SLUR1_HUMAN
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 03-AUG-2022, entry version 179.
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]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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}.
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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; P55000; -.
DR PeptideAtlas; P55000; -.
DR PRIDE; P55000; -.
DR ProteomicsDB; 56749; -.
DR Antibodypedia; 27784; 162 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 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; 1592016at2759; -.
DR PhylomeDB; P55000; -.
DR TreeFam; TF336080; -.
DR PathwayCommons; P55000; -.
DR SignaLink; P55000; -.
DR BioGRID-ORCS; 57152; 19 hits in 1061 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 96 other tissues.
DR Genevisible; P55000; HS.
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; -; 1.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR027103; SLURP1.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR PANTHER; PTHR10036:SF17; PTHR10036:SF17; 1.
DR Pfam; PF00021; UPAR_LY6; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
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:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000255,
FT ECO:0000305|PubMed:23581991"
FT DISULFID 28..37
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000255,
FT ECO:0000305|PubMed:23581991"
FT DISULFID 43..73
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000255,
FT ECO:0000305|PubMed:23581991"
FT DISULFID 77..93
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000255,
FT ECO:0000305|PubMed:23581991"
FT DISULFID 94..99
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000255,
FT ECO:0000305|PubMed:23581991"
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; unknown pathological significance;
FT no effect on 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
