ID KLK1_RAT Reviewed; 261 AA.
AC P00758; Q68G17;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 24-JAN-2024, entry version 158.
DE RecName: Full=Kallikrein-1;
DE EC=3.4.21.35;
DE AltName: Full=Gamma-NGF;
DE AltName: Full=Nerve growth factor gamma chain;
DE AltName: Full=PS kallikrein;
DE AltName: Full=Pancreatic kallikrein;
DE AltName: Full=RGK-1;
DE Short=rK-1;
DE AltName: Full=Tissue kallikrein;
DE AltName: Full=True tissue kallikrein;
DE Short=True kallikrein;
DE Contains:
DE RecName: Full=Nerve growth factor gamma chain 1;
DE Contains:
DE RecName: Full=Nerve growth factor gamma chain 2;
DE Flags: Precursor;
GN Name=Ngfg; Synonyms=Klk-1, Klk1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=6961406; DOI=10.1073/pnas.79.23.7263;
RA Swift G.H., Dagorn J.-C., Ashley P.L., Cummings S.W., MacDonald R.J.;
RT "Rat pancreatic kallikrein mRNA: nucleotide sequence and amino acid
RT sequence of the encoded preproenzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:7263-7267(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Submandibular gland;
RX PubMed=2998455; DOI=10.1021/bi00338a005;
RA Ashley P.L., MacDonald R.J.;
RT "Kallikrein-related mRNAs of the rat submaxillary gland: nucleotide
RT sequences of four distinct types including tonin.";
RL Biochemistry 24:4512-4520(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Kidney;
RX PubMed=2753879; DOI=10.1093/oxfordjournals.jbchem.a122754;
RA Inoue H., Fukui K., Miyake Y.;
RT "Identification and structure of the rat true tissue kallikrein gene
RT expressed in the kidney.";
RL J. Biochem. 105:834-840(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2708383; DOI=10.1016/s0021-9258(18)83284-7;
RA Wines D.R., Brady J.M., Pritchett D.B., Roberts J.L., MacDonald R.J.;
RT "Organization and expression of the rat kallikrein gene family.";
RL J. Biol. Chem. 264:7653-7662(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-261.
RC TISSUE=Submandibular gland;
RX PubMed=3004582; DOI=10.1016/0167-4781(86)90093-x;
RA Gerald W.L., Chao J., Chao L.;
RT "Immunological identification of rat tissue kallikrein cDNA and
RT characterization of the kallikrein gene family.";
RL Biochim. Biophys. Acta 866:1-14(1986).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule
CC substrates. Highly selective action to release kallidin (lysyl-
CC bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-
CC Xaa.; EC=3.4.21.35;
CC -!- TISSUE SPECIFICITY: High levels in pancreas, submaxillary and parotid
CC glands, spleen, and kidney. {ECO:0000269|PubMed:6961406}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41464.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH78784.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA00346.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J00758; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M11563; AAA41464.1; ALT_INIT; mRNA.
DR EMBL; D00448; BAA00346.1; ALT_INIT; Genomic_DNA.
DR EMBL; M23876; AAA41462.1; -; Genomic_DNA.
DR EMBL; M23874; AAA41462.1; JOINED; Genomic_DNA.
DR EMBL; M23875; AAA41462.1; JOINED; Genomic_DNA.
DR EMBL; BC078784; AAH78784.1; ALT_INIT; mRNA.
DR EMBL; X03560; CAA27247.1; -; mRNA.
DR PIR; A00944; KQRTP.
DR RefSeq; NP_113711.1; NM_031523.1.
DR AlphaFoldDB; P00758; -.
DR SMR; P00758; -.
DR IntAct; P00758; 3.
DR MEROPS; S01.405; -.
DR GlyCosmos; P00758; 1 site, No reported glycans.
DR GlyGen; P00758; 1 site.
DR PaxDb; 10116-ENSRNOP00000025831; -.
DR GeneID; 24594; -.
DR KEGG; rno:24594; -.
DR UCSC; RGD:3175; rat.
DR AGR; RGD:3175; -.
DR CTD; 18050; -.
DR RGD; 3175; Ngfg.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P00758; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; P00758; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.35; 5301.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR PRO; PR:P00758; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; 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:SF47; KALLIKREIN-1; 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 Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000027999"
FT CHAIN 25..261
FT /note="Kallikrein-1"
FT /id="PRO_0000028000"
FT CHAIN 25..111
FT /note="Nerve growth factor gamma chain 1"
FT /id="PRO_0000028001"
FT CHAIN 112..261
FT /note="Nerve growth factor gamma chain 2"
FT /id="PRO_0000028002"
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 ACT_SITE 120
FT /note="Charge relay system"
FT ACT_SITE 213
FT /note="Charge relay system"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
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"
SQ SEQUENCE 261 AA; 28852 MW; F2F99C0227A7882B CRC64;
MWFLILFLAL SLGRNDAAPP VQSRVVGGYN CEMNSQPWQV AVYYFGEYLC GGVLIDPSWV
ITAAHCATDN YQVWLGRNNL YEDEPFAQHR LVSQSFPHPG FNQDLIWNHT RQPGDDYSND
LMLLHLSQPA DITDGVKVID LPIEEPKVGS TCLASGWGSI TPDGLELSDD LQCVNIDLLS
NEKCVEAHKE EVTDLMLCAG EMDGGKDTCK GDSGGPLICN GVLQGITSWG FNPCGEPKKP
GIYTKLIKFT PWIKEVMKEN P
//
