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 13-FEB-2019, entry version 170. DE RecName: Full=Protein Wnt-7a; DE Flags: Precursor; GN Name=WNT7A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT development and cell transformation, and mapping to chromosome 3p25."; RL Gene 189:25-29(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8893824; RA Ikegawa S., Kumano Y., Okui K., Fujiwara T., Takahashi E., RA Nakamura Y.; RT "Isolation, characterization and chromosomal assignment of the human RT WNT7A 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT breast cell lines and normal and disease states of human breast RT 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 RT by a serum glycoprotein afamin/alpha-albumin."; RL Elife 5:0-0(2016). RN [7] RP FUNCTION, INTERACTION WITH RECK, DOMAIN, PALMITOLEOYLATION AT SER-206, RP AND 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:0000244|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., RA Liu Y., Feizi T., Bineva G., O'Reilly N., Snijders A.P., Jones E.Y., RA 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 RP VARIANT FUHRS THR-109, CHARACTERIZATION OF VARIANT LPHAS CYS-292, RP INVOLVEMENT IN 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., RA Toomes C., Bond J., Kumar D., Al-Gazali L., Mundlos S.; RT "Mutations in WNT7A cause a range of limb malformations, including RT Fuhrmann syndrome and Al-Awadi/Raas-Rothschild/Schinzel phocomelia RT 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 RT sisters with severe Al-Awadi/Raas-Rothschild/Schinzel phocomelia RT 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) RT syndrome and WNT7A mutations: genetic homogeneity and nosological RT 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 CC in embryonic development, including dorsal versus ventral CC patterning during limb development, skeleton development and CC urogenital tract development (PubMed:16826533). Required for CC central nervous system (CNS) angiogenesis and blood-brain barrier CC regulation (PubMed:30026314). Required for normal, sexually CC dimorphic development of the Mullerian ducts, and for normal CC fertility in both sexes (By similarity). Required for normal CC neural stem cell proliferation in the hippocampus dentate gyrus CC (By similarity). Required for normal progress through the cell CC cycle in neural progenitor cells, for self-renewal of neural stem CC cells, and for normal neuronal differentiation and maturation (By CC similarity). Promotes formation of synapses via its interaction CC 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 CC physiological form in body fluids (PubMed:26902720). Interacts CC with FZD5 (By similarity). Interacts with PORCN (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 CC Wnt7 (PubMed:30026314). {ECO:0000250|UniProtKB:P24383, CC ECO:0000269|PubMed:26902720, ECO:0000269|PubMed:30026314}. CC -!- INTERACTION: CC Q9Z0J1:Reck (xeno); NbExp=4; IntAct=EBI-727198, EBI-20720091; CC Q9Y5W5:WIF1; NbExp=3; IntAct=EBI-727198, EBI-3922719; 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 CC frizzled receptors. Depalmitoleoylation leads to Wnt signaling CC pathway inhibition. {ECO:0000250|UniProtKB:P27467, CC ECO:0000250|UniProtKB:P56704}. CC -!- DISEASE: Limb pelvis hypoplasia aplasia syndrome (LPHAS) CC [MIM:276820]: A syndrome of severe deficiency of the extremities CC due to hypo- or aplasia of one or more long bones of one or more CC limbs. Pelvic manifestations include hip dislocation, hypoplastic CC iliac bone and aplastic pubic bones. Thoracic deformity, unusual CC facies and genitourinary anomalies can be present. CC {ECO:0000269|PubMed:16826533, ECO:0000269|PubMed:17431918, CC ECO:0000269|PubMed:20949531, ECO:0000269|PubMed:21271649, CC ECO:0000269|PubMed:27638328}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Fuhrmann syndrome (FUHRS) [MIM:228930]: Distinct limb- CC malformation disorder characterized also by various degrees of CC limb aplasia/hypoplasia and joint dysplasia. CC {ECO:0000269|PubMed:16826533}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 UniGene; Hs.72290; -. DR PDB; 4UZQ; X-ray; 1.50 A; B=202-209. DR PDBsum; 4UZQ; -. DR ProteinModelPortal; O00755; -. DR SMR; O00755; -. DR BioGrid; 113313; 31. DR DIP; DIP-61511N; -. DR IntAct; O00755; 5. DR MINT; O00755; -. DR STRING; 9606.ENSP00000285018; -. DR iPTMnet; O00755; -. DR PhosphoSitePlus; O00755; -. DR BioMuta; WNT7A; -. DR MaxQB; O00755; -. DR PaxDb; O00755; -. DR PeptideAtlas; O00755; -. DR PRIDE; O00755; -. DR ProteomicsDB; 48019; -. DR TopDownProteomics; O00755; -. DR DNASU; 7476; -. DR Ensembl; ENST00000285018; ENSP00000285018; ENSG00000154764. DR GeneID; 7476; -. DR KEGG; hsa:7476; -. DR UCSC; uc003bye.2; human. DR CTD; 7476; -. DR DisGeNET; 7476; -. DR EuPathDB; HostDB:ENSG00000154764.5; -. DR GeneCards; WNT7A; -. DR HGNC; HGNC:12786; WNT7A. DR HPA; CAB025894; -. DR HPA; HPA015719; -. 