ID SLUR1_HUMAN Reviewed; 103 AA. AC P55000; Q53YJ6; Q6PUA6; Q92483; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 187. DE RecName: Full=Secreted Ly-6/uPAR-related protein 1; DE Short=SLURP-1; DE AltName: Full=ARS component B; DE AltName: Full=ARS(component B)-81/S; DE AltName: Full=Anti-neoplastic urinary protein; DE Short=ANUP; DE Flags: Precursor; GN Name=SLURP1; Synonyms=ARS; 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 [GENOMIC DNA]. RC TISSUE=Placenta; RA Mastrangeli R.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skin; RX PubMed=16354194; DOI=10.1111/j.0022-202x.2005.23973.x; RA Arredondo J., Chernyavsky A.I., Webber R.J., Grando S.A.; RT "Biological effects of SLURP-1 on human keratinocytes."; RL J. Invest. Dermatol. 125:1236-1241(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION. RC TISSUE=Granulocyte; RX PubMed=8742060; DOI=10.1006/cyto.1996.0001; RA Ridge R.J., Sloane N.H.; RT "Partial N-terminal amino acid sequence of the anti-neoplastic urinary RT protein (ANUP) and the anti-tumour effect of the N-terminal nonapeptide of RT the unique cytokine present in human granulocytes."; RL Cytokine 8:1-5(1996). RN [5] RP PARTIAL PROTEIN SEQUENCE, AND SIGNAL SEQUENCE CLEAVAGE SITE. RX PubMed=10211827; DOI=10.1110/ps.8.4.810; RA Andermann K., Wattler F., Wattler S., Heine G., Meyer M., Forssmann W.-G., RA Nehls M.; RT "Structural and phylogenetic characterization of human SLURP-1, the first RT secreted mammalian member of the Ly-6/uPAR protein superfamily."; RL Protein Sci. 8:810-819(1999). RN [6] RP TISSUE SPECIFICITY, INDUCTION, AND POSSIBLE FUNCTION. RX PubMed=14721776; RA Mastrangeli R., Donini S., Kelton C.A., He C., Bressan A., Milazzo F., RA Ciolli V., Borrelli F., Martelli F., Biffoni M., Serlupi-Crescenzi O., RA Serani S., Micangeli E., El Tayar N., Vaccaro R., Renda T., Lisciani R., RA Rossi M., Papoian R.; RT "ARS component B: structural characterization, tissue expression and RT regulation of the gene and protein (SLURP-1) associated with Mal de RT Meleda."; RL Eur. J. Dermatol. 13:560-570(2003). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=14506129; DOI=10.1093/hmg/ddg320; RA Chimienti F., Hogg R.C., Plantard L., Lehmann C., Brakch N., Fischer J., RA Huber M., Bertrand D., Hohl D.; RT "Identification of SLURP-1 as an epidermal neuromodulator explains the RT clinical phenotype of Mal de Meleda."; RL Hum. Mol. Genet. 12:3017-3024(2003). RN [8] RP TISSUE SPECIFICITY, POSSIBLE FUNCTION, VARIANT MDM HIS-71, AND RP CHARACTERIZATION OF VARIANTS MDM ARG-15 AND ARG-86. RX PubMed=17008884; DOI=10.1038/sj.jid.5700551; RA Favre B., Plantard L., Aeschbach L., Brakch N., Christen-Zaech S., RA de Viragh P.A., Sergeant A., Huber M., Hohl D.; RT "SLURP1 is a late marker of epidermal differentiation and is absent in Mal RT de Meleda."; RL J. Invest. Dermatol. 