KLK7_HUMAN
ID KLK7_HUMAN Reviewed; 253 AA.
AC P49862; A8K0U5; Q8N5N9; Q8NFV7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Kallikrein-7;
DE Short=hK7;
DE EC=3.4.21.117;
DE AltName: Full=Serine protease 6;
DE AltName: Full=Stratum corneum chymotryptic enzyme;
DE Short=hSCCE;
DE Flags: Precursor;
GN Name=KLK7; Synonyms=PRSS6, SCCE;
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), AND PROTEIN SEQUENCE OF 23-53.
RC TISSUE=Skin;
RX PubMed=8034709; DOI=10.1016/s0021-9258(17)32185-3;
RA Hansson L., Stroemqvist M., Baeckman A., Wallbrandt P., Carlstein A.,
RA Egelrud T.;
RT "Cloning, expression, and characterization of stratum corneum chymotryptic
RT enzyme. A skin-specific human serine proteinase.";
RL J. Biol. Chem. 269:19420-19426(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Keratinocyte;
RX PubMed=10974542; DOI=10.1016/s0378-1119(00)00280-8;
RA Yousef G.M., Scorilas A., Magklara A., Soosaipillai A., Diamandis E.P.;
RT "The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic
RT enzyme is a new member of the human kallikrein gene family -- genomic
RT characterization, mapping, tissue expression and hormonal regulation.";
RL Gene 254:119-128(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11054574; DOI=10.1016/s0378-1119(00)00382-6;
RA Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P.,
RA Paeper B., Wang K.;
RT "Sequencing and expression analysis of the serine protease gene cluster
RT located in chromosome 19q13 region.";
RL Gene 257:119-130(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11874483; DOI=10.1046/j.0022-202x.2001.01684.x;
RA Hansson L., Backman A., Ny A., Edlund M., Ekholm E.,
RA Ekstrand Hammarstrom B., Tornell J., Wallbrandt P., Wennbo H., Egelrud T.;
RT "Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a
RT model for chronic itchy dermatitis.";
RL J. Invest. Dermatol. 118:444-449(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Ovarian carcinoma;
RX PubMed=12738725;
RA Dong Y., Kaushal A., Brattsand M., Nicklin J., Clements J.A.;
RT "Differential splicing of KLK5 and KLK7 in epithelial ovarian cancer
RT produces novel variants with potential as cancer biomarkers.";
RL Clin. Cancer Res. 9:1710-1720(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Prostate;
RA Mo Z., Yang X.;
RT "Prostate epithelial cells KLK7 protein.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [10]
RP CHARACTERIZATION.
RX PubMed=7794273; DOI=10.1006/bbrc.1995.1853;
RA Skytt A., Stroemqvist M., Egelrud T.;
RT "Primary substrate specificity of recombinant human stratum corneum
RT chymotryptic enzyme.";
RL Biochem. Biophys. Res. Commun. 211:586-589(1995).
RN [11]
RP FUNCTION, CLEAVAGE SPECIFICITY FOR INSULIN, AND ACTIVITY REGULATION.
RX PubMed=23370777; DOI=10.1007/s00018-013-1258-8;
RA Heiker J.T., Kloting N., Kovacs P., Kuettner E.B., Strater N., Schultz S.,
RA Kern M., Stumvoll M., Bluher M., Beck-Sickinger A.G.;
RT "Vaspin inhibits kallikrein 7 by serpin mechanism.";
RL Cell. Mol. Life Sci. 70:2569-2583(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 30-253 IN COMPLEX WITH ZINC OR
RP COPPER, ACTIVE SITE, DISULFIDE BONDS, AND MUTAGENESIS OF HIS-54 AND
RP HIS-109.
RX PubMed=17909180; DOI=10.1073/pnas.0707811104;
RA Debela M., Hess P., Magdolen V., Schechter N.M., Steiner T., Huber R.,
RA Bode W., Goettig P.;
RT "Chymotryptic specificity determinants in the 1.0 A structure of the zinc-
RT inhibited human tissue kallikrein 7.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:16086-16091(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-250, AND DISULFIDE BONDS.
RX PubMed=18329042; DOI=10.1016/j.jmb.2008.01.089;
RA Fernandez I.S., Standker L., Magert H.J., Forssmann W.G.,
RA Gimenez-Gallego G., Romero A.;
RT "Crystal structure of human epidermal kallikrein 7 (hK7) synthesized
RT directly in its native state in E. coli: insights into the atomic basis of
RT its inhibition by LEKTI domain 6 (LD6).";
RL J. Mol. Biol. 377:1488-1497(2008).
