ID   WNT7A_HUMAN             Reviewed;         349 AA.
AC   O00755; Q96H90; Q9Y560;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Protein Wnt-7a;
DE   Flags: Precursor;
GN   Name=WNT7A;
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].
RC   TISSUE=Fetal brain;
RX   PubMed=9161407; DOI=10.1016/s0378-1119(96)00808-6;
RA   Bui T.D., Lako M., Lejeune S., Curtis A.R.J., Strachan T., Lindsay S.,
RA   Harris A.L.;
RT   "Isolation of a full-length human WNT7A gene implicated in limb development
RT   and cell transformation, and mapping to chromosome 3p25.";
RL   Gene 189:25-29(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8893824; DOI=10.1159/000134404;
RA   Ikegawa S., Kumano Y., Okui K., Fujiwara T., Takahashi E., Nakamura Y.;
RT   "Isolation, characterization and chromosomal assignment of the human WNT7A
RT   gene.";
RL   Cytogenet. Cell Genet. 74:149-152(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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 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   [7]
RP   FUNCTION, INTERACTION WITH RECK, DOMAIN, PALMITOLEOYLATION AT SER-206, AND
RP   MUTAGENESIS OF SER-206; VAL-241; 251-PHE-LEU-252 AND LYS-262.
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).
RN   [8] {ECO:0007744|PDB:4UZQ}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 202-209 IN COMPLEX WITH
RP   (9Z)-HEXADECENOIC ACID.
RX   PubMed=25731175; DOI=10.1038/nature14259;
RA   Kakugawa S., Langton P.F., Zebisch M., Howell S.A., Chang T.H., Liu Y.,
RA   Feizi T., Bineva G., O'Reilly N., Snijders A.P., Jones E.Y., Vincent J.P.;
RT   "Notum deacylates Wnt proteins to suppress signalling activity.";
RL   Nature 519:187-192(2015).
RN   [9]
RP   VARIANT FUHRS THR-109, VARIANT LPHAS CYS-292, CHARACTERIZATION OF VARIANT
RP   FUHRS THR-109, CHARACTERIZATION OF VARIANT LPHAS CYS-292, INVOLVEMENT IN
RP   FUHRS, INVOLVEMENT IN LPHAS, AND FUNCTION.
RX   PubMed=16826533; DOI=10.1086/506332;
RA   Woods C.G., Stricker S., Seemann P., Stern R., Cox J., Sherridan E.,
RA   Roberts E., Springell K., Scott S., Karbani G., Sharif S.M., Toomes C.,
RA   Bond J., Kumar D., Al-Gazali L., Mundlos S.;
RT   "Mutations in WNT7A cause a range of limb malformations, including Fuhrmann
RT   syndrome and Al-Awadi/Raas-Rothschild/Schinzel phocomelia syndrome.";
RL   Am. J. Hum. Genet. 79:402-408(2006).
RN   [10]
RP   VARIANT LPHAS CYS-292.
RX   PubMed=17431918; DOI=10.1002/ajmg.a.31712;
RA   Lonardo F., Sabba G., Luquetti D.V., Monica M.D., Scarano G.;
RT   "Al-Awadi/Raas-Rothschild syndrome: two new cases and review.";
RL   Am. J. Med. Genet. A 143:3169-3174(2007).
RN   [11]
RP   VARIANT LPHAS TRP-222.
RX   PubMed=20949531; DOI=10.1002/ajmg.a.33673;
RA   Kantaputra P.N., Mundlos S., Sripathomsawat W.;
RT   "A novel homozygous Arg222Trp missense mutation in WNT7A in two sisters
RT   with severe Al-Awadi/Raas-Rothschild/Schinzel phocomelia syndrome.";
RL   Am. J. Med. Genet. A 152:2832-2837(2010).
RN   [12]
RP   VARIANT LPHAS LYS-72.
RX   PubMed=21271649; DOI=10.1002/ajmg.a.33793;
RA   Garavelli L., Wischmeijer A., Rosato S., Gelmini C., Reverberi S.,
RA   Sassi S., Ferrari A., Mari F., Zabel B., Lausch E., Unger S.,
RA   Superti-Furga A.;
RT   "Al-Awadi-Raas-Rothschild (limb/pelvis/uterus-hypoplasia/aplasia) syndrome
RT   and WNT7A mutations: genetic homogeneity and nosological delineation.";
RL   Am. J. Med. Genet. A 155:332-336(2011).
RN   [13]
RP   VARIANT LPHAS TRP-102.
