha-albumin.";
RL Elife 5:0-0(2016).
RN [8]
RP FUNCTION, INTERACTION WITH RECK, AND DOMAIN.
RX PubMed=30026314; DOI=10.1126/science.aat1178;
RA Eubelen M., Bostaille N., Cabochette P., Gauquier A., Tebabi P.,
RA Dumitru A.C., Koehler M., Gut P., Alsteens D., Stainier D.Y.R.,
RA Garcia-Pino A., Vanhollebeke B.;
RT "A molecular mechanism for Wnt ligand-specific signaling.";
RL Science 361:0-0(2018).
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:30026314). Required for normal fusion
CC of the chorion and the allantois during placenta development (By
CC similarity). Required for central nervous system (CNS) angiogenesis and
CC blood-brain barrier regulation (PubMed:30026314).
CC {ECO:0000250|UniProtKB:P28047, ECO:0000269|PubMed:30026314}.
CC -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC oligomerization and is required for prolonged biological activity
CC (PubMed:16227623). The complex with AFM may represent the physiological
CC form in body fluids (PubMed:26902720). Interacts with FZD1 and FZD10.
CC Interacts with FZD4 (in vitro). Interacts with PORCN (By similarity).
CC Interacts with glypican GPC3 (PubMed:16227623). Interacts (via
CC intrinsically disordered linker region) with RECK; interaction with
CC RECK confers ligand selectivity for Wnt7 in brain endothelial cells and
CC allows these cells to selectively respond to Wnt7 (PubMed:30026314).
CC {ECO:0000250|UniProtKB:P28047, ECO:0000269|PubMed:16227623,
CC ECO:0000269|PubMed:26902720, ECO:0000269|PubMed:30026314}.
CC -!- INTERACTION:
CC P56706; Q9Z0J1: Reck; Xeno; NbExp=4; IntAct=EBI-3913589, EBI-20720091;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
CC -!- TISSUE SPECIFICITY: Moderately expressed in fetal brain, weakly
CC expressed in fetal lung and kidney, and faintly expressed in adult
CC brain, lung and prostate.
CC -!- DOMAIN: The intrinsically disordered linker region is required for
CC recognition by RECK in brain endothelial cells.
CC {ECO:0000269|PubMed:30026314}.
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; AB062766; BAB68399.1; -; mRNA.
DR EMBL; AF416743; AAN32640.1; -; mRNA.
DR EMBL; BX511035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR536603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034923; AAH34923.1; -; mRNA.
DR CCDS; CCDS33667.1; -.
DR RefSeq; NP_478679.1; NM_058238.2.
DR AlphaFoldDB; P56706; -.
DR SMR; P56706; -.
DR BioGRID; 113314; 9.
DR IntAct; P56706; 8.
DR STRING; 9606.ENSP00000341032; -.
DR GlyGen; P56706; 3 sites.
DR iPTMnet; P56706; -.
DR PhosphoSitePlus; P56706; -.
DR BioMuta; WNT7B; -.
DR DMDM; 20532426; -.
DR MassIVE; P56706; -.
DR MaxQB; P56706; -.
DR PaxDb; P56706; -.
DR PeptideAtlas; P56706; -.
DR PRIDE; P56706; -.
DR ProteomicsDB; 56939; -.
DR Antibodypedia; 27975; 102 antibodies from 22 providers.
DR DNASU; 7477; -.
DR Ensembl; ENST00000339464.9; ENSP00000341032.4; ENSG00000188064.10.
DR GeneID; 7477; -.
DR KEGG; hsa:7477; -.
DR MANE-Select; ENST00000339464.9; ENSP00000341032.4; NM_058238.3; NP_478679.1.
DR UCSC; uc003bgo.4; human.
DR CTD; 7477; -.
DR DisGeNET; 7477; -.
DR GeneCards; WNT7B; -.
DR HGNC; HGNC:12787; WNT7B.
DR HPA; ENSG00000188064; Tissue enhanced (esophagus, skin, urinary bladder).
DR MalaCards; WNT7B; -.
DR MIM; 601967; gene.
DR neXtProt; NX_P56706; -.
DR OpenTargets; ENSG00000188064; -.