CC -!- FUNCTION: May catalyze the degradation of intercellular cohesive
CC structures in the cornified layer of the skin in the continuous
CC shedding of cells from the skin surface. Specific for amino acid
CC residues with aromatic side chains in the P1 position. Cleaves insulin
CC A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7',
CC '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play
CC a role in the activation of precursors to inflammatory cytokines.
CC {ECO:0000269|PubMed:23370777}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of proteins with aromatic side chains in the P1
CC position.; EC=3.4.21.117;
CC -!- ACTIVITY REGULATION: Inhibited by Zn2+ and Cu2+ at low micromolar
CC concentrations. Inhibited by SERPINA12. {ECO:0000269|PubMed:23370777}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12738725}. Note=In
CC ovarian carcinoma, secreted and also observed at the apical membrane
CC and in cytoplasm at the invasive front.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=P49862-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P49862-2; Sequence=VSP_013581;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the skin and is expressed
CC by keratinocytes in the epidermis. Also expressed in the brain, mammary
CC gland, cerebellum, spinal cord and kidney. Lower levels in salivary
CC glands, uterus, thymus, thyroid, placenta, trachea and testis. Up-
CC regulated in ovarian carcinoma, especially late-stage serous carcinoma,
CC compared with normal ovaries and benign adenomas (at protein level).
CC {ECO:0000269|PubMed:10974542, ECO:0000269|PubMed:12738725}.
CC -!- INDUCTION: By estrogens and glucocorticoids in a breast carcinoma cell
CC line. {ECO:0000269|PubMed:10974542}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/KLK7ID41087ch19q13.html";
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DR EMBL; L33404; AAC37551.1; -; mRNA.
DR EMBL; AF166330; AAD49718.1; -; Genomic_DNA.
DR EMBL; AF243527; AAG33360.1; -; Genomic_DNA.
DR EMBL; AF332583; AAK69624.1; -; Genomic_DNA.
DR EMBL; AF411214; AAN03662.1; -; mRNA.
DR EMBL; AF411215; AAN03663.1; -; mRNA.
DR EMBL; AY601109; AAU04540.1; -; mRNA.
DR EMBL; AK289660; BAF82349.1; -; mRNA.
DR EMBL; CH471135; EAW71959.1; -; Genomic_DNA.
DR EMBL; BC032005; AAH32005.1; -; mRNA.
DR CCDS; CCDS12812.1; -. [P49862-1]
DR CCDS; CCDS59414.1; -. [P49862-2]
DR PIR; A53968; A53968.
DR RefSeq; NP_001193982.1; NM_001207053.1. [P49862-2]
DR RefSeq; NP_001230055.1; NM_001243126.1.
DR RefSeq; NP_005037.1; NM_005046.3. [P49862-1]
DR RefSeq; NP_644806.1; NM_139277.2. [P49862-1]
DR PDB; 2QXG; X-ray; 2.60 A; A/B=30-253.
DR PDB; 2QXH; X-ray; 2.00 A; A=30-253.
DR PDB; 2QXI; X-ray; 1.00 A; A=30-253.
DR PDB; 2QXJ; X-ray; 2.10 A; A=30-253.
DR PDB; 3BSQ; X-ray; 2.80 A; A/B/C=30-250.
DR PDB; 5FAH; X-ray; 1.10 A; A=30-253.
DR PDB; 5Y9L; X-ray; 2.15 A; A=30-253.
DR PDB; 5YJK; X-ray; 2.40 A; A=30-253.
DR PDB; 6SHH; X-ray; 2.00 A; A/B/C/D/E/F/G/H=30-253.
DR PDB; 6SHI; X-ray; 1.85 A; A/B/C/D/E/F/G/H=30-253.
DR PDB; 6SJU; X-ray; 1.97 A; A/B/C/D/E/F/G/H=30-253.
DR PDB; 6Y4S; X-ray; 2.23 A; A/B/C=30-253.
DR PDBsum; 2QXG; -.
DR PDBsum; 2QXH; -.
DR PDBsum; 2QXI; -.
DR PDBsum; 2QXJ; -.
DR PDBsum; 3BSQ; -.
DR PDBsum; 5FAH; -.
DR PDBsum; 5Y9L; -.
DR PDBsum; 5YJK; -.
DR PDBsum; 6SHH; -.
DR PDBsum; 6SHI; -.
DR PDBsum; 6SJU; -.
DR PDBsum; 6Y4S; -.
DR AlphaFoldDB; P49862; -.
DR SMR; P49862; -.
DR BioGRID; 111631; 103.
DR IntAct; P49862; 23.
DR MINT; P49862; -.
DR STRING; 9606.ENSP00000375683; -.
DR BindingDB; P49862; -.
DR ChEMBL; CHEMBL2443; -.
DR DrugBank; DB08038; L-alanyl-N-[(1S,2R)-1-benzyl-2-hydroxypropyl]-L-alaninamide.