RX   PubMed=27638328; DOI=10.1016/j.ejmg.2016.09.009;
RA   Mutlu M.B., Cetinkaya A., Koc N., Ceylaner G., Erguner B., Aydin H.,
RA   Karaman S., Demirci O., Goksu K., Karaman A.;
RT   "A novel missense mutation, p.(R102W) in WNT7A causes Al-Awadi Raas-
RT   Rothschild syndrome in a fetus.";
RL   Eur. J. Med. Genet. 59:604-606(2016).
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 (By similarity). Plays an important role in
CC       embryonic development, including dorsal versus ventral patterning
CC       during limb development, skeleton development and urogenital tract
CC       development (PubMed:16826533). Required for central nervous system
CC       (CNS) angiogenesis and blood-brain barrier regulation
CC       (PubMed:30026314). Required for normal, sexually dimorphic development
CC       of the Mullerian ducts, and for normal fertility in both sexes (By
CC       similarity). Required for normal neural stem cell proliferation in the
CC       hippocampus dentate gyrus (By similarity). Required for normal progress
CC       through the cell cycle in neural progenitor cells, for self-renewal of
CC       neural stem cells, and for normal neuronal differentiation and
CC       maturation (By similarity). Promotes formation of synapses via its
CC       interaction with FZD5 (By similarity). {ECO:0000250|UniProtKB:P24383,
CC       ECO:0000269|PubMed:16826533, 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:26902720). The complex with AFM may represent the physiological
CC       form in body fluids (PubMed:26902720). Interacts with FZD5 (By
CC       similarity). Interacts with PORCN (By similarity). 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:P24383, ECO:0000269|PubMed:26902720,
CC       ECO:0000269|PubMed:30026314}.
CC   -!- INTERACTION:
CC       O00755; P55212: CASP6; NbExp=3; IntAct=EBI-727198, EBI-718729;
CC       O00755; P22607: FGFR3; NbExp=3; IntAct=EBI-727198, EBI-348399;
CC       O00755; P06396: GSN; NbExp=3; IntAct=EBI-727198, EBI-351506;
CC       O00755; P13473-2: LAMP2; NbExp=3; IntAct=EBI-727198, EBI-21591415;
CC       O00755; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-727198, EBI-741480;
CC       O00755; Q9Y5W5: WIF1; NbExp=3; IntAct=EBI-727198, EBI-3922719;
CC       O00755; Q9Z0J1: Reck; Xeno; NbExp=4; IntAct=EBI-727198, EBI-20720091;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
CC   -!- TISSUE SPECIFICITY: Expression is restricted to placenta, kidney,
CC       testis, uterus, fetal lung, and fetal and adult brain.
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   -!- DISEASE: Limb pelvis hypoplasia aplasia syndrome (LPHAS) [MIM:276820]:
CC       A syndrome of severe deficiency of the extremities due to hypo- or
CC       aplasia of one or more long bones of one or more limbs. Pelvic
CC       manifestations include hip dislocation, hypoplastic iliac bone and
CC       aplastic pubic bones. Thoracic deformity, unusual facies and
CC       genitourinary anomalies can be present. {ECO:0000269|PubMed:16826533,
CC       ECO:0000269|PubMed:17431918, ECO:0000269|PubMed:20949531,
CC       ECO:0000269|PubMed:21271649, ECO:0000269|PubMed:27638328}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Fuhrmann syndrome (FUHRS) [MIM:228930]: Distinct limb-
CC       malformation disorder characterized also by various degrees of limb
CC       aplasia/hypoplasia and joint dysplasia. {ECO:0000269|PubMed:16826533}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR   EMBL; U53476; AAC51319.1; -; mRNA.
DR   EMBL; D83175; BAA82509.1; -; mRNA.
DR   EMBL; CH471055; EAW64173.1; -; Genomic_DNA.
DR   EMBL; BC008811; AAH08811.1; -; mRNA.
DR   CCDS; CCDS2616.1; -.
DR   RefSeq; NP_004616.2; NM_004625.3.
DR   PDB; 4UZQ; X-ray; 1.50 A; B=202-209.
DR   PDB; 8TZO; EM; 3.10 A; A=1-349.
DR   PDB; 8TZP; EM; 3.23 A; A=1-349.
DR   PDBsum; 4UZQ; -.
DR   PDBsum; 8TZO; -.
DR   PDBsum; 8TZP; -.
DR   AlphaFoldDB; O00755; -.
DR   EMDB; EMD-41764; -.
