K1B16_MOUSE
ID K1B16_MOUSE Reviewed; 261 AA.
AC P04071;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Kallikrein 1-related peptidase b16;
DE EC=3.4.21.54;
DE AltName: Full=Gamma-renin, submandibular gland;
DE AltName: Full=Glandular kallikrein K16;
DE Short=mGK-16;
DE Flags: Precursor;
GN Name=Klk1b16; Synonyms=Klk-16, Klk16;
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].
RX PubMed=3288617; DOI=10.1016/s0021-9258(18)68341-3;
RA Drinkwater C.C., Evans B.A., Richards R.I.;
RT "Sequence and expression of mouse gamma-renin.";
RL J. Biol. Chem. 263:8565-8568(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-54 AND 70-122.
RX PubMed=3036794; DOI=10.1016/s0021-9258(18)47521-7;
RA Evans B.A., Drinkwater C.C., Richards R.I.;
RT "Mouse glandular kallikrein genes. Structure and partial sequence analysis
RT of the kallikrein gene locus.";
RL J. Biol. Chem. 262:8027-8034(1987).
RN [4]
RP PROTEIN SEQUENCE OF 25-64 AND 165-184.
RC STRAIN=Swiss Webster;
RX PubMed=6337154; DOI=10.1016/s0021-9258(18)32909-0;
RA Poe M., Wu J.K., Florance J.R., Rodkey J.A., Bennett C.D., Hoogsteen K.;
RT "Purification and properties of renin and gamma-renin from the mouse
RT submaxillary gland.";
RL J. Biol. Chem. 258:2209-2216(1983).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of the Leu-|-Leu bond in synthetic tetradecapeptide
CC renin substrate, to produce angiotensin I, but not active on natural
CC angiotensinogen. Also hydrolyzes Bz-Arg-p-nitroanilide.;
CC EC=3.4.21.54;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; J03877; AAA40049.1; -; mRNA.
DR EMBL; BC012237; AAH12237.1; -; mRNA.
DR EMBL; M18594; AAA39357.1; -; Genomic_DNA.
DR EMBL; M18615; AAA39358.1; -; Genomic_DNA.
DR CCDS; CCDS21197.1; -.
DR PIR; A28062; A28062.
DR RefSeq; NP_032480.1; NM_008454.3.
DR AlphaFoldDB; P04071; -.
DR SMR; P04071; -.
DR STRING; 10090.ENSMUSP00000005933; -.
DR MEROPS; S01.163; -.
DR GlyGen; P04071; 1 site.
DR MaxQB; P04071; -.
DR PaxDb; P04071; -.
DR PRIDE; P04071; -.
DR ProteomicsDB; 268929; -.
DR DNASU; 16615; -.
DR Ensembl; ENSMUST00000005933; ENSMUSP00000005933; ENSMUSG00000038968.
DR GeneID; 16615; -.
DR KEGG; mmu:16615; -.
DR UCSC; uc009goj.1; mouse.
DR CTD; 16615; -.
DR MGI; MGI:891982; Klk1b16.
DR VEuPathDB; HostDB:ENSMUSG00000038968; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P04071; -.
DR OMA; KWIKETI; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P04071; -.
DR TreeFam; TF331065; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 16615; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Klk1b16; mouse.
DR PRO; PR:P04071; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P04071; protein.
DR Bgee; ENSMUSG00000038968; Expressed in submandibular gland and 12 other tissues.
DR ExpressionAtlas; P04071; baseline and differential.
DR Genevisible; P04071; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:6337154"
FT /id="PRO_0000027985"
FT CHAIN 25..261
FT /note="Kallikrein 1-related peptidase b16"
FT /id="PRO_0000027986"
FT DOMAIN 25..258
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
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 213
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 152..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 184..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 209..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 45
FT /note="H -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48..49
FT /note="HI -> YL (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 28722 MW; 53D8984BF41E0F3D CRC64;
MWFLILFLAL SLGGIDAAPP VQSRIVGGFK CEKNSQPWQV AVYYHKEHIC GGVLLDRNWV
LTAAHCYVDE CEVWLGKNQL FQEEPSAQNR LVSKSFPHPG FNMTLLTFEK LPPGADFSND
LMLLRLSKPA DITDVVKPID LPTKEPKLDS TCLVSGWGSI TPTKWQKPDD LQCMFTKLLP
NENCAKAYLL KVTDVMLCTI EMGEDKGPCV GDSGGPLICD GVLQGTVSIG PDPCGIPGVS
AIYTNLVKFN SWIKDTMMKN A
