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Granzyme K (EC 3.4.21.-) (NK-tryptase-2) (NK-Tryp-2)

 GRAK_RAT                Reviewed;         258 AA.
P49864;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-MAY-2017, entry version 111.
RecName: Full=Granzyme K;
EC=3.4.21.-;
AltName: Full=NK-tryptase-2;
Short=NK-Tryp-2;
Flags: Precursor;
Name=Gzmk;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 26-58.
STRAIN=Fischer 344; TISSUE=Lymphocyte;
PubMed=8133042;
Sayers T.J., Wiltrout T.A., Smyth M.J., Ottaway K.S., Pilaro A.M.,
Sowder R., Henderson L.E., Sprenger H., Lloyd A.R.;
"Purification and cloning of a novel serine protease, RNK-Tryp-2, from
the granules of a rat NK cell leukemia.";
J. Immunol. 152:2289-2297(1994).
-!- SUBCELLULAR LOCATION: Cytoplasmic granule.
-!- TISSUE SPECIFICITY: Speen, lungs and liver non-parenchymal cells.
-!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; L19694; AAA42057.1; -; mRNA.
PIR; I56220; I56220.
RefSeq; NP_058815.1; NM_017119.2.
UniGene; Rn.11190; -.
ProteinModelPortal; P49864; -.
SMR; P49864; -.
IntAct; P49864; 1.
STRING; 10116.ENSRNOP00000014319; -.
ChEMBL; CHEMBL4557; -.
MEROPS; S01.146; -.
PaxDb; P49864; -.
PRIDE; P49864; -.
GeneID; 29165; -.
KEGG; rno:29165; -.
CTD; 3003; -.
RGD; 68401; Gzmk.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P49864; -.
KO; K08663; -.
PhylomeDB; P49864; -.
PRO; PR:P49864; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IDA:RGD.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Hydrolase; Protease; Reference proteome; Serine protease; Signal;
Zymogen.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 25 Activation peptide.
{ECO:0000269|PubMed:8133042}.
/FTId=PRO_0000027419.
CHAIN 26 258 Granzyme K.
/FTId=PRO_0000027420.
DOMAIN 26 253 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 66 66 Charge relay system. {ECO:0000250}.
ACT_SITE 110 110 Charge relay system. {ECO:0000250}.
ACT_SITE 208 208 Charge relay system. {ECO:0000250}.
DISULFID 51 67 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 143 214 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 175 193 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 204 228 {ECO:0000255|PROSITE-ProRule:PRU00274}.
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


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