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 eggNOG; KOG3913; Eukaryota. DR eggNOG; ENOG410XQZ1; LUCA. DR GeneTree; ENSGT00940000158523; -. DR HOGENOM; HOG000039528; -. DR HOVERGEN; HBG001595; -. DR InParanoid; O00755; -. DR KO; K00572; -. DR OMA; KNMRLEC; -. DR OrthoDB; 745245at2759; -. DR PhylomeDB; O00755; -. DR TreeFam; TF105310; -. 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 ChiTaRS; WNT7A; human. DR GeneWiki; WNT7A; -. DR GenomeRNAi; 7476; -. DR PRO; PR:O00755; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000154764; Expressed in 49 organ(s), highest expression level in epithelium of bronchus. 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: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:0032270; P:positive regulation of cellular protein metabolic process; IDA:ARUK-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: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: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:0016055; P:Wnt signaling pathway; IBA:GO_Central. 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 InterPro; IPR005817; Wnt. DR InterPro; IPR013300; Wnt7. 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; Complete proteome; Developmental protein; KW Disease mutation; Disulfide bond; Extracellular matrix; Glycoprotein; KW Lipoprotein; Reference proteome; Secreted; Signal; KW Wnt signaling pathway. FT SIGNAL 1 31 {ECO:0000255}. FT CHAIN 32 349 Protein Wnt-7a. FT /FTId=PRO_0000041442. FT REGION 238 266 Intrinsically disordered linker. FT {ECO:0000269|PubMed:30026314}. FT LIPID 206 206 O-palmitoleoyl serine; by PORCN. FT {ECO:0000305|PubMed:30026314}. FT CARBOHYD 83 83 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 127 127 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 295 295 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 73 84 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 123 131 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 133 152 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 200 214 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 202 209 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 278 309 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 294 304 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 308 348 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 324 339 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 326 336 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 331 332 {ECO:0000250|UniProtKB:P28026}. FT VARIANT 72 72 E -> K (in LPHAS; dbSNP:rs397514666). FT {ECO:0000269|PubMed:21271649}. FT /FTId=VAR_065765. FT VARIANT 102 102 R -> W (in LPHAS; unknown pathological FT significance; dbSNP:rs879255548). FT {ECO:0000269|PubMed:27638328}. FT /FTId=VAR_077340. FT VARIANT 109 109 A -> T (in FUHRS; retains activity that FT is significant but not comparable to FT wild-type activity; dbSNP:rs104893832). FT {ECO:0000269|PubMed:16826533}. FT /FTId=VAR_030673. FT VARIANT 222 222 R -> W (in LPHAS; dbSNP:rs397514643). FT {ECO:0000269|PubMed:20949531}. FT /FTId=VAR_064480. FT VARIANT 292 292 R -> C (in LPHAS; results in a loss of FT function mutation with some residual FT activity; dbSNP:rs104893835). FT {ECO:0000269|PubMed:16826533, FT ECO:0000269|PubMed:17431918}. FT /FTId=VAR_030674. FT MUTAGEN 206 206 S->A: Does not affect interaction with FT RECK. {ECO:0000269|PubMed:30026314}. FT MUTAGEN 241 241 V->A: In 4A; abolished interaction with FT RECK; when associated with 251-A-A-252 FT and A-262. {ECO:0000269|PubMed:30026314}. FT MUTAGEN 251 252 FL->AA: In 4A; abolished interaction with FT RECK; when associated with A-241 and A- FT 262. {ECO:0000269|PubMed:30026314}. FT MUTAGEN 262 262 K->A: In 4A; abolished interaction with FT RECK; when associated with A-241 and 251- FT A-A-252. {ECO:0000269|PubMed:30026314}. FT CONFLICT 6 6 R -> L (in Ref. 1; AAC51319). FT {ECO:0000305}. FT CONFLICT 14 14 L -> F (in Ref. 2; BAA82509). FT {ECO:0000305}. FT CONFLICT 20 20 Y -> C (in Ref. 1; AAC51319). FT {ECO:0000305}. FT CONFLICT 35 35 S -> T (in Ref. 1; AAC51319). FT {ECO:0000305}. FT CONFLICT 103 104 EA -> DG (in Ref. 1; AAC51319). FT {ECO:0000305}. FT CONFLICT 125 125 Q -> H (in Ref. 1; AAC51319). FT {ECO:0000305}. FT CONFLICT 280 280 E -> G (in Ref. 5; no nucleotide entry). FT {ECO:0000305}. FT CONFLICT 329 329 H -> Q (in Ref. 2; BAA82509). FT {ECO:0000305}. FT CONFLICT 338 338 T -> K (in Ref. 2; BAA82509). FT {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 //