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Granzyme M (EC 3.4.21.-) (Met-ase) (Natural killer cell granular protease) (RNK-Met-1) (Fragment)

 GRAM_RAT                Reviewed;         258 AA.
Q03238;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
10-MAY-2017, entry version 115.
RecName: Full=Granzyme M;
EC=3.4.21.-;
AltName: Full=Met-ase;
AltName: Full=Natural killer cell granular protease;
AltName: Full=RNK-Met-1;
Flags: Precursor; Fragment;
Name=Gzmm;
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 21-44.
PubMed=1447189;
Smyth M.J., Wiltrout T., Trapani J.A., Ottaway K.S., Sowder R.,
Henderson L.E., Kam C.-M., Powers J.C., Young H.A., Sayers T.J.;
"Purification and cloning of a novel serine protease, RNK-Met-1, from
the granules of a rat natural killer cell leukemia.";
J. Biol. Chem. 267:24418-24425(1992).
-!- FUNCTION: Cleaves peptide substrates after methionine, leucine,
and norleucine. Physiological substrates include EZR, alpha-
tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes
caspase activation and subsequent apoptosis of target cells (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Granules
of large granular lymphocytes.
-!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; L05175; AAA42056.1; -; mRNA.
PIR; A45161; A45161.
UniGene; Rn.9838; -.
ProteinModelPortal; Q03238; -.
SMR; Q03238; -.
IntAct; Q03238; 1.
STRING; 10116.ENSRNOP00000011086; -.
MEROPS; S01.139; -.
PaxDb; Q03238; -.
PRIDE; Q03238; -.
UCSC; RGD:620022; rat.
RGD; 620022; Gzmm.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q03238; -.
PhylomeDB; Q03238; -.
BRENDA; 3.4.21.B2; 5301.
Proteomes; UP000002494; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IDA:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR033040; GZMM.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24256:SF361; PTHR24256:SF361; 1.
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;
Apoptosis; Complete proteome; Cytolysis; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
Protease; Reference proteome; Secreted; Serine protease; Signal;
Zymogen.
SIGNAL <1 ? {ECO:0000255}.
PROPEP ? 20 Activation peptide.
{ECO:0000269|PubMed:1447189}.
/FTId=PRO_0000027423.
CHAIN 21 258 Granzyme M.
/FTId=PRO_0000027424.
DOMAIN 21 250 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 61 61 Charge relay system. {ECO:0000250}.
ACT_SITE 107 107 Charge relay system. {ECO:0000250}.
ACT_SITE 204 204 Charge relay system. {ECO:0000250}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 46 62 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 142 210 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 173 189 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 200 226 {ECO:0000255|PROSITE-ProRule:PRU00274}.
NON_TER 1 1
SEQUENCE 258 AA; 28339 MW; B89DC10EF54DF495 CRC64;
LLLLLALKTL WAVGNRFEAQ IIGGREAVPH SRPYMVSLQN TKSHMCGGVL VHQKWVLTAA
HCLSEPLQQL KLVFGLHSLH DPQDