ID   GRAK_RAT                Reviewed;         258 AA.
AC   P49864;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 130.
DE   RecName: Full=Granzyme K;
DE            EC=3.4.21.-;
DE   AltName: Full=NK-tryptase-2;
DE            Short=NK-Tryp-2;
DE   Flags: Precursor;
GN   Name=Gzmk;
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 PROTEIN SEQUENCE OF 26-58.
RC   STRAIN=Fischer 344; TISSUE=Lymphocyte;
RX   PubMed=8133042;
RA   Sayers T.J., Wiltrout T.A., Smyth M.J., Ottaway K.S., Pilaro A.M.,
RA   Sowder R., Henderson L.E., Sprenger H., Lloyd A.R.;
RT   "Purification and cloning of a novel serine protease, RNK-Tryp-2, from the
RT   granules of a rat NK cell leukemia.";
RL   J. Immunol. 152:2289-2297(1994).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule.
CC   -!- TISSUE SPECIFICITY: Speen, lungs and liver non-parenchymal cells.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; L19694; AAA42057.1; -; mRNA.
DR   PIR; I56220; I56220.
DR   RefSeq; NP_058815.1; NM_017119.2.
DR   AlphaFoldDB; P49864; -.
DR   SMR; P49864; -.
DR   BioGRID; 247846; 1.
DR   IntAct; P49864; 1.
DR   STRING; 10116.ENSRNOP00000014319; -.
DR   ChEMBL; CHEMBL4557; -.
DR   MEROPS; S01.146; -.
DR   CarbonylDB; P49864; -.
DR   PhosphoSitePlus; P49864; -.
DR   PaxDb; 10116-ENSRNOP00000014319; -.
DR   GeneID; 29165; -.
DR   KEGG; rno:29165; -.
DR   AGR; RGD:68401; -.
DR   CTD; 3003; -.
DR   RGD; 68401; Gzmk.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; P49864; -.
DR   OrthoDB; 2878201at2759; -.
DR   PhylomeDB; P49864; -.
DR   BRENDA; 3.4.21.B4; 5301.
DR   PRO; PR:P49864; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR   GO; GO:0008236; F:serine-type peptidase activity; IDA:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF52; GRANZYME K; 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; Hydrolase; Protease;
KW   Reference proteome; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..25
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:8133042"
FT                   /id="PRO_0000027419"
FT   CHAIN           26..258
FT                   /note="Granzyme K"
FT                   /id="PRO_0000027420"
FT   DOMAIN          26..253
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        66
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        208
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        143..214
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        175..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        204..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   258 AA;  28465 MW;  988AD71DB08AFBB4 CRC64;
     MSFSSSALVF LVAGIYMSSE SFHTEIIGGR EVQPHSRPFM ASIQYRGKHI CGGVLIHPQW
     VLTAAHCYSR GHSPTVVLGA HSLSKNEPMK QTFEIKEFIP FSGFKSGTND IMLIKLRTAA
     ELNKHVQLLH LRSKNYIRDG TKCQVTGWGS TKPDVLTTSD TLQEVTVTII SRKRCNSQSY
     YNHKPVITKD MICAGDRRGE KDSCKGDSGG PLICKGVFHA LVSGGYKCGI SNKPGVYTLL
     TKKYQTWIKS KLAPSSAH
//