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   04-NOV-2026, entry version 209.
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 IN COMPLEX WITH ZINC OR COPPER, ACTIVE SITE,
RP   DISULFIDE BONDS, AND MUTAGENESIS OF HIS-54 AND 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, 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="https://atlasgeneticsoncology.org/gene/41087/KLK7";
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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_001207053.2. [P49862-2]
DR   RefSeq; NP_001230055.1; NM_001243126.1.
DR   RefSeq; NP_005037.1; NM_005046.4. [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   AlphaFoldDB; P49862; -.
DR   MDRepo; P49862; -.
DR   SMR; P49862; -.
DR   BioGRID; 111631; 105.
DR   FunCoup; P49862; 281.
DR   IntAct; P49862; 75.
DR   NDEx; IQUERY-CP-KLK7; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000470538; -.
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   GlyCosmos; P49862; 1 site, No reported glycans.
DR   GlyGen; P49862; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P49862; -.
DR   PhosphoSitePlus; P49862; -.
DR   BioMuta; KLK7; -.
DR   DMDM; 1710878; -.
DR   jPOST; P49862; -.
DR   MassIVE; P49862; -.
DR   PaxDb; 9606-ENSP00000470538; -.
DR   PeptideAtlas; P49862; -.
DR   ProteomicsDB; 56160; -. [P49862-1]
DR   ProteomicsDB; 56161; -. [P49862-2]
DR   Pumba; P49862; -.
DR   Antibodypedia; 18939; 464 antibodies from 35 providers.
DR   DNASU; 5650; -.
DR   Ensembl; ENST00000391807.5; ENSP00000375683.1; ENSG00000169035.13. [P49862-1]
DR   Ensembl; ENST00000595820.6; ENSP00000470538.1; ENSG00000169035.13. [P49862-1]
DR   Ensembl; ENST00000597707.5; ENSP00000469950.1; ENSG00000169035.13. [P49862-2]
DR   Ensembl; ENST00000900087.1; ENSP00000570146.1; ENSG00000169035.13. [P49862-1]
DR   Ensembl; ENST00000900088.1; ENSP00000570147.1; ENSG00000169035.13. [P49862-1]
DR   Ensembl; ENST00000900089.1; ENSP00000570148.1; ENSG00000169035.13. [P49862-1]
DR   Ensembl; ENST00000900090.1; ENSP00000570149.1; ENSG00000169035.13. [P49862-1]
DR   Ensembl; ENST00000900091.1; ENSP00000570150.1; ENSG00000169035.13. [P49862-1]
DR   Ensembl; ENST00000900092.1; ENSP00000570151.1; ENSG00000169035.13. [P49862-1]
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   AGR; HGNC:6368; -.
DR   ClinPGx; PA30157; -.
DR   CTD; 5650; -.
DR   DisGeNET; 5650; -.
DR   GeneCards; KLK7; -.
DR   HGNC; HGNC:6368; KLK7.
DR   HPA; ENSG00000169035; Tissue enhanced (esophagus, skin).
DR   MIM; 604438; gene.
DR   OpenTargets; ENSG00000169035; -.
DR   VEuPathDB; HostDB:ENSG00000169035; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01020000230389; -.
DR   HOGENOM; CLU_006842_1_1_1; -.
DR   InParanoid; P49862; -.
DR   OMA; AAHCKMD; -.
DR   OrthoDB; 10061449at2759; -.
DR   PAN-GO; P49862; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; P49862; -.
DR   BRENDA; 3.4.21.117; 2681.
DR   BRENDA; 3.4.21.35; 2681.
DR   PathwayCommons; P49862; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-HSA-9725554; Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin.
DR   SignaLink; P49862; -.
DR   Agora; ENSG00000169035; -.
DR   BioGRID-ORCS; 5650; 17 hits in 1143 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 cell types or tissues.
DR   ExpressionAtlas; P49862; baseline and differential.
DR   GO; GO:0097209; C:epidermal lamellar body; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IMP:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IBA:GO_Central.
DR   GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR   GO; GO:0002780; P:antibacterial peptide biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR   GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR   GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.40.10.10:FF:000021; Kallikrein 1; 1.
DR   FunFam; 2.40.10.10:FF:000010; Kallikrein related peptidase 11; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24271:SF45; KALLIKREIN-7; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Proteomics identification; Reference proteome; Secreted; Serine protease;
KW   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   HELIX           130..134
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
//