LGMN_HUMAN
ID LGMN_HUMAN Reviewed; 433 AA.
AC Q99538; O00123; Q86TV2; Q86TV3; Q9BTY1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Legumain;
DE EC=3.4.22.34;
DE AltName: Full=Asparaginyl endopeptidase;
DE AltName: Full=Protease, cysteine 1;
DE Flags: Precursor;
GN Name=LGMN; Synonyms=PRSC1;
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] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9065484; DOI=10.1074/jbc.272.12.8090;
RA Chen J.-M., Dando P.M., Rawlings N.D., Brown M.A., Young N.E.,
RA Stevens R.A.E., Hewitt E., Watts C., Barrett A.J.;
RT "Cloning, isolation, and characterization of mammalian legumain, an
RT asparaginyl endopeptidase.";
RL J. Biol. Chem. 272:8090-8098(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=8893817; DOI=10.1159/000134397;
RA Tanaka T., Inazawa J., Nakamura Y.;
RT "Molecular cloning of a human cDNA encoding putative cysteine protease
RT (PRSC1) and its chromosome assignment to 14q32.1.";
RL Cytogenet. Cell Genet. 74:120-123(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Neuroblastoma, and Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-18.
RC TISSUE=Placenta;
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 [6]
RP PROTEIN SEQUENCE OF 18-24 AND 324-330, AND PROTEOLYTIC PROCESSING.
RX PubMed=11085925; DOI=10.1042/bj3520327;
RA Chen J.-M., Fortunato M., Barrett A.J.;
RT "Activation of human prolegumain by cleavage at a C-terminal asparagine
RT residue.";
RL Biochem. J. 352:327-334(2000).
RN [7]
RP CHARACTERIZATION OF ACTIVITY ON ASPARTATE BONDS, AND AUTOCATALYTIC
RP CLEAVAGE.
RX PubMed=9821970; DOI=10.1016/s0014-5793(98)01281-2;
RA Halfon S., Patel S., Vega F., Zurawski S., Zurawski G.;
RT "Autocatalytic activation of human legumain at aspartic acid residues.";
RL FEBS Lett. 438:114-118(1998).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-91 AND ASN-167.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=30425301; DOI=10.1038/s41436-018-0355-3;
RA van den Bogaard E.H.J., van Geel M., van Vlijmen-Willems I.M.J.J.,
RA Jansen P.A.M., Peppelman M., van Erp P.E.J., Atalay S., Venselaar H.,
RA Simon M.E.H., Joosten M., Schalkwijk J., Zeeuwen P.L.J.M.;
RT "Deficiency of the human cysteine protease inhibitor cystatin M/E causes
RT hypotrichosis and dry skin.";
RL Genet. Med. 21:1559-1567(2019).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-309, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, PROPEPTIDE,
RP GLYCOSYLATION AT ASN-91; ASN-167; ASN-263 AND ASN-272, SUBUNIT, DOMAIN,
RP MUTAGENESIS OF GLU-190, AND AUTOCATALYTIC PROCESSING.
RX PubMed=23776206; DOI=10.1073/pnas.1300686110;
RA Dall E., Brandstetter H.;
RT "Mechanistic and structural studies on legumain explain its zymogenicity,
RT distinct activation pathways, and regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10940-10945(2013).
CC -!- FUNCTION: Has a strict specificity for hydrolysis of asparaginyl bonds.
CC Can also cleave aspartyl bonds slowly, especially under acidic
CC conditions. Required for normal lysosomal protein degradation in renal
CC proximal tubules. Required for normal degradation of internalized EGFR.
