KLK7_MOUSE
ID KLK7_MOUSE Reviewed; 249 AA.
AC Q91VE3; Q9R048;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Kallikrein-7;
DE EC=3.4.21.117;
DE AltName: Full=Serine protease 6;
DE AltName: Full=Stratum corneum chymotryptic enzyme;
DE AltName: Full=Thymopsin;
DE Flags: Precursor;
GN Name=Klk7; Synonyms=Prss6, Scce;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RA Yamaguchi N.;
RT "A novel cDNA cloning of mouse serine protease, thymopsin.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Hansson L., Baeckman A., Ny A., Edlund M., Edholm E., Tornell J.,
RA Wallbrandt P., Egelrud T.;
RT "Epidermal overexpression of stratum corneum chymotryptic enzyme in mice; a
RT model for chronic ithchy dermatitis.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-234, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Tail;
RX PubMed=10469296; DOI=10.1046/j.1523-1747.1999.00662.x;
RA Baeckman A., Stranden P., Brattsand M., Hansson L., Egelrud T.;
RT "Molecular cloning and tissue expression of the murine analog to human
RT stratum corneum chymotryptic enzyme.";
RL J. Invest. Dermatol. 113:152-155(1999).
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in skin and, at lower levels, in lung,
CC kidney, brain, heart and spleen. In skin, expressed in high suprabasal
CC keratinocytes and in the luminal parts of hair follicles. Not detected
CC in liver and skeletal muscle. {ECO:0000269|PubMed:10469296}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AB008371; BAB55604.1; -; mRNA.
DR EMBL; AF339930; AAK69652.1; -; Genomic_DNA.
DR EMBL; AK029477; BAC26467.1; -; mRNA.
DR EMBL; AK077406; BAC36787.1; -; mRNA.
DR EMBL; BC027823; AAH27823.1; -; mRNA.
DR EMBL; AF124299; AAF01139.1; -; mRNA.
DR CCDS; CCDS21183.1; -.
DR RefSeq; NP_036002.1; NM_011872.3.
DR PDB; 5ZFH; X-ray; 1.93 A; A=26-249.
DR PDB; 5ZFI; X-ray; 1.80 A; A=26-249.
DR PDB; 6AHS; X-ray; 1.75 A; A=26-249.
DR PDBsum; 5ZFH; -.
DR PDBsum; 5ZFI; -.
DR PDBsum; 6AHS; -.
DR AlphaFoldDB; Q91VE3; -.
DR SMR; Q91VE3; -.
DR STRING; 10090.ENSMUSP00000032955; -.
DR BindingDB; Q91VE3; -.
DR ChEMBL; CHEMBL4295910; -.
DR MEROPS; S01.300; -.
DR PhosphoSitePlus; Q91VE3; -.
DR PaxDb; Q91VE3; -.
DR PRIDE; Q91VE3; -.
DR ProteomicsDB; 264853; -.
DR Antibodypedia; 18939; 410 antibodies from 32 providers.
DR DNASU; 23993; -.
DR Ensembl; ENSMUST00000032955; ENSMUSP00000032955; ENSMUSG00000030713.
DR GeneID; 23993; -.
DR KEGG; mmu:23993; -.
DR UCSC; uc009gnt.1; mouse.
DR CTD; 5650; -.
DR MGI; MGI:1346336; Klk7.
DR VEuPathDB; HostDB:ENSMUSG00000030713; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; Q91VE3; -.
DR OMA; YSTKTHA; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q91VE3; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.117; 3474.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 23993; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q91VE3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91VE3; protein.
DR Bgee; ENSMUSG00000030713; Expressed in tail skin and 48 other tissues.
DR ExpressionAtlas; Q91VE3; baseline and differential.
DR Genevisible; Q91VE3; MM.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0097209; C:epidermal lamellar body; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0002803; P:positive regulation of antibacterial peptide production; ISO:MGI.
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; Disulfide bond; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..25
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027944"
FT CHAIN 26..249
FT /note="Kallikrein-7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027945"
FT REGION 26..246
FT /note="Serine protease"
FT /evidence="ECO:0000250"
FT ACT_SITE 66
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 105
FT /note="Major binding site for inhibitory zinc or copper"
FT /evidence="ECO:0000250"
FT DISULFID 32..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 51..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 133..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 140..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 172..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 197..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 215..217
FT /note="VSW -> ASR (in Ref. 5; AAF01139)"
FT /evidence="ECO:0000305"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6AHS"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:6AHS"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:6AHS"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:6AHS"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6AHS"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:6AHS"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6AHS"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:6AHS"
SQ SEQUENCE 249 AA; 27257 MW; 0D4E380F12D14F87 CRC64;
MGVWLLSLIT VLLSLALETA GQGERIIDGY KCKEGSHPWQ VALLKGNQLH CGGVLVDKYW
VLTAAHCKMG QYQVQLGSDK IGDQSAQKIK ATKSFRHPGY STKTHVNDIM LVRLDEPVKM
SSKVEAVQLP EHCEPPGTSC TVSGWGTTTS PDVTFPSDLM CSDVKLISSR ECKKVYKDLL
GKTMLCAGIP DSKTNTCNGD SGGPLVCNDT LQGLVSWGTY PCGQPNDPGV YTQVCKYKRW
VMETMKTHR
