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Kallikrein-7 (hK7) (EC 3.4.21.117) (Serine protease 6) (Stratum corneum chymotryptic enzyme) (hSCCE)

 KLK7_HUMAN              Reviewed;         253 AA.
P49862; A8K0U5; Q8N5N9; Q8NFV7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-DEC-2018, entry version 168.
RecName: Full=Kallikrein-7;
Short=hK7;
EC=3.4.21.117;
AltName: Full=Serine protease 6;
AltName: Full=Stratum corneum chymotryptic enzyme;
Short=hSCCE;
Flags: Precursor;
Name=KLK7; Synonyms=PRSS6, SCCE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 23-53.
TISSUE=Skin;
PubMed=8034709;
Hansson L., Stroemqvist M., Baeckman A., Wallbrandt P., Carlstein A.,
Egelrud T.;
"Cloning, expression, and characterization of stratum corneum
chymotryptic enzyme. A skin-specific human serine proteinase.";
J. Biol. Chem. 269:19420-19426(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
TISSUE=Keratinocyte;
PubMed=10974542; DOI=10.1016/S0378-1119(00)00280-8;
Yousef G.M., Scorilas A., Magklara A., Soosaipillai A.,
Diamandis E.P.;
"The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic
enzyme is a new member of the human kallikrein gene family -- genomic
characterization, mapping, tissue expression and hormonal
regulation.";
Gene 254:119-128(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11054574; DOI=10.1016/S0378-1119(00)00382-6;
Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J.,
Moss P., Paeper B., Wang K.;
"Sequencing and expression analysis of the serine protease gene
cluster located in chromosome 19q13 region.";
Gene 257:119-130(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11874483; DOI=10.1046/j.0022-202x.2001.01684.x;
Hansson L., Backman A., Ny A., Edlund M., Ekholm E.,
Ekstrand Hammarstrom B., Tornell J., Wallbrandt P., Wennbo H.,
Egelrud T.;
"Epidermal overexpression of stratum corneum chymotryptic enzyme in
mice: a model for chronic itchy dermatitis.";
J. Invest. Dermatol. 118:444-449(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Ovarian carcinoma;
PubMed=12738725;
Dong Y., Kaushal A., Brattsand M., Nicklin J., Clements J.A.;
"Differential splicing of KLK5 and KLK7 in epithelial ovarian cancer
produces novel variants with potential as cancer biomarkers.";
Clin. Cancer Res. 9:1710-1720(2003).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Prostate;
Mo Z., Yang X.;
"Prostate epithelial cells KLK7 protein.";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
CHARACTERIZATION.
PubMed=7794273; DOI=10.1006/bbrc.1995.1853;
Skytt A., Stroemqvist M., Egelrud T.;
"Primary substrate specificity of recombinant human stratum corneum
chymotryptic enzyme.";
Biochem. Biophys. Res. Commun. 211:586-589(1995).
[11]
FUNCTION, CLEAVAGE SPECIFICITY FOR INSULIN, AND ACTIVITY REGULATION.
PubMed=23370777; DOI=10.1007/s00018-013-1258-8;
Heiker J.T., Kloting N., Kovacs P., Kuettner E.B., Strater N.,
Schultz S., Kern M., Stumvoll M., Bluher M., Beck-Sickinger A.G.;
"Vaspin inhibits kallikrein 7 by serpin mechanism.";
Cell. Mol. Life Sci. 70:2569-2583(2013).
[12]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 30-253 IN COMPLEX WITH ZINC
OR COPPER, ACTIVE SITE, DISULFIDE BONDS, AND MUTAGENESIS OF HIS-54 AND
HIS-109.
PubMed=17909180; DOI=10.1073/pnas.0707811104;
Debela M., Hess P., Magdolen V., Schechter N.M., Steiner T., Huber R.,
Bode W., Goettig P.;
"Chymotryptic specificity determinants in the 1.0 A structure of the
zinc-inhibited human tissue kallikrein 7.";
Proc. Natl. Acad. Sci. U.S.A. 104:16086-16091(2007).
[13]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-250, AND DISULFIDE BONDS.
PubMed=18329042; DOI=10.1016/j.jmb.2008.01.089;
Fernandez I.S., Standker L., Magert H.J., Forssmann W.G.,
Gimenez-Gallego G., Romero A.;
"Crystal structure of human epidermal kallikrein 7 (hK7) synthesized
directly in its native state in E. coli: insights into the atomic
basis of its inhibition by LEKTI domain 6 (LD6).";
J. Mol. Biol. 377:1488-1497(2008).
-!- FUNCTION: May catalyze the degradation of intercellular cohesive
structures in the cornified layer of the skin in the continuous
shedding of cells from the skin surface. Specific for amino acid
residues with aromatic side chains in the P1 position. Cleaves
insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-
Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-
Thr-27'. Could play a role in the activation of precursors to
inflammatory cytokines. {ECO:0000269|PubMed:23370777}.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of proteins with aromatic side chains in the P1
position.; EC=3.4.21.117;
-!- ACTIVITY REGULATION: Inhibited by Zn2+ and Cu2+ at low micromolar
concentrations. Inhibited by SERPINA12.