CC Plays a role in the regulation of cell proliferation via its role in
CC EGFR degradation (By similarity). May be involved in the processing of
CC proteins for MHC class II antigen presentation in the
CC lysosomal/endosomal system. {ECO:0000250, ECO:0000269|PubMed:23776206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins and small molecule substrates at
CC -Asn-|-Xaa- bonds.; EC=3.4.22.34;
CC Evidence={ECO:0000269|PubMed:23776206};
CC -!- ACTIVITY REGULATION: Inhibited by CST6. {ECO:0000269|PubMed:30425301}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5 for the free enzyme, and pH 6 in the presence of
CC bound integrins. {ECO:0000269|PubMed:23776206};
CC -!- SUBUNIT: Homodimer before autocatalytic removal of the propeptide (By
CC similarity). Monomer after autocatalytic processing. May interact with
CC integrins. {ECO:0000250, ECO:0000269|PubMed:23776206}.
CC -!- INTERACTION:
CC PRO_0000026502; PRO_0000006639 [P01034]: CST3; NbExp=4; IntAct=EBI-29020361, EBI-29036734;
CC PRO_0000026502; PRO_0000006648 [Q15828]: CST6; NbExp=5; IntAct=EBI-29020361, EBI-29014783;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99538-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99538-2; Sequence=VSP_056454;
CC Name=3;
CC IsoId=Q99538-3; Sequence=VSP_056455, VSP_056456;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Particularly abundant in kidney, heart
CC and placenta.
CC -!- DOMAIN: In the zymogen form, the uncleaved propeptide blocks access to
CC the active site. {ECO:0000269|PubMed:23776206}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:23776206}.
CC -!- PTM: Activated by autocatalytic processing at pH 4.
CC {ECO:0000269|PubMed:11085925}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR EMBL; Y09862; CAA70989.1; -; mRNA.
DR EMBL; D55696; BAA09530.1; -; mRNA.
DR EMBL; BX161380; CAD61872.1; -; mRNA.
DR EMBL; BX161422; CAD61895.1; -; mRNA.
DR EMBL; AL132987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003061; AAH03061.1; -; mRNA.
DR CCDS; CCDS86423.1; -. [Q99538-3]
DR CCDS; CCDS86424.1; -. [Q99538-2]
DR CCDS; CCDS9904.1; -. [Q99538-1]
DR RefSeq; NP_001008530.1; NM_001008530.2. [Q99538-1]
DR RefSeq; NP_005597.3; NM_005606.6. [Q99538-1]
DR RefSeq; XP_005267919.1; XM_005267862.3. [Q99538-2]
DR RefSeq; XP_005267920.1; XM_005267863.3. [Q99538-3]
DR RefSeq; XP_016876952.1; XM_017021463.1. [Q99538-1]
DR RefSeq; XP_016876953.1; XM_017021464.1. [Q99538-1]
DR RefSeq; XP_016876954.1; XM_017021465.1. [Q99538-1]
DR RefSeq; XP_016876955.1; XM_017021466.1.
DR RefSeq; XP_016876956.1; XM_017021467.1.
DR PDB; 4AW9; X-ray; 2.20 A; A=26-309.
DR PDB; 4AWA; X-ray; 2.50 A; A=26-309.
DR PDB; 4AWB; X-ray; 2.70 A; A/B=26-309.
DR PDB; 4FGU; X-ray; 3.90 A; A/B=18-433.
DR PDB; 4N6N; X-ray; 1.87 A; A=26-303.
DR PDB; 4N6O; X-ray; 1.80 A; A=26-303.
DR PDB; 5LU8; X-ray; 1.95 A; A=26-288.
DR PDB; 5LU9; X-ray; 2.27 A; A=26-288.
DR PDB; 5LUA; X-ray; 2.00 A; A/B=26-287.
DR PDB; 5LUB; X-ray; 2.10 A; A/B=26-287.
DR PDB; 7O50; X-ray; 1.90 A; A/B=26-287.
DR PDBsum; 4AW9; -.
DR PDBsum; 4AWA; -.
DR PDBsum; 4AWB; -.
DR PDBsum; 4FGU; -.
DR PDBsum; 4N6N; -.
DR PDBsum; 4N6O; -.
DR PDBsum; 5LU8; -.
DR PDBsum; 5LU9; -.