DR GuidetoPHARMACOLOGY; 2377; -.
DR MEROPS; S01.300; -.
DR GlyGen; P49862; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P49862; -.
DR PhosphoSitePlus; P49862; -.
DR BioMuta; KLK7; -.
DR DMDM; 1710878; -.
DR EPD; P49862; -.
DR MassIVE; P49862; -.
DR PaxDb; P49862; -.
DR PeptideAtlas; P49862; -.
DR PRIDE; P49862; -.
DR ProteomicsDB; 56160; -. [P49862-1]
DR ProteomicsDB; 56161; -. [P49862-2]
DR Antibodypedia; 18939; 410 antibodies from 32 providers.
DR DNASU; 5650; -.
DR Ensembl; ENST00000391807.5; ENSP00000375683.1; ENSG00000169035.12. [P49862-1]
DR Ensembl; ENST00000595820.6; ENSP00000470538.1; ENSG00000169035.12. [P49862-1]
DR Ensembl; ENST00000597707.5; ENSP00000469950.1; ENSG00000169035.12. [P49862-2]
DR GeneID; 5650; -.
DR KEGG; hsa:5650; -.
DR MANE-Select; ENST00000595820.6; ENSP00000470538.1; NM_005046.4; NP_005037.1.
DR UCSC; uc002puo.4; human. [P49862-1]
DR CTD; 5650; -.
DR DisGeNET; 5650; -.
DR GeneCards; KLK7; -.
DR HGNC; HGNC:6368; KLK7.
DR HPA; ENSG00000169035; Group enriched (esophagus, skin).
DR MIM; 604438; gene.
DR neXtProt; NX_P49862; -.
DR OpenTargets; ENSG00000169035; -.
DR PharmGKB; PA30157; -.
DR VEuPathDB; HostDB:ENSG00000169035; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P49862; -.
DR OMA; YSTKTHA; -.
DR PhylomeDB; P49862; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.117; 2681.
DR PathwayCommons; P49862; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR SignaLink; P49862; -.
DR BioGRID-ORCS; 5650; 16 hits in 1067 CRISPR screens.
DR ChiTaRS; KLK7; human.
DR EvolutionaryTrace; P49862; -.
DR GeneWiki; KLK7; -.
DR GenomeRNAi; 5650; -.
DR Pharos; P49862; Tchem.
DR PRO; PR:P49862; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P49862; protein.
DR Bgee; ENSG00000169035; Expressed in gingival epithelium and 151 other tissues.
DR ExpressionAtlas; P49862; baseline and differential.
DR Genevisible; P49862; HS.
DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR GO; GO:0097209; C:epidermal lamellar body; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IMP:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
DR GO; GO:0008233; F:peptidase activity; IMP:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR GO; GO:0002803; P:positive regulation of antibacterial peptide production; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..22
FT /evidence="ECO:0000269|PubMed:8034709"
FT PROPEP 23..29
FT /note="Activation peptide"
FT /id="PRO_0000027942"
FT CHAIN 30..253
FT /note="Kallikrein-7"
FT /id="PRO_0000027943"
FT DOMAIN 30..250
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 70
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:17909180"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:17909180"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:17909180"
FT SITE 109
FT /note="Major binding site for inhibitory zinc or copper"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..165
FT DISULFID 55..71
FT DISULFID 137..239
FT DISULFID 144..211
FT DISULFID 176..190
FT DISULFID 201..226
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12738725"
FT /id="VSP_013581"
FT MUTAGEN 54
FT /note="H->F: No effect on zinc inhibition."
FT /evidence="ECO:0000269|PubMed:17909180"
FT MUTAGEN 109
FT /note="H->A: No zinc inhibition."
FT /evidence="ECO:0000269|PubMed:17909180"
FT CONFLICT 226
FT /note="C -> W (in Ref. 9; AAH32005)"
FT /evidence="ECO:0000305"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2QXI"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2QXI"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6SJU"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:2QXI"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:2QXI"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2QXI"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:2QXI"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2QXI"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:2QXI"
SQ SEQUENCE 253 AA; 27525 MW; 2D68B6B15A76A668 CRC64;
MARSLLLPLQ ILLLSLALET AGEEAQGDKI IDGAPCARGS HPWQVALLSG NQLHCGGVLV
NERWVLTAAH CKMNEYTVHL GSDTLGDRRA QRIKASKSFR HPGYSTQTHV NDLMLVKLNS
QARLSSMVKK VRLPSRCEPP GTTCTVSGWG TTTSPDVTFP SDLMCVDVKL ISPQDCTKVY
KDLLENSMLC AGIPDSKKNA CNGDSGGPLV CRGTLQGLVS WGTFPCGQPN DPGVYTQVCK
FTKWINDTMK KHR
