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 24-JAN-2024, entry version 143.
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 MEROPS; S01.406; -.
DR GlyCosmos; P36373; 1 site, No reported glycans.
DR GlyGen; P36373; 1 site.
DR iPTMnet; P36373; -.
DR PhosphoSitePlus; P36373; -.
DR PaxDb; 10116-ENSRNOP00000066004; -.
DR GeneID; 24523; -.
DR KEGG; rno:24523; -.
DR UCSC; RGD:1306420; rat.
DR AGR; RGD:2969; -.
DR CTD; 3816; -.
DR RGD; 1306420; Klk7.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P36373; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; P36373; -.
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; 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 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
//
