WNT7A_HUMAN
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 03-AUG-2022, entry version 187.
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 PDBsum; 4UZQ; -.
DR AlphaFoldDB; O00755; -.
DR SMR; O00755; -.
DR BioGRID; 113313; 41.
DR DIP; DIP-61511N; -.
DR IntAct; O00755; 37.
DR MINT; O00755; -.
DR STRING; 9606.ENSP00000285018; -.
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; O00755; -.
DR PeptideAtlas; O00755; -.
DR PRIDE; O00755; -.
DR ProteomicsDB; 48019; -.
DR TopDownProteomics; O00755; -.
DR Antibodypedia; 2520; 211 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 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; VQHISGC; -.
DR OrthoDB; 745245at2759; -.
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; 9 hits in 1057 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 68 other tissues.
DR Genevisible; O00755; HS.
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: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: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:0045893; P:positive regulation of transcription, DNA-templated; 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 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 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; unknown pathological 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
