ID   KLK7_RAT                Reviewed;         261 AA.
AC   P36373;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Glandular kallikrein-7, submandibular/renal;
DE            Short=rGK-7;
DE            EC=3.4.21.35;
DE   AltName: Full=Esterase B;
DE   AltName: Full=Kallikrein-related protein K1;
DE   AltName: Full=Proteinase A;
DE   AltName: Full=RSKG-7;
DE   AltName: Full=Tissue kallikrein;
DE   Flags: Precursor;
GN   Name=Klk7; Synonyms=Klk-7;
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 [GENOMIC DNA].
RX   PubMed=2849988; DOI=10.1021/bi00419a005;
RA   Chen Y.-P., Chao J., Chao L.;
RT   "Molecular cloning and characterization of two rat renal kallikrein
RT   genes.";
RL   Biochemistry 27:7189-7196(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-75.
RC   TISSUE=Submandibular gland;
RX   PubMed=3482210; DOI=10.1093/oxfordjournals.jbchem.a122185;
RA   Kato H., Nakanishi E., Enjyoji K., Hayashi I., Oh-Ishi S., Iwanaga S.;
RT   "Characterization of serine proteinases isolated from rat submaxillary
RT   gland: with special reference to the degradation of rat kininogens by these
RT   enzymes.";
RL   J. Biochem. 102:1389-1404(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-36.
RC   TISSUE=Submandibular gland;
RX   PubMed=2194829; DOI=10.1016/0014-5793(90)80903-v;
RA   Elmoujahed A., Gutman N., Brillard M., Gauthier F.;
RT   "Substrate specificity of two kallikrein family gene products isolated from
RT   the rat submaxillary gland.";
RL   FEBS Lett. 265:137-140(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 43-261, AND TISSUE SPECIFICITY.
RX   PubMed=2183721; DOI=10.1016/0003-9861(90)90269-5;
RA   Brady J.M., MacDonald R.J.;
RT   "The expression of two kallikrein gene family members in the rat kidney.";
RL   Arch. Biochem. Biophys. 278:342-349(1990).
CC   -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in
CC       kininogen to release Lys-bradykinin. Predominant kallikrein protein in
CC       the kidney.
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: Kidney and submandibular gland. Not expressed in
CC       liver, pancreas, spleen, parotid, testis, cortex, prostate, ovary and
CC       pituitary. {ECO:0000269|PubMed:2183721}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; M19647; AAA41461.1; -; Genomic_DNA.
DR   PIR; A31136; A31136.
DR   RefSeq; NP_036725.1; NM_012593.1.
DR   AlphaFoldDB; P36373; -.
DR   SMR; P36373; -.
DR   STRING; 10116.ENSRNOP00000066004; -.
DR   MEROPS; S01.406; -.
DR   GlyGen; P36373; 1 site.
DR   iPTMnet; P36373; -.
DR   PhosphoSitePlus; P36373; -.
DR   PaxDb; P36373; -.
DR   PRIDE; P36373; -.
DR   GeneID; 24523; -.
DR   KEGG; rno:24523; -.
DR   UCSC; RGD:1306420; rat.
DR   CTD; 3816; -.
DR   RGD; 1306420; Klk7.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; P36373; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P36373; -.
DR   Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
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:P36373; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR   GO; GO:0097209; C:epidermal lamellar body; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002803; P:positive regulation of antibacterial peptide production; ISO:RGD.
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:0000305|PubMed:2194829,
FT                   ECO:0000305|PubMed:3482210"
FT                   /id="PRO_0000028005"
FT   CHAIN           25..261
FT                   /note="Glandular kallikrein-7, submandibular/renal"
FT                   /id="PRO_0000028006"
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: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        35
FT                   /note="S -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="T -> S (in Ref. 2; AA sequence and 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="D -> A (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  28972 MW;  4FB06C422F25AF16 CRC64;
     MWFLILFLDL SLGQIDAAPP GQSRVIGGYK CEKNSQPWQV ALYSFTKYLC GGVLIDPSWV
     ITAAHCSSNN YQVWLGRNNL LEDEPFAQHR LVSQSFPHPD YKPFLMRNHT RKPGDDHSND
     LMLLHLSQPA DITDGVKVID LPTEEPKVGS TCLASGWGST KPLIWEFPDD LQCVNIHLLS
     NEKCIKAYKE KVTDLMLCAG ELEGGKDTCT GDSGGPLLCD GVLQGITSWG SVPCAKTNMP
     AIYTKLIKFT SWIKEVMKEN P