KLK8_RAT
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 03-AUG-2022, entry version 126.
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 GlyGen; O88780; 1 site.
DR PaxDb; O88780; -.
DR UCSC; RGD:1305998; rat.
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:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0043616; P:keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
DR GO; GO:0031642; P:negative regulation of myelination; 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; -; 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 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
