CMA1_HUMAN
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 03-AUG-2022, entry version 205.
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; 62.
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 GlyGen; P23946; 2 sites.
DR iPTMnet; P23946; -.
DR PhosphoSitePlus; P23946; -.
DR BioMuta; CMA1; -.
DR DMDM; 126825; -.
DR jPOST; P23946; -.
DR MassIVE; P23946; -.
DR PaxDb; P23946; -.
DR PeptideAtlas; P23946; -.
DR PRIDE; P23946; -.
DR ProteomicsDB; 54171; -. [P23946-1]
DR Antibodypedia; 3125; 409 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 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; PQACRHY; -.
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 1070 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 gall bladder and 95 other tissues.
DR Genevisible; P23946; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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: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; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
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
