ID   K1KB8_MOUSE             Reviewed;         261 AA.
AC   P07628;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   26-MAY-2009, entry version 77.
DE   RecName: Full=Kallikrein 1-related peptidase b8;
DE            EC=3.4.21.35;
DE   AltName: Full=Glandular kallikrein K8;
DE            Short=mGK-8;
DE   AltName: Full=Tissue kallikrein-8;
DE   Flags: Precursor;
GN   Name=Klk1b8; Synonyms=Klk-8, Klk8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86259061; PubMed=3636812; DOI=10.1093/nar/14.12.4823;
RA   Fahnestock M., Brundage S., Shooter E.M.;
RT   "The sequence of a cDNA clone coding for a novel kallikrein from mouse
RT   submaxillary gland.";
RL   Nucleic Acids Res. 14:4823-4835(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 16-54 AND 70-122.
RX   MEDLINE=87250386; PubMed=3036794;
RA   Evans B.A., Drinkwater C.C., Richards R.I.;
RT   "Mouse glandular kallikrein genes. Structure and partial sequence
RT   analysis of the kallikrein gene locus.";
RL   J. Biol. Chem. 262:8027-8034(1987).
CC   -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds
CC       in kininogen to release Lys-bradykinin.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage of Arg-|-Xaa bonds in
CC       small molecule substrates. Highly selective action to release
CC       kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of
CC       Met-|-Xaa or Leu-|-Xaa.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   EMBL; X03994; CAA27630.1; -; mRNA.
DR   EMBL; M18587; AAA39347.1; -; Genomic_DNA.
DR   EMBL; M18607; AAA39348.1; -; Genomic_DNA.
DR   IPI; IPI00130801; -.
DR   PIR; A24378; A24378.
DR   RefSeq; NP_032483.1; -.
DR   UniGene; Mm.435488; -.
DR   HSSP; P36368; 1AO5.
DR   SMR; P07628; 25-261.
DR   PRIDE; P07628; -.
DR   Ensembl; ENSMUSG00000063089; Mus musculus.
DR   GeneID; 16624; -.
DR   KEGG; mmu:16624; -.
DR   MGI; MGI:892018; Klk1b8.
DR   HOVERGEN; P07628; -.
DR   BRENDA; 3.4.21.118; 244.
DR   BRENDA; 3.4.21.35; 244.
DR   NextBio; 290239; -.
DR   ArrayExpress; P07628; -.
DR   Bgee; P07628; -.
DR   CleanEx; MM_KLK1B8; -.
DR   CleanEx; MM_KLK8; -.
DR   GermOnline; ENSMUSG00000063089; Mus musculus.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 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   Disulfide bond; Glycoprotein; Hydrolase; Protease; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL        1     18       Probable.
FT   PROPEP       19     24       Activation peptide (Probable).
FT                                /FTId=PRO_0000027977.
FT   CHAIN        25    261       Kallikrein 1-related peptidase b8.
FT                                /FTId=PRO_0000027978.
FT   DOMAIN       25    258       Peptidase S1.
FT   ACT_SITE     65     65       Charge relay system.
FT   ACT_SITE    120    120       Charge relay system.
FT   ACT_SITE    213    213       Charge relay system.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Probable).
FT   DISULFID     31    173       By similarity.
FT   DISULFID     50     66       By similarity.
FT   DISULFID    152    219       By similarity.
FT   DISULFID    184    198       By similarity.
FT   DISULFID    209    234       By similarity.
SQ   SEQUENCE   261 AA;  28531 MW;  D0174F7093137322 CRC64;
     MRFLILFLAL SLGGIDAAPP LQSRVVGGFN CEKNSQPWQV AVYDNKEHIC GGVLLERNWV
     LTAAHCYVDQ YEVWLGKNKL FQEEPSAQHR LVSKSFPHPG FNMSLLTLKE IPPGADFSND
     LMLLRLSKPA DITDAVKPIT LPTKESKLGS TCLASGWGSI TPTKWQKPDD LQCVFLKLLP
     IKNCIENHNV KVTDVMLCAG EMSGGKNICK GDSGGPLICD SVLQGITSTG PIPCGKPGVP
     AMYTNLIKFN SWIKDTMTKN S
//