DR PDBsum; 5LUA; -.
DR PDBsum; 5LUB; -.
DR PDBsum; 7O50; -.
DR AlphaFoldDB; Q99538; -.
DR SMR; Q99538; -.
DR BioGRID; 111624; 46.
DR IntAct; Q99538; 20.
DR MINT; Q99538; -.
DR STRING; 9606.ENSP00000376911; -.
DR BindingDB; Q99538; -.
DR ChEMBL; CHEMBL4244; -.
DR GuidetoPHARMACOLOGY; 2380; -.
DR MEROPS; C13.004; -.
DR GlyConnect; 1449; 6 N-Linked glycans (2 sites).
DR GlyGen; Q99538; 7 sites, 6 N-linked glycans (2 sites), 3 O-linked glycans (3 sites).
DR iPTMnet; Q99538; -.
DR PhosphoSitePlus; Q99538; -.
DR BioMuta; LGMN; -.
DR DMDM; 2842759; -.
DR EPD; Q99538; -.
DR jPOST; Q99538; -.
DR MassIVE; Q99538; -.
DR MaxQB; Q99538; -.
DR PaxDb; Q99538; -.
DR PeptideAtlas; Q99538; -.
DR PRIDE; Q99538; -.
DR ProteomicsDB; 69735; -.
DR ProteomicsDB; 69736; -.
DR ProteomicsDB; 78313; -. [Q99538-1]
DR Antibodypedia; 17; 331 antibodies from 28 providers.
DR DNASU; 5641; -.
DR Ensembl; ENST00000334869.9; ENSP00000334052.4; ENSG00000100600.15. [Q99538-1]
DR Ensembl; ENST00000393218.6; ENSP00000376911.2; ENSG00000100600.15. [Q99538-1]
DR Ensembl; ENST00000555699.5; ENSP00000451861.1; ENSG00000100600.15. [Q99538-3]
DR Ensembl; ENST00000557434.5; ENSP00000452572.1; ENSG00000100600.15. [Q99538-2]
DR GeneID; 5641; -.
DR KEGG; hsa:5641; -.
DR MANE-Select; ENST00000334869.9; ENSP00000334052.4; NM_005606.7; NP_005597.3.
DR UCSC; uc001yav.4; human. [Q99538-1]
DR CTD; 5641; -.
DR DisGeNET; 5641; -.
DR GeneCards; LGMN; -.
DR HGNC; HGNC:9472; LGMN.
DR HPA; ENSG00000100600; Low tissue specificity.
DR MIM; 602620; gene.
DR neXtProt; NX_Q99538; -.
DR OpenTargets; ENSG00000100600; -.
DR PharmGKB; PA30354; -.
DR VEuPathDB; HostDB:ENSG00000100600; -.
DR eggNOG; KOG1348; Eukaryota.
DR GeneTree; ENSGT00940000154782; -.
DR HOGENOM; CLU_024160_2_0_1; -.
DR InParanoid; Q99538; -.
DR OMA; HCFNWHL; -.
DR PhylomeDB; Q99538; -.
DR TreeFam; TF313403; -.
DR BRENDA; 3.4.22.34; 2681.
DR PathwayCommons; Q99538; -.
DR Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-HSA-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR SABIO-RK; Q99538; -.
DR SignaLink; Q99538; -.
DR BioGRID-ORCS; 5641; 8 hits in 1086 CRISPR screens.
DR ChiTaRS; LGMN; human.
DR GeneWiki; LGMN; -.
DR GenomeRNAi; 5641; -.
DR Pharos; Q99538; Tchem.
DR PRO; PR:Q99538; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q99538; protein.
DR Bgee; ENSG00000100600; Expressed in synovial joint and 202 other tissues.
DR ExpressionAtlas; Q99538; baseline and differential.
DR Genevisible; Q99538; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0036021; C:endolysosome lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:ARUK-UCL.