127:301-308(2007). RN [9] RP FUNCTION. RX PubMed=17286989; DOI=10.1016/j.lfs.2006.12.028; RA Moriwaki Y., Yoshikawa K., Fukuda H., Fujii Y.X., Misawa H., Kawashima K.; RT "Immune system expression of SLURP-1 and SLURP-2, two endogenous nicotinic RT acetylcholine receptor ligands."; RL Life Sci. 80:2365-2368(2007). RN [10] RP INVOLVEMENT IN MDM. RX PubMed=11285253; DOI=10.1093/hmg/10.8.875; RA Fischer J., Bouadjar B., Heilig R., Huber M., Lefevre C., Jobard F., RA Macari F., Bakija-Konsuo A., Ait-Belkacem F., Weissenbach J., Lathrop M., RA Hohl D., Prud'homme J.-F.; RT "Mutations in the gene encoding SLURP-1 in Mal de Meleda."; RL Hum. Mol. Genet. 10:875-880(2001). RN [11] RP INDUCTION. RX PubMed=20621062; DOI=10.1016/j.bbrc.2010.07.006; RA Narumoto O., Horiguchi K., Horiguchi S., Moriwaki Y., Takano-Ohmuro H., RA Shoji S., Misawa H., Yamashita N., Nagase T., Kawashima K., Yamashita N.; RT "Down-regulation of secreted lymphocyte antigen-6/urokinase-type RT plasminogen activator receptor-related peptide-1 (SLURP-1), an endogenous RT allosteric alpha7 nicotinic acetylcholine receptor modulator, in murine and RT human asthmatic conditions."; RL Biochem. Biophys. Res. Commun. 398:713-718(2010). RN [12] RP FUNCTION, AND INTERACTION WITH PLAU. RX PubMed=25168896; DOI=10.1167/iovs.14-15107; RA Swamynathan S., Swamynathan S.K.; RT "SLURP-1 modulates corneal homeostasis by serving as a soluble scavenger of RT urokinase-type plasminogen activator."; RL Invest. Ophthalmol. Vis. Sci. 55:6251-6261(2014). RN [13] RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS MDM HIS-71; PRO-71; RP ARG-77; SER-82; SER-94 AND PRO-98. RX PubMed=25919322; DOI=10.1111/bjd.13868; RA Adeyo O., Oberer M., Ploug M., Fong L.G., Young S.G., Beigneux A.P.; RT "Heterogeneity in the properties of mutant secreted lymphocyte antigen RT 6/urokinase receptor-related protein 1 (SLURP1) in Mal de Meleda."; RL Br. J. Dermatol. 173:1066-1069(2015). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHRNA7. RX PubMed=26905431; DOI=10.1371/journal.pone.0149733; RA Lyukmanova E.N., Shulepko M.A., Kudryavtsev D., Bychkov M.L., RA Kulbatskii D.S., Kasheverov I.E., Astapova M.V., Feofanov A.V., RA Thomsen M.S., Mikkelsen J.D., Shenkarev Z.O., Tsetlin V.I., Dolgikh D.A., RA Kirpichnikov M.P.; RT "Human secreted Ly-6/uPAR related protein-1 (SLURP-1) is a selective RT allosteric antagonist of alpha7 nicotinic acetylcholine receptor."; RL PLoS ONE 11:E0149733-E0149733(2016). RN [15] RP STRUCTURE BY NMR OF 23-103. RX PubMed=23581991; DOI=10.1134/s0006297913020090; RA Shulepko M.A., Lyukmanova E.N., Paramonov A.S., Lobas A.A., Shenkarev Z.O., RA Kasheverov I.E., Dolgikh D.A., Tsetlin V.I., Arseniev A.S., RA Kirpichnikov M.P.; RT "Human neuromodulator SLURP-1: bacterial expression, binding to muscle-type RT nicotinic acetylcholine receptor, secondary structure, and conformational RT heterogeneity in solution."; RL Biochemistry (Mosc.) 78:204-211(2013). RN [16] {ECO:0007744|PDB:6ZZE, ECO:0007744|PDB:6ZZF} RP STRUCTURE BY NMR OF 23-103, AND DISULFIDE BONDS. RX PubMed=33019770; DOI=10.3390/ijms21197280; RA Paramonov