DR   EMDB; EMD-41765; -.
DR   SMR; O00755; -.
DR   BioGRID; 113313; 41.
DR   DIP; DIP-61511N; -.
DR   IntAct; O00755; 37.
DR   MINT; O00755; -.
DR   STRING; 9606.ENSP00000285018; -.
DR   GlyCosmos; O00755; 3 sites, No reported glycans.
DR   GlyGen; O00755; 3 sites.
DR   iPTMnet; O00755; -.
DR   PhosphoSitePlus; O00755; -.
DR   BioMuta; WNT7A; -.
DR   jPOST; O00755; -.
DR   MassIVE; O00755; -.
DR   MaxQB; O00755; -.
DR   PaxDb; 9606-ENSP00000285018; -.
DR   PeptideAtlas; O00755; -.
DR   ProteomicsDB; 48019; -.
DR   TopDownProteomics; O00755; -.
DR   Antibodypedia; 2520; 239 antibodies from 30 providers.
DR   DNASU; 7476; -.
DR   Ensembl; ENST00000285018.5; ENSP00000285018.4; ENSG00000154764.6.
DR   GeneID; 7476; -.
DR   KEGG; hsa:7476; -.
DR   MANE-Select; ENST00000285018.5; ENSP00000285018.4; NM_004625.4; NP_004616.2.
DR   UCSC; uc003bye.2; human.
DR   AGR; HGNC:12786; -.
DR   CTD; 7476; -.
DR   DisGeNET; 7476; -.
DR   GeneCards; WNT7A; -.
DR   HGNC; HGNC:12786; WNT7A.
DR   HPA; ENSG00000154764; Tissue enhanced (brain, gallbladder, placenta).
DR   MalaCards; WNT7A; -.
DR   MIM; 228930; phenotype.
DR   MIM; 276820; phenotype.
DR   MIM; 601570; gene.
DR   neXtProt; NX_O00755; -.
DR   OpenTargets; ENSG00000154764; -.
DR   Orphanet; 2854; Fuhrmann syndrome.
DR   Orphanet; 2879; Phocomelia, Schinzel type.
DR   PharmGKB; PA37387; -.
DR   VEuPathDB; HostDB:ENSG00000154764; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000158523; -.
DR   HOGENOM; CLU_033039_1_4_1; -.
DR   InParanoid; O00755; -.
DR   OMA; CRCRGFS; -.
DR   OrthoDB; 2874082at2759; -.
DR   PhylomeDB; O00755; -.
DR   TreeFam; TF105310; -.
DR   PathwayCommons; O00755; -.
DR   Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
DR   Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR   SignaLink; O00755; -.
DR   SIGNOR; O00755; -.
DR   BioGRID-ORCS; 7476; 11 hits in 1136 CRISPR screens.
DR   GeneWiki; WNT7A; -.
DR   GenomeRNAi; 7476; -.
DR   Pharos; O00755; Tbio.
DR   PRO; PR:O00755; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O00755; Protein.
DR   Bgee; ENSG00000154764; Expressed in cortical plate and 69 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
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:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR   GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:BHF-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR   GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IEA:Ensembl.
DR   GO; GO:0007409; P:axonogenesis; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0001502; P:cartilage condensation; IDA:AgBase.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0021846; P:cell proliferation in forebrain; IDA:BHF-UCL.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
DR   GO; GO:0022009; P:central nervous system vasculogenesis; IEA:Ensembl.
DR   GO; GO:0021707; P:cerebellar granule cell differentiation; IEA:Ensembl.
DR   GO; GO:0002062; P:chondrocyte differentiation; IDA:AgBase.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR   GO; GO:0000578; P:embryonic axis specification; IMP:BHF-UCL.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
DR   GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR   GO; GO:1904861; P:excitatory synapse assembly; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0070307; P:lens fiber cell development; ISS:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IDA:BHF-UCL.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR   GO; GO:0060066; P:oviduct development; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IDA:BHF-UCL.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1904891; P:positive regulation of excitatory synapse assembly; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR   GO; GO:1905386; P:positive regulation of protein localization to presynapse; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; IDA:ARUK-UCL.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0099068; P:postsynapse assembly; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0099054; P:presynapse assembly; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0031133; P:regulation of axon diameter; IEA:Ensembl.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL.
DR   GO; GO:0007548; P:sex differentiation; TAS:ProtInc.
DR   GO; GO:0014719; P:skeletal muscle satellite cell activation; IEA:Ensembl.
DR   GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IEA:Ensembl.