{ECO:0000269|PubMed:23370777}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12738725}.
Note=In ovarian carcinoma, secreted and also observed at the
apical membrane and in cytoplasm at the invasive front.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=P49862-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P49862-2; Sequence=VSP_013581;
-!- TISSUE SPECIFICITY: Abundantly expressed in the skin and is
expressed by keratinocytes in the epidermis. Also expressed in the
brain, mammary gland, cerebellum, spinal cord and kidney. Lower
levels in salivary glands, uterus, thymus, thyroid, placenta,
trachea and testis. Up-regulated in ovarian carcinoma, especially
late-stage serous carcinoma, compared with normal ovaries and
benign adenomas (at protein level). {ECO:0000269|PubMed:10974542,
ECO:0000269|PubMed:12738725}.
-!- INDUCTION: By estrogens and glucocorticoids in a breast carcinoma
cell line. {ECO:0000269|PubMed:10974542}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/KLK7ID41087ch19q13.html";
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EMBL; L33404; AAC37551.1; -; mRNA.
EMBL; AF166330; AAD49718.1; -; Genomic_DNA.
EMBL; AF243527; AAG33360.1; -; Genomic_DNA.
EMBL; AF332583; AAK69624.1; -; Genomic_DNA.
EMBL; AF411214; AAN03662.1; -; mRNA.
EMBL; AF411215; AAN03663.1; -; mRNA.
EMBL; AY601109; AAU04540.1; -; mRNA.
EMBL; AK289660; BAF82349.1; -; mRNA.
EMBL; CH471135; EAW71959.1; -; Genomic_DNA.
EMBL; BC032005; AAH32005.1; -; mRNA.
CCDS; CCDS12812.1; -. [P49862-1]
CCDS; CCDS59414.1; -. [P49862-2]
PIR; A53968; A53968.
RefSeq; NP_001193982.1; NM_001207053.1. [P49862-2]
RefSeq; NP_001230055.1; NM_001243126.1.
RefSeq; NP_005037.1; NM_005046.3. [P49862-1]
RefSeq; NP_644806.1; NM_139277.2. [P49862-1]
UniGene; Hs.151254; -.
PDB; 2QXG; X-ray; 2.60 A; A/B=30-253.
PDB; 2QXH; X-ray; 2.00 A; A=30-253.
PDB; 2QXI; X-ray; 1.00 A; A=30-253.
PDB; 2QXJ; X-ray; 2.10 A; A=30-253.
PDB; 3BSQ; X-ray; 2.80 A; A/B/C=30-250.
PDB; 5FAH; X-ray; 1.10 A; A=30-253.
PDB; 5Y9L; X-ray; 2.15 A; A=30-253.
PDB; 5YJK; X-ray; 2.40 A; A=30-253.
PDBsum; 2QXG; -.
PDBsum; 2QXH; -.
PDBsum; 2QXI; -.
PDBsum; 2QXJ; -.
PDBsum; 3BSQ; -.
PDBsum; 5FAH; -.
PDBsum; 5Y9L; -.
PDBsum; 5YJK; -.
ProteinModelPortal; P49862; -.
SMR; P49862; -.
BioGrid; 111631; 27.
IntAct; P49862; 9.
MINT; P49862; -.
STRING; 9606.ENSP00000375683; -.
BindingDB; P49862; -.
ChEMBL; CHEMBL2443; -.
GuidetoPHARMACOLOGY; 2377; -.
MEROPS; S01.300; -.
iPTMnet; P49862; -.
PhosphoSitePlus; P49862; -.
BioMuta; KLK7; -.
DMDM; 1710878; -.
EPD; P49862; -.
PaxDb; P49862; -.
PeptideAtlas; P49862; -.
PRIDE; P49862; -.
ProteomicsDB; 56160; -.
ProteomicsDB; 56161; -. [P49862-2]
DNASU; 5650; -.
Ensembl; ENST00000391807; ENSP00000375683; ENSG00000169035. [P49862-1]
Ensembl; ENST00000595820; ENSP00000470538; ENSG00000169035. [P49862-1]
Ensembl; ENST00000597707; ENSP00000469950; ENSG00000169035. [P49862-2]
GeneID; 5650; -.
KEGG; hsa:5650; -.
UCSC; uc002puo.4; human. [P49862-1]
CTD; 5650; -.
DisGeNET; 5650; -.
EuPathDB; HostDB:ENSG00000169035.11; -.
GeneCards; KLK7; -.
HGNC; HGNC:6368; KLK7.
HPA; CAB026342; -.
HPA; HPA018994; -.