A.S., Kocharovskaya M.V., Tsarev A.V., Kulbatskii D.S., RA Loktyushov E.V., Shulepko M.A., Kirpichnikov M.P., Lyukmanova E.N., RA Shenkarev Z.O.; RT "Structural Diversity and Dynamics of Human Three-Finger Proteins Acting on RT Nicotinic Acetylcholine Receptors."; RL Int. J. Mol. Sci. 21:0-0(2020). RN [17] RP VARIANT MDM PRO-98. RX PubMed=12950349; DOI=10.1046/j.1365-2230.2003.01342.x; RA Yerebakan O., Hu G., Yilmaz E., Celebi J.T.; RT "A novel mutation in the ARS (component B) gene encoding SLURP-1 in a RT family with Mal de Meleda."; RL Clin. Exp. Dermatol. 28:542-544(2003). RN [18] RP VARIANTS MDM ARG-15 AND ARG-86. RX PubMed=12483299; DOI=10.1007/s00439-002-0838-8; RA Eckl K.M., Stevens H.P., Lestringant G.G., Westenberger-Treumann M., RA Traupe H., Hinz B., Frossard P.M., Stadler R., Leigh I.M., Nuernberg P., RA Reis A., Hennies H.C.; RT "Mal de Meleda (MDM) caused by mutations in the gene for SLURP-1 in RT patients from Germany, Turkey, Palestine, and the United Arab Emirates."; RL Hum. Genet. 112:50-56(2003). RN [19] RP VARIANTS MDM ARG-77 AND TYR-99. RX PubMed=14756676; DOI=10.1111/j.0009-9163.2004.00224.x; RA Mokni M., Charfeddine C., Ben Mously R., Baccouche D., Kaabi B., RA Ben Osman A., Dellagi K., Abdelhak S.; RT "Heterozygous manifestations in female carriers of Mal de Meleda."; RL Clin. Genet. 65:244-246(2004). RN [20] RP VARIANTS MDM ARG-15 AND PRO-71. RX PubMed=19120323; DOI=10.1111/j.1365-2133.2008.08980.x; RA Nellen R.G., van Geel M., Steijlen P.M., van Steensel M.A.; RT "Compound heterozygosity for ARS component B mutations in a Dutch patient RT with mal de Meleda."; RL Br. J. Dermatol. 160:878-880(2009). RN [21] RP VARIANT MDM SER-82. RX PubMed=21690549; DOI=10.1001/archdermatol.2011.138; RA Gruber R., Hennies H.C., Romani N., Schmuth M.; RT "A novel homozygous missense mutation in SLURP1 causing Mal de Meleda with RT an atypical phenotype."; RL Arch. Dermatol. 147:748-750(2011). RN [22] RP VARIANTS MDM ARG-15 AND SER-94. RX PubMed=24604124; DOI=10.2340/00015555-1840; RA Zhao L., Vahlquist A., Virtanen M., Wennerstrand L., Lind L.K., RA Lundstroem A., Hellstroem Pigg M.; RT "Palmoplantar keratoderma of the Gamborg-Nielsen type is caused by RT mutations in the SLURP1 gene and represents a variant of Mal de Meleda."; RL Acta Derm. Venereol. 94:707-710(2014). CC -!- FUNCTION: Has an antitumor activity (PubMed:8742060). Was found to be a CC marker of late differentiation of the skin. Implicated in maintaining CC the physiological and structural integrity of the keratinocyte layers CC of the skin (PubMed:14721776, PubMed:17008884). In vitro down-regulates CC keratinocyte proliferation; the function may involve the proposed role CC as modulator of nicotinic acetylcholine receptors (nAChRs) activity. In CC vitro inhibits alpha-7-dependent nAChR currents in an allosteric manner CC (PubMed:14506129, PubMed:26905431). In T cells may be involved in CC regulation of intracellular Ca(2+) signaling (PubMed:17286989). Seems