ID   CMA1_HUMAN              Reviewed;         247 AA.
AC   P23946; B5BUM8; Q16018; Q3SY36; Q3SY37; Q9UDH5;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   24-JAN-2024, entry version 213.
DE   RecName: Full=Chymase;
DE            EC=3.4.21.39;
DE   AltName: Full=Alpha-chymase;
DE   AltName: Full=Mast cell protease I;
DE   Flags: Precursor;
GN   Name=CMA1; Synonyms=CYH, CYM;
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].
RX   PubMed=2071582; DOI=10.1016/s0021-9258(18)98788-0;
RA   Caughey G.H., Zerweck E.H., Vanderslice P.;
RT   "Structure, chromosomal assignment, and deduced amino acid sequence of a
RT   human gene for mast cell chymase.";
RL   J. Biol. Chem. 266:12956-12963(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RX   PubMed=1894611; DOI=10.1016/s0021-9258(19)47355-9;
RA   Urata H., Kinoshita A., Perez D.M., Misono K.S., Bumpus F.M., Graham R.M.,
RA   Husain A.;
RT   "Cloning of the gene and cDNA for human heart chymase.";
RL   J. Biol. Chem. 266:17173-17179(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 22-56; 123-132;
RP   136-148; 167-194 AND 197-247, AND TISSUE SPECIFICITY.
RC   TISSUE=Skin;
RX   PubMed=8144971;
RA   Schechter N.M., Wang Z.M., Blacher R.W., Lessin S.R., Lazarus G.S.,
RA   Rubin H.;
RT   "Determination of the primary structures of human skin chymase and
RT   cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions.";
RL   J. Immunol. 152:4062-4069(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA   Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA   Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA   Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA   Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA   Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA   Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in vitro-
RT   expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [5]
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   [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   ARG-66.
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   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-247 (ISOFORM 1).
RX   PubMed=8495723; DOI=10.1016/0014-5793(93)81461-8;
RA   Sukenaga Y., Kido H., Neki A., Enomoto M., Ishida K., Takagi K.,
RA   Katunuma N.;
RT   "Purification and molecular cloning of chymase from human tonsils.";
RL   FEBS Lett. 323:119-122(1993).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-60.
RC   TISSUE=Placenta;
RX   PubMed=2049082; DOI=10.1042/bj2760567;
RA   Jenne D.E., Tschopp J.;
RT   "Angiotensin II-forming heart chymase is a mast-cell-specific enzyme.";
RL   Biochem. J. 276:567-568(1991).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-103.
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   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=9400368; DOI=10.1021/bi971403n;
RA   McGrath M.E., Mirzadegan T., Schmidt B.F.;
RT   "Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase
RT   at 1.9 A.";
RL   Biochemistry 36:14318-14324(1997).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=9931257; DOI=10.1006/jmbi.1998.2462;
RA   Pereira P.J.P., Wang Z.-M., Rubin H., Huber R., Bode W., Schechter N.M.,
RA   Strobl S.;
RT   "The 2.2-A crystal structure of human chymase in complex with succinyl-Ala-
RT   Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl
RT   carboxypeptidase specificity.";
RL   J. Mol. Biol. 286:163-173(1999).
RN   [13]
RP   ERRATUM OF PUBMED:9931257.
RX   PubMed=10208809; DOI=10.1006/jmbi.1999.2691;
RA   Pereira P.J.P., Wang Z.-M., Rubin H., Huber R., Bode W., Schechter N.M.,
RA   Strobl S.;
RL   J. Mol. Biol. 286:817-817(1999).
CC   -!- FUNCTION: Major secreted protease of mast cells with suspected roles in
CC       vasoactive peptide generation, extracellular matrix degradation, and
CC       regulation of gland secretion.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa >
CC         Leu-|-Xaa.; EC=3.4.21.39;
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Mast cell
CC       granules.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P23946-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P23946-2; Sequence=VSP_056947;
CC   -!- TISSUE SPECIFICITY: Mast cells in lung, heart, skin and placenta.
CC       Expressed in both normal skin and in urticaria pigmentosa lesions.
CC       {ECO:0000269|PubMed:8144971}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; M64269; AAA52020.1; -; Genomic_DNA.
DR   EMBL; M69137; AAA52021.1; -; Genomic_DNA.
DR   EMBL; M69136; AAA52019.1; -; mRNA.
DR   EMBL; AB451464; BAG70278.1; -; mRNA.
DR   EMBL; AL132800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471078; EAW66007.1; -; Genomic_DNA.
DR   EMBL; BC069110; AAH69110.1; -; mRNA.
DR   EMBL; BC069370; AAH69370.1; -; mRNA.
DR   EMBL; BC069490; AAH69490.1; -; mRNA.
DR   EMBL; BC103974; AAI03975.1; -; mRNA.
DR   EMBL; BC103975; AAI03976.1; -; mRNA.
