ID   KLK8_RAT                Reviewed;         260 AA.
AC   O88780;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Kallikrein-8;
DE            EC=3.4.21.118;
DE   AltName: Full=Brain serine protease 1;
DE   AltName: Full=Neuropsin;
DE            Short=NP;
DE   AltName: Full=Serine protease 19;
DE   Flags: Precursor;
GN   Name=Klk8; Synonyms=Bsp1, Nrpn, Prss19;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Fischer; TISSUE=Brain;
RX   PubMed=9722524; DOI=10.1074/jbc.273.36.23004;
RA   Davies B.J., Pickard B.S., Steel M., Morris R.G.M., Lathe R.;
RT   "Serine proteases in rodent hippocampus.";
RL   J. Biol. Chem. 273:23004-23011(1998).
CC   -!- FUNCTION: Serine protease which is capable of degrading a number of
CC       proteins such as casein, fibrinogen, kininogen, fibronectin and
CC       collagen type IV. Also cleaves L1CAM in response to increased neural
CC       activity. Induces neurite outgrowth and fasciculation of cultured
CC       hippocampal neurons. Plays a role in the formation and maturation of
CC       orphan and small synaptic boutons in the Schaffer-collateral pathway,
CC       regulates Schaffer-collateral long-term potentiation in the hippocampus
CC       and is required for memory acquisition and synaptic plasticity.
CC       Involved in skin desquamation and keratinocyte proliferation. Plays a
CC       role in the secondary phase of pathogenesis following spinal cord
CC       injury (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of amide substrates following the basic amino acids
CC         Arg or Lys at the P1 position, with a preference for Arg over Lys.;
CC         EC=3.4.21.118;
CC   -!- SUBUNIT: Interacts with SPINK9. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Shows a cytoplasmic distribution in the keratinocytes.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Restricted to hippocampus.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AJ005641; CAA06643.1; -; mRNA.
DR   AlphaFoldDB; O88780; -.
DR   SMR; O88780; -.
DR   STRING; 10116.ENSRNOP00000025174; -.
DR   MEROPS; S01.244; -.
DR   CarbonylDB; O88780; -.
DR   GlyCosmos; O88780; 1 site, No reported glycans.
DR   GlyGen; O88780; 1 site.
DR   PhosphoSitePlus; O88780; -.
DR   PaxDb; 10116-ENSRNOP00000025174; -.
DR   UCSC; RGD:1305998; rat.
DR   AGR; RGD:1305998; -.
DR   RGD; 1305998; Klk8.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; O88780; -.
DR   PhylomeDB; O88780; -.
DR   BRENDA; 3.4.21.118; 5301.
DR   Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR   PRO; PR:O88780; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0097180; C:serine protease inhibitor complex; ISO:RGD.
DR   GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0043616; P:keratinocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0007613; P:memory; ISS:UniProtKB.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050807; P:regulation of synapse organization; ISS:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR   GO; GO:0050808; P:synapse organization; ISO:RGD.
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:SF62; KALLIKREIN-8; 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   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..32
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027950"
FT   CHAIN           33..260
FT                   /note="Kallikrein-8"
FT                   /id="PRO_0000027951"
FT   DOMAIN          33..257
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        73
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        212
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        39..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        58..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        145..246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        152..218
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        184..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        208..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   260 AA;  28510 MW;  58DF4F0602A0B7F5 CRC64;
     MGRPPPCAIQ TWILLFLLMG AWAGLTRAQG SKILEGQECK PHSQPWQTAL FQGERLVCGG
     VLVGDRWVLT AAHCKKDKYS VRLGDHSLQK RDEPEQEIQV ARSIQHPCFN SSNPEDHSHD
     IMLIRLQNSA NLGDKVKPIE LANLCPKVGQ KCIISGWGTV TSPQENFPNT LNCAEVKIYS
     QNKCERAYPG KITEGMVCAG SSNGADTCQG DSGGPLVCNG VLQGITTWGS DPCGKPEKPG
     VYTKICRYTN WIKKTMGKRD
//