CC to have an immunomodulatory function in the cornea (By similarity). The CC function may implicate a possible role as a scavenger receptor for PLAU CC thereby blocking PLAU-dependent functions of PLAUR such as in cell CC migration and proliferation (PubMed:25168896). CC {ECO:0000250|UniProtKB:Q9Z0K7, ECO:0000269|PubMed:14506129, CC ECO:0000269|PubMed:17286989, ECO:0000269|PubMed:26905431, CC ECO:0000269|PubMed:8742060, ECO:0000305|PubMed:14721776, CC ECO:0000305|PubMed:17008884}. CC -!- SUBUNIT: Homodimer. Interacts with PLAU (PubMed:25168896). Interacts CC with CHRNA7 (PubMed:26905431). CC -!- INTERACTION: CC P55000; P36544: CHRNA7; NbExp=2; IntAct=EBI-8830896, EBI-79333; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14506129, CC ECO:0000269|PubMed:25919322, ECO:0000269|PubMed:26905431}. CC -!- TISSUE SPECIFICITY: Granulocytes. Expressed in skin. Predominantly CC expressed in the granular layer of skin, notably the acrosyringium. CC Identified in several biological fluids such as sweat, saliva, tears, CC plasma and urine. {ECO:0000269|PubMed:14721776, CC ECO:0000269|PubMed:17008884}. CC -!- INDUCTION: Regulated by retinoic acid, EGF and IFNG/IFN-gamma CC (PubMed:14721776). Down-regulated by IL-13 in cultured human bronchial CC epithelial cells (related to asthmatic condition) (PubMed:20621062). CC {ECO:0000269|PubMed:14721776, ECO:0000269|PubMed:20621062}. CC -!- DISEASE: Mal de Meleda (MDM) [MIM:248300]: A rare autosomal recessive CC skin disorder, characterized by diffuse transgressive palmoplantar CC keratoderma with keratotic lesions extending onto the dorsa of the CC hands and the feet (transgrediens). Patients may have hyperhidrosis. CC Other features include perioral erythema, lichenoid plaques on the CC knees and the elbows, and nail abnormalities. CC {ECO:0000269|PubMed:11285253, ECO:0000269|PubMed:12483299, CC ECO:0000269|PubMed:12950349, ECO:0000269|PubMed:14756676, CC ECO:0000269|PubMed:17008884, ECO:0000269|PubMed:19120323, CC ECO:0000269|PubMed:21690549, ECO:0000269|PubMed:24604124, CC ECO:0000269|PubMed:25919322}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- CAUTION: It is not certain that ARS and ANUP are identical proteins. CC {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; X99977; CAA68237.1; -; Genomic_DNA. DR EMBL; AY579079; AAT01436.1; -; mRNA. DR EMBL; AY579080; AAT01437.1; -; mRNA. DR EMBL; BC069292; AAH69292.1; -; mRNA. DR EMBL; BC105133; AAI05134.1; -; mRNA. DR EMBL; BC105135; AAI05136.1; -; mRNA. DR CCDS; CCDS6387.1; -. DR PIR; A59031; A59031. DR RefSeq; NP_065160.1; NM_020427.2. DR PDB; 6ZZE; NMR; -; A=23-103. DR PDB; 6ZZF; NMR; -; A=23-103. DR PDBsum; 6ZZE; -. DR PDBsum; 6ZZF; -. DR AlphaFoldDB; P55000; -. DR SMR; P55000; -. DR BioGRID; 121409; 163. DR IntAct; P55000; 3. DR STRING; 9606.ENSP00000246515; -. DR TCDB; 8.A.31.1.3; the ly-6 neurotoxin-like protein1 precursor (lynx1) family. DR iPTMnet; P55000; -. DR PhosphoSitePlus; P55000; -. DR BioMuta; SLURP1; -. DR