HPA; HPA062126; -.
MIM; 604438; gene.
neXtProt; NX_P49862; -.
OpenTargets; ENSG00000169035; -.
PharmGKB; PA30157; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00940000153679; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P49862; -.
KO; K08668; -.
OMA; FPSDLMC; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P49862; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.117; 2681.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
ChiTaRS; KLK7; human.
EvolutionaryTrace; P49862; -.
GeneWiki; KLK7; -.
GenomeRNAi; 5650; -.
PMAP-CutDB; P49862; -.
PRO; PR:P49862; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000169035; Expressed in 177 organ(s), highest expression level in mammalian vulva.
CleanEx; HS_KLK7; -.
ExpressionAtlas; P49862; baseline and differential.
Genevisible; P49862; HS.
GO; GO:0097209; C:epidermal lamellar body; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IMP:UniProtKB.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0008233; F:peptidase activity; IMP:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0002803; P:positive regulation of antibacterial peptide production; IMP:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Protease; Reference proteome; Secreted; Serine protease; Signal;
Zymogen.
SIGNAL 1 22 {ECO:0000269|PubMed:8034709}.
PROPEP 23 29 Activation peptide.
/FTId=PRO_0000027942.
CHAIN 30 253 Kallikrein-7.
/FTId=PRO_0000027943.
DOMAIN 30 250 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 70 70 Charge relay system.
{ECO:0000269|PubMed:17909180}.
ACT_SITE 112 112 Charge relay system.
{ECO:0000269|PubMed:17909180}.
ACT_SITE 205 205 Charge relay system.
{ECO:0000269|PubMed:17909180}.
SITE 109 109 Major binding site for inhibitory zinc or
copper.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 165
DISULFID 55 71
DISULFID 137 239
DISULFID 144 211
DISULFID 176 190
DISULFID 201 226
VAR_SEQ 1 72 Missing (in isoform 2).
{ECO:0000303|PubMed:12738725}.
/FTId=VSP_013581.
MUTAGEN 54 54 H->F: No effect on zinc inhibition.
{ECO:0000269|PubMed:17909180}.
MUTAGEN 109 109 H->A: No zinc inhibition.
{ECO:0000269|PubMed:17909180}.
CONFLICT 226 226 C -> W (in Ref. 9; AAH32005).
{ECO:0000305}.
STRAND 44 49 {ECO:0000244|PDB:2QXI}.
STRAND 52 61 {ECO:0000244|PDB:2QXI}.
STRAND 64 67 {ECO:0000244|PDB:2QXI}.
HELIX 69 71 {ECO:0000244|PDB:2QXI}.
STRAND 76 81 {ECO:0000244|PDB:2QXI}.
STRAND 90 95 {ECO:0000244|PDB:2QXI}.
STRAND 97 100 {ECO:0000244|PDB:2QXI}.
TURN 106 108 {ECO:0000244|PDB:2QXI}.
STRAND 114 117 {ECO:0000244|PDB:2QXI}.
STRAND 125 127 {ECO:0000244|PDB:5Y9L}.
STRAND 143 150 {ECO:0000244|PDB:2QXI}.
STRAND 152 156 {ECO:0000244|PDB:2QXI}.
STRAND 164 171 {ECO:0000244|PDB:2QXI}.
HELIX 173 180 {ECO:0000244|PDB:2QXI}.
HELIX 181 183 {ECO:0000244|PDB:2QXI}.
STRAND 188 192 {ECO:0000244|PDB:2QXI}.
STRAND 208 211 {ECO:0000244|PDB:2QXI}.
STRAND 214 221 {ECO:0000244|PDB:2QXI}.
STRAND 224 226 {ECO:0000244|PDB:2QXI}.
STRAND 233 237 {ECO:0000244|PDB:2QXI}.
HELIX 238 240 {ECO:0000244|PDB:2QXI}.
HELIX 242 251 {ECO:0000244|PDB:2QXI}.
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


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U0690h CLIA hK8,Homo sapiens,Human,Kallikrein-8,KLK8,Neuropsin,NP,NRPN,Ovasin,PRSS19,Serine protease 19,Serine protease TADG-14,TADG14,Tumor-associated differentially expressed gene 14 protein,UNQ283_PRO322 96T
E0690h ELISA kit hK8,Homo sapiens,Human,Kallikrein-8,KLK8,Neuropsin,NP,NRPN,Ovasin,PRSS19,Serine protease 19,Serine protease TADG-14,TADG14,Tumor-associated differentially expressed gene 14 protein,UNQ283_P 96T
E0690h ELISA hK8,Homo sapiens,Human,Kallikrein-8,KLK8,Neuropsin,NP,NRPN,Ovasin,PRSS19,Serine protease 19,Serine protease TADG-14,TADG14,Tumor-associated differentially expressed gene 14 protein,UNQ283_PRO322 96T


 

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