DR GO; GO:0005770; C:late endosome; TAS:ARUK-UCL.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:ARUK-UCL.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:ARUK-UCL.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0008306; P:associative learning; ISS:ARUK-UCL.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:ARUK-UCL.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:ARUK-UCL.
DR GO; GO:0097061; P:dendritic spine organization; ISS:ARUK-UCL.
DR GO; GO:0007613; P:memory; ISS:ARUK-UCL.
DR GO; GO:1901185; P:negative regulation of ERBB signaling pathway; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:ARUK-UCL.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IDA:ARUK-UCL.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:ARUK-UCL.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:ARUK-UCL.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:ARUK-UCL.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISS:UniProtKB.
DR GO; GO:0032801; P:receptor catabolic process; ISS:UniProtKB.
DR GO; GO:0003014; P:renal system process; ISS:UniProtKB.
DR GO; GO:0010447; P:response to acidic pH; IDA:ARUK-UCL.
DR GO; GO:0097264; P:self proteolysis; IDA:ARUK-UCL.
DR GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central.
DR GO; GO:0042359; P:vitamin D metabolic process; TAS:Reactome.
DR InterPro; IPR043577; AE.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; PTHR12000; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500139; AE; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:11085925"
FT CHAIN 18..323
FT /note="Legumain"
FT /id="PRO_0000026502"
FT PROPEP 324..433
FT /id="PRO_0000026503"
FT ACT_SITE 148
FT /evidence="ECO:0000305|PubMed:23776206"
FT ACT_SITE 189
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:23776206"
FT SITE 323..324
FT /note="Cleavage; by autolysis"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:23776206"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:23776206"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23776206"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23776206"
FT DISULFID 378..412
FT /evidence="ECO:0000250"
FT DISULFID 390..429
FT /evidence="ECO:0000250"
FT VAR_SEQ 341..397
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_056454"
FT VAR_SEQ 341..372
FT /note="ARHLIEKSVRKIVSLLAASEAEVEQLLSERAP -> DKIVHGPRVPWSLLKS
FT CLLEAFPSVSAPPTVC (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_056455"
FT VAR_SEQ 373..433
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_056456"
FT VARIANT 18
FT /note="V -> I (in dbSNP:rs2236264)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024588"
FT MUTAGEN 190
FT /note="E->K: Increases catalytic activity at pH 5.5."
FT /evidence="ECO:0000269|PubMed:23776206"
FT MUTAGEN 323
FT /note="N->D,Q,S: Loss of autoactivation."
FT CONFLICT 31
FT /note="V -> A (in Ref. 2; BAA09530)"
FT /evidence="ECO:0000305"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4AW9"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:4N6O"
FT TURN 121..126
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4N6O"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4N6O"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:4N6O"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:4N6O"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:4N6O"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:4N6O"
SQ SEQUENCE 433 AA; 49411 MW; 081AD2D0D584E72A CRC64;
MVWKVAVFLS VALGIGAVPI DDPEDGGKHW VVIVAGSNGW YNYRHQADAC HAYQIIHRNG
IPDEQIVVMM YDDIAYSEDN PTPGIVINRP NGTDVYQGVP KDYTGEDVTP QNFLAVLRGD
AEAVKGIGSG KVLKSGPQDH VFIYFTDHGS TGILVFPNED LHVKDLNETI HYMYKHKMYR
KMVFYIEACE SGSMMNHLPD NINVYATTAA NPRESSYACY YDEKRSTYLG DWYSVNWMED
SDVEDLTKET LHKQYHLVKS HTNTSHVMQY GNKTISTMKV MQFQGMKRKA SSPVPLPPVT
HLDLTPSPDV PLTIMKRKLM NTNDLEESRQ LTEEIQRHLD ARHLIEKSVR KIVSLLAASE
AEVEQLLSER APLTGHSCYP EALLHFRTHC FNWHSPTYEY ALRHLYVLVN LCEKPYPLHR
IKLSMDHVCL GHY