DR PharmGKB; PA37388; -.
DR VEuPathDB; HostDB:ENSG00000188064; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000158861; -.
DR InParanoid; P56706; -.
DR OMA; NSCSERT; -.
DR PhylomeDB; P56706; -.
DR TreeFam; TF105310; -.
DR PathwayCommons; P56706; -.
DR Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR SignaLink; P56706; -.
DR SIGNOR; P56706; -.
DR BioGRID-ORCS; 7477; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; WNT7B; human.
DR GeneWiki; WNT7B; -.
DR GenomeRNAi; 7477; -.
DR Pharos; P56706; Tbio.
DR PRO; PR:P56706; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P56706; protein.
DR Bgee; ENSG00000188064; Expressed in vena cava and 98 other tissues.
DR ExpressionAtlas; P56706; baseline and differential.
DR Genevisible; P56706; HS.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0048018; F:receptor ligand activity; IDA:WormBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:WormBase.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:UniProtKB.
DR GO; GO:0022009; P:central nervous system vasculogenesis; ISS:UniProtKB.
DR GO; GO:0060710; P:chorio-allantoic fusion; ISS:UniProtKB.
DR GO; GO:0060560; P:developmental growth involved in morphogenesis; ISS:UniProtKB.
DR GO; GO:0048568; P:embryonic organ development; ISS:UniProtKB.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; ISS:UniProtKB.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; ISS:UniProtKB.
DR GO; GO:0048144; P:fibroblast proliferation; IEP:UniProtKB.
DR GO; GO:0021871; P:forebrain regionalization; IEP:UniProtKB.
DR GO; GO:0042592; P:homeostatic process; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR GO; GO:0072061; P:inner medullary collecting duct development; ISS:UniProtKB.
DR GO; GO:0070307; P:lens fiber cell development; ISS:BHF-UCL.
DR GO; GO:0060482; P:lobar bronchus development; ISS:UniProtKB.
DR GO; GO:0030324; P:lung development; ISS:UniProtKB.
DR GO; GO:0060428; P:lung epithelium development; ISS:UniProtKB.
DR GO; GO:0060425; P:lung morphogenesis; ISS:UniProtKB.
DR GO; GO:0061180; P:mammary gland epithelium development; IEP:UniProtKB.
DR GO; GO:0072205; P:metanephric collecting duct development; ISS:UniProtKB.
DR GO; GO:0072207; P:metanephric epithelium development; ISS:UniProtKB.
DR GO; GO:0072236; P:metanephric loop of Henle development; ISS:UniProtKB.
DR GO; GO:0003338; P:metanephros morphogenesis; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0072060; P:outer medullary collecting duct development; ISS:UniProtKB.
DR GO; GO:0032364; P:oxygen homeostasis; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0032536; P:regulation of cell projection size; IEA:Ensembl.
DR GO; GO:0072053; P:renal inner medulla development; ISS:UniProtKB.
DR GO; GO:0072054; P:renal outer medulla development; ISS:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; IEP:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
DR GO; GO:0060535; P:trachea cartilage morphogenesis; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
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_0000041444"
FT REGION 238..266
FT /note="Disordered linker"
FT /evidence="ECO:0000269|PubMed:30026314"
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 293
FT /note="L -> I (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 39327 MW; D114C329118C7CB1 CRC64;
MHRNFRKWIF YVFLCFGVLY VKLGALSSVV ALGANIICNK IPGLAPRQRA ICQSRPDAII
VIGEGAQMGI NECQYQFRFG RWNCSALGEK TVFGQELRVG SREAAFTYAI TAAGVAHAVT
AACSQGNLSN CGCDREKQGY YNQAEGWKWG GCSADVRYGI DFSRRFVDAR EIKKNARRLM
NLHNNEAGRK VLEDRMQLEC KCHGVSGSCT TKTCWTTLPK FREVGHLLKE KYNAAVQVEV
VRASRLRQPT FLRIKQLRSY QKPMETDLVY IEKSPNYCEE DAATGSVGTQ GRLCNRTSPG
ADGCDTMCCG RGYNTHQYTK VWQCNCKFHW CCFVKCNTCS ERTEVFTCK
