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   24-JAN-2024, entry version 153.
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; 10090-ENSMUSP00000032955; -.
DR   ProteomicsDB; 264853; -.
DR   Antibodypedia; 18939; 451 antibodies from 32 providers.
DR   DNASU; 23993; -.
DR   Ensembl; ENSMUST00000032955.7; ENSMUSP00000032955.6; ENSMUSG00000030713.7.
DR   GeneID; 23993; -.
DR   KEGG; mmu:23993; -.
DR   UCSC; uc009gnt.1; mouse.
DR   AGR; MGI:1346336; -.
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; 4629979at2759; -.
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 77 CRISPR screens.
DR   PRO; PR:Q91VE3; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q91VE3; Protein.
DR   Bgee; ENSMUSG00000030713; Expressed in tail skin and 51 other cell types or tissues.
DR   ExpressionAtlas; Q91VE3; baseline and differential.
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; Trypsin-like serine proteases; 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   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.
DR   Genevisible; Q91VE3; MM.
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
//