DMDM; 3287957; -. DR jPOST; P55000; -. DR MassIVE; P55000; -. DR PaxDb; 9606-ENSP00000246515; -. DR PeptideAtlas; P55000; -. DR PRIDE; P55000; -. DR ProteomicsDB; 56749; -. DR Pumba; P55000; -. DR Antibodypedia; 27784; 183 antibodies from 21 providers. DR DNASU; 57152; -. DR Ensembl; ENST00000246515.2; ENSP00000246515.1; ENSG00000126233.2. DR GeneID; 57152; -. DR KEGG; hsa:57152; -. DR MANE-Select; ENST00000246515.2; ENSP00000246515.1; NM_020427.3; NP_065160.1. DR UCSC; uc003ywy.3; human. DR AGR; HGNC:18746; -. DR CTD; 57152; -. DR DisGeNET; 57152; -. DR GeneCards; SLURP1; -. DR HGNC; HGNC:18746; SLURP1. DR HPA; ENSG00000126233; Group enriched (esophagus, skin). DR MalaCards; SLURP1; -. DR MIM; 248300; phenotype. DR MIM; 606119; gene. DR neXtProt; NX_P55000; -. DR OpenTargets; ENSG00000126233; -. DR Orphanet; 86923; Hereditary palmoplantar keratoderma, Gamborg-Nielsen type. DR Orphanet; 87503; Mal de Meleda. DR PharmGKB; PA134936818; -. DR VEuPathDB; HostDB:ENSG00000126233; -. DR eggNOG; ENOG502TDUY; Eukaryota. DR GeneTree; ENSGT00940000162933; -. DR HOGENOM; CLU_141358_2_1_1; -. DR InParanoid; P55000; -. DR OMA; GEAFRCY; -. DR OrthoDB; 3013155at2759; -. DR PhylomeDB; P55000; -. DR TreeFam; TF336080; -. DR PathwayCommons; P55000; -. DR SignaLink; P55000; -. DR BioGRID-ORCS; 57152; 19 hits in 1139 CRISPR screens. DR GeneWiki; SLURP1; -. DR GenomeRNAi; 57152; -. DR Pharos; P55000; Tbio. DR PRO; PR:P55000; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P55000; Protein. DR Bgee; ENSG00000126233; Expressed in lower esophagus mucosa and 97 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0030549; F:acetylcholine receptor activator activity; IDA:UniProtKB. DR GO; GO:0005125; F:cytokine activity; NAS:UniProtKB. DR GO; GO:0001775; P:cell activation; NAS:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB. DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl. DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl. DR GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl. DR GO; GO:0038195; P:urokinase plasminogen activator signaling pathway; IDA:UniProtKB. DR CDD; cd00117; LU; 1. DR Gene3D; 2.10.60.10; CD59; 1. DR InterPro; IPR016054; LY6_UPA_recep-like. DR InterPro; IPR045860; Snake_toxin-like_sf. DR PANTHER; PTHR16983; UPAR/LY6 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR16983:SF16; UPAR_LY6 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00021; UPAR_LY6; 1. DR SUPFAM; SSF57302; Snake toxin-like; 1. DR Genevisible; P55000; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytokine; Direct protein sequencing; Disease variant; KW Disulfide bond; Palmoplantar keratoderma; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:10211827" FT CHAIN 23..103 FT /note="Secreted Ly-6/uPAR-related protein 1" FT /id="PRO_0000036167" FT DOMAIN 24..73 FT /note="UPAR/Ly6" FT DISULFID 25..50 FT /evidence="ECO:0000269|PubMed:33019770, FT ECO:0000305|PubMed:23581991, ECO:0007744|PDB:6ZZE, FT ECO:0007744|PDB:6ZZF" FT DISULFID 28..37 FT /evidence="ECO:0000269|PubMed:33019770, FT ECO:0000305|PubMed:23581991, ECO:0007744|PDB:6ZZE, FT ECO:0007744|PDB:6ZZF" FT DISULFID 43..73 FT /evidence="ECO:0000269|PubMed:33019770, FT ECO:0000305|PubMed:23581991, ECO:0007744|PDB:6ZZE, FT ECO:0007744|PDB:6ZZF" FT DISULFID 77..93 FT /evidence="ECO:0000269|PubMed:33019770, FT ECO:0000305|PubMed:23581991, ECO:0007744|PDB:6ZZE, FT ECO:0007744|PDB:6ZZF" FT DISULFID 94..99 FT /evidence="ECO:0000269|PubMed:33019770, FT ECO:0000305|PubMed:23581991, ECO:0007744|PDB:6ZZE, FT ECO:0007744|PDB:6ZZF" FT VARIANT 15 FT /note="W -> R (in MDM; no expression of the protein; FT dbSNP:rs121908318)" FT /evidence="ECO:0000269|PubMed:12483299, FT ECO:0000269|PubMed:17008884, ECO:0000269|PubMed:19120323, FT ECO:0000269|PubMed:24604124" FT /id="VAR_032871" FT VARIANT 71 FT /note="R -> H (in MDM; reduced expression of the protein; FT decreased secretion; dbSNP:rs1448017161)" FT /evidence="ECO:0000269|PubMed:17008884, FT ECO:0000269|PubMed:25919322" FT /id="VAR_032872" FT VARIANT 71 FT /note="R -> P (in MDM; decreased secretion)" FT /evidence="ECO:0000269|PubMed:19120323, FT ECO:0000269|PubMed:25919322" FT /id="VAR_077307" FT VARIANT 77 FT /note="C -> R (in MDM; decreased secretion; FT dbSNP:rs121908319)" FT /evidence="ECO:0000269|PubMed:14756676, FT ECO:0000269|PubMed:25919322" FT /id="VAR_032873" FT VARIANT 82 FT /note="P -> S (in MDM; uncertain significance; no effect on FT secretion; dbSNP:rs1181208026)" FT /evidence="ECO:0000269|PubMed:21690549, FT ECO:0000269|PubMed:25919322" FT /id="VAR_077308" FT VARIANT 86 FT /note="G -> R (in MDM; reduced expression of the protein; FT dbSNP:rs28937888)" FT /evidence="ECO:0000269|PubMed:12483299, FT ECO:0000269|PubMed:17008884" FT /id="VAR_032874" FT VARIANT 94 FT /note="C -> S (in MDM; decreased secretion; FT dbSNP:rs772388665)" FT /evidence="ECO:0000269|PubMed:24604124, FT ECO:0000269|PubMed:25919322" FT /id="VAR_077309" FT VARIANT 98 FT /note="L -> P (in MDM; decreased secretion)" FT /evidence="ECO:0000269|PubMed:12950349, FT ECO:0000269|PubMed:25919322" FT /id="VAR_077310" FT VARIANT 99 FT /note="C -> Y (in MDM; dbSNP:rs121908320)" FT /evidence="ECO:0000269|PubMed:14756676" FT /id="VAR_032875" FT CONFLICT 17 FT /note="M -> V (in Ref. 2; AAT01436)" FT /evidence="ECO:0000305" FT CONFLICT 22 FT /note="A -> Q (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 36 FT /note="S -> A (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:6ZZE" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:6ZZE" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:6ZZE" FT STRAND 49..55 FT /evidence="ECO:0007829|PDB:6ZZE" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:6ZZE" FT STRAND 68..76 FT /evidence="ECO:0007829|PDB:6ZZE" FT STRAND 90..96 FT /evidence="ECO:0007829|PDB:6ZZE" SQ SEQUENCE 103 AA; 11186 MW; 07AAF6BCA8031282 CRC64; MASRWAVQLL LVAAWSMGCG EALKCYTCKE PMTSASCRTI TRCKPEDTAC MTTLVTVEAE YPFNQSPVVT RSCSSSCVAT DPDSIGAAHL IFCCFRDLCN SEL //