DR   GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0048864; P:stem cell development; IDA:BHF-UCL.
DR   GO; GO:0036465; P:synaptic vesicle recycling; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0061038; P:uterus morphogenesis; IEA:Ensembl.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:BHF-UCL.
DR   GO; GO:0035313; P:wound healing, spreading of epidermal cells; IDA:BHF-UCL.
DR   CDD; cd19349; Wnt_Wnt7a; 1.
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:SF78; PROTEIN WNT-7A; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01891; WNT7PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
DR   Genevisible; O00755; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Developmental protein; Disease variant; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Lipoprotein; Reference proteome;
KW   Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..349
FT                   /note="Protein Wnt-7a"
FT                   /id="PRO_0000041442"
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:0000305|PubMed:30026314"
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   VARIANT         72
FT                   /note="E -> K (in LPHAS; dbSNP:rs397514666)"
FT                   /evidence="ECO:0000269|PubMed:21271649"
FT                   /id="VAR_065765"
FT   VARIANT         102
FT                   /note="R -> W (in LPHAS; uncertain significance;
FT                   dbSNP:rs879255548)"
FT                   /evidence="ECO:0000269|PubMed:27638328"
FT                   /id="VAR_077340"
FT   VARIANT         109
FT                   /note="A -> T (in FUHRS; retains activity that is
FT                   significant but not comparable to wild-type activity;
FT                   dbSNP:rs104893832)"
FT                   /evidence="ECO:0000269|PubMed:16826533"
FT                   /id="VAR_030673"
FT   VARIANT         222
FT                   /note="R -> W (in LPHAS; dbSNP:rs397514643)"
FT                   /evidence="ECO:0000269|PubMed:20949531"
FT                   /id="VAR_064480"
FT   VARIANT         292
FT                   /note="R -> C (in LPHAS; results in a loss of function
FT                   mutation with some residual activity; dbSNP:rs104893835)"
FT                   /evidence="ECO:0000269|PubMed:16826533,
FT                   ECO:0000269|PubMed:17431918"
FT                   /id="VAR_030674"
FT   MUTAGEN         206
FT                   /note="S->A: Does not affect interaction with RECK."
FT                   /evidence="ECO:0000269|PubMed:30026314"
FT   MUTAGEN         241
FT                   /note="V->A: In 4A; abolished interaction with RECK; when
FT                   associated with 251-A-A-252 and A-262."
FT                   /evidence="ECO:0000269|PubMed:30026314"
FT   MUTAGEN         251..252
FT                   /note="FL->AA: In 4A; abolished interaction with RECK; when
FT                   associated with A-241 and A-262."
FT                   /evidence="ECO:0000269|PubMed:30026314"
FT   MUTAGEN         262
FT                   /note="K->A: In 4A; abolished interaction with RECK; when
FT                   associated with A-241 and 251-A-A-252."
FT                   /evidence="ECO:0000269|PubMed:30026314"
FT   CONFLICT        6
FT                   /note="R -> L (in Ref. 1; AAC51319)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14
FT                   /note="L -> F (in Ref. 2; BAA82509)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="Y -> C (in Ref. 1; AAC51319)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        35
FT                   /note="S -> T (in Ref. 1; AAC51319)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103..104
FT                   /note="EA -> DG (in Ref. 1; AAC51319)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="Q -> H (in Ref. 1; AAC51319)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280
FT                   /note="E -> G (in Ref. 5; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="H -> Q (in Ref. 2; BAA82509)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338
FT                   /note="T -> K (in Ref. 2; BAA82509)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   349 AA;  39005 MW;  259EF506CFCD7AB0 CRC64;
     MNRKARRCLG HLFLSLGMVY LRIGGFSSVV ALGASIICNK IPGLAPRQRA ICQSRPDAII
     VIGEGSQMGL DECQFQFRNG RWNCSALGER TVFGKELKVG SREAAFTYAI IAAGVAHAIT
     AACTQGNLSD CGCDKEKQGQ YHRDEGWKWG GCSADIRYGI GFAKVFVDAR EIKQNARTLM
     NLHNNEAGRK ILEENMKLEC KCHGVSGSCT TKTCWTTLPQ FRELGYVLKD KYNEAVHVEP
     VRASRNKRPT FLKIKKPLSY RKPMDTDLVY IEKSPNYCEE DPVTGSVGTQ GRACNKTAPQ
     ASGCDLMCCG RGYNTHQYAR VWQCNCKFHW CCYVKCNTCS ERTEMYTCK
//