DR   EMBL; S61334; AAB26828.1; -; mRNA.
DR   EMBL; X59072; CAA41796.1; -; Genomic_DNA.
DR   CCDS; CCDS76666.1; -. [P23946-2]
DR   CCDS; CCDS9630.1; -. [P23946-1]
DR   PIR; A40967; KYHUCM.
DR   RefSeq; NP_001295012.1; NM_001308083.1. [P23946-2]
DR   RefSeq; NP_001827.1; NM_001836.4. [P23946-1]
DR   PDB; 1KLT; X-ray; 1.90 A; A=22-247.
DR   PDB; 1NN6; X-ray; 1.75 A; A=20-247.
DR   PDB; 1PJP; X-ray; 2.20 A; A=22-247.
DR   PDB; 1T31; X-ray; 1.90 A; A=22-247.
DR   PDB; 2HVX; X-ray; 2.60 A; A=22-247.
DR   PDB; 3N7O; X-ray; 1.80 A; A=22-247.
DR   PDB; 3S0N; X-ray; 1.95 A; A=22-247.
DR   PDB; 4AFQ; X-ray; 1.51 A; A/B=22-247.
DR   PDB; 4AFS; X-ray; 1.90 A; A=22-247.
DR   PDB; 4AFU; X-ray; 1.82 A; A/B=22-247.
DR   PDB; 4AFZ; X-ray; 2.25 A; A/B=22-247.
DR   PDB; 4AG1; X-ray; 1.40 A; A=22-247.
DR   PDB; 4AG2; X-ray; 1.80 A; A/B=22-247.
DR   PDB; 4K2Y; X-ray; 2.30 A; A=22-247.
DR   PDB; 4K5Z; X-ray; 1.80 A; A=22-247.
DR   PDB; 4K60; X-ray; 1.50 A; A=22-247.
DR   PDB; 4K69; X-ray; 1.50 A; A=22-247.
DR   PDB; 4KP0; X-ray; 2.80 A; A=22-247.
DR   PDB; 5YJM; X-ray; 1.90 A; A=22-247.
DR   PDB; 5YJP; X-ray; 1.80 A; A=22-247.
DR   PDBsum; 1KLT; -.
DR   PDBsum; 1NN6; -.
DR   PDBsum; 1PJP; -.
DR   PDBsum; 1T31; -.
DR   PDBsum; 2HVX; -.
DR   PDBsum; 3N7O; -.
DR   PDBsum; 3S0N; -.
DR   PDBsum; 4AFQ; -.
DR   PDBsum; 4AFS; -.
DR   PDBsum; 4AFU; -.
DR   PDBsum; 4AFZ; -.
DR   PDBsum; 4AG1; -.
DR   PDBsum; 4AG2; -.
DR   PDBsum; 4K2Y; -.
DR   PDBsum; 4K5Z; -.
DR   PDBsum; 4K60; -.
DR   PDBsum; 4K69; -.
DR   PDBsum; 4KP0; -.
DR   PDBsum; 5YJM; -.
DR   PDBsum; 5YJP; -.
DR   AlphaFoldDB; P23946; -.
DR   SMR; P23946; -.
DR   BioGRID; 107624; 63.
DR   IntAct; P23946; 1.
DR   STRING; 9606.ENSP00000250378; -.
DR   BindingDB; P23946; -.
DR   ChEMBL; CHEMBL4068; -.
DR   DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR   DrugBank; DB04016; 2-[3-({Methyl[1-(2-Naphthoyl)Piperidin-4-Yl]Amino}Carbonyl)-2-Naphthyl]-1-(1-Naphthyl)-2-Oxoethylphosphonic Acid.
DR   DrugBank; DB07680; [(1S)-1-(5-CHLORO-1-BENZOTHIEN-3-YL)-2-(2-NAPHTHYLAMINO)-2-OXOETHYL]PHOSPHONIC ACID.
DR   DrugBank; DB03297; Benzylsulfonic acid.
DR   DrugCentral; P23946; -.
DR   GuidetoPHARMACOLOGY; 2340; -.
DR   MEROPS; S01.140; -.
DR   GlyCosmos; P23946; 2 sites, No reported glycans.
DR   GlyGen; P23946; 2 sites.
DR   iPTMnet; P23946; -.
DR   PhosphoSitePlus; P23946; -.
DR   BioMuta; CMA1; -.
DR   DMDM; 126825; -.
DR   jPOST; P23946; -.
DR   MassIVE; P23946; -.
DR   PaxDb; 9606-ENSP00000250378; -.
DR   PeptideAtlas; P23946; -.
DR   ProteomicsDB; 54171; -. [P23946-1]
DR   Antibodypedia; 3125; 459 antibodies from 39 providers.
DR   DNASU; 1215; -.
DR   Ensembl; ENST00000206446.4; ENSP00000206446.4; ENSG00000092009.10. [P23946-2]
DR   Ensembl; ENST00000250378.7; ENSP00000250378.3; ENSG00000092009.10. [P23946-1]
DR   GeneID; 1215; -.
DR   KEGG; hsa:1215; -.
DR   MANE-Select; ENST00000250378.7; ENSP00000250378.3; NM_001836.5; NP_001827.1.
DR   UCSC; uc001wpp.2; human. [P23946-1]
DR   AGR; HGNC:2097; -.
DR   CTD; 1215; -.
DR   DisGeNET; 1215; -.
DR   GeneCards; CMA1; -.
DR   HGNC; HGNC:2097; CMA1.
DR   HPA; ENSG00000092009; Tissue enhanced (breast).
DR   MIM; 118938; gene.
DR   neXtProt; NX_P23946; -.
DR   OpenTargets; ENSG00000092009; -.
DR   PharmGKB; PA26623; -.
DR   VEuPathDB; HostDB:ENSG00000092009; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01030000234551; -.
DR   HOGENOM; CLU_006842_1_0_1; -.
DR   InParanoid; P23946; -.
DR   OMA; MDPQACR; -.
DR   OrthoDB; 2540265at2759; -.
DR   PhylomeDB; P23946; -.
DR   TreeFam; TF333630; -.
DR   BRENDA; 3.4.21.39; 2681.
DR   PathwayCommons; P23946; -.
DR   Reactome; R-HSA-1433557; Signaling by SCF-KIT.
DR   Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   SABIO-RK; P23946; -.
DR   SignaLink; P23946; -.
DR   SIGNOR; P23946; -.
DR   BioGRID-ORCS; 1215; 11 hits in 1148 CRISPR screens.
DR   EvolutionaryTrace; P23946; -.
DR   GeneWiki; CMA1; -.
DR   GenomeRNAi; 1215; -.
DR   Pharos; P23946; Tchem.
DR   PRO; PR:P23946; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; P23946; Protein.
DR   Bgee; ENSG00000092009; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 96 other cell types or tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0030141; C:secretory granule; IDA:MGI.
DR   GO; GO:0004175; F:endopeptidase activity; EXP:Reactome.
DR   GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0008236; F:serine-type peptidase activity; EXP:Reactome.
DR   GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
DR   GO; GO:0034769; P:basement membrane disassembly; IDA:BHF-UCL.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0140447; P:cytokine precursor processing; IDA:BHF-UCL.
DR   GO; GO:0022617; P:extracellular matrix disassembly; IDA:BHF-UCL.
DR   GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IDA:BHF-UCL.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24271:SF24; CHYMASE; 1.
DR   PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; P23946; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..19
FT   PROPEP          20..21
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:8144971"
FT                   /id="PRO_0000027433"
FT   CHAIN           22..247
FT                   /note="Chymase"
FT                   /id="PRO_0000027434"
FT   DOMAIN          22..245
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        66
FT                   /note="Charge relay system"
FT   ACT_SITE        110
FT                   /note="Charge relay system"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:2071582"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   DISULFID        51..67
FT   DISULFID        144..209
FT   DISULFID        175..188
FT   VAR_SEQ         1..111
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056947"
FT   VARIANT         46
FT                   /note="G -> R (in dbSNP:rs5246)"
FT                   /id="VAR_011770"
FT   VARIANT         66
FT                   /note="H -> R (in dbSNP:rs5247)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_011771"
FT   VARIANT         98
FT                   /note="R -> H (in dbSNP:rs13306252)"
FT                   /id="VAR_029190"
FT   CONFLICT        28
FT                   /note="C -> S (in Ref. 8; AAB26828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131..132
FT                   /note="FP -> AV (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          36..42
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          49..57
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:4AFU"
FT   STRAND          89..98
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          112..118
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          143..153
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          163..170
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   TURN            183..185
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   TURN            192..194
FT                   /evidence="ECO:0007829|PDB:1NN6"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          212..219
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   STRAND          228..232
FT                   /evidence="ECO:0007829|PDB:4AG1"
FT   HELIX           233..246
FT                   /evidence="ECO:0007829|PDB:4AG1"
SQ   SEQUENCE   247 AA;  27325 MW;  DC1464A049ED6B00 CRC64;
     MLLLPLPLLL FLLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKF CGGFLIRRNF
     VLTAAHCAGR SITVTLGAHN ITEEEDTWQK LEVIKQFRHP KYNTSTLHHD IMLLKLKEKA
     SLTLAVGTLP FPSQFNFVPP GRMCRVAGWG RTGVLKPGSD TLQEVKLRLM DPQACSHFRD
     FDHNLQLCVG NPRKTKSAFK GDSGGPLLCA GVAQGIVSYG RSDAKPPAVF TRISHYRPWI
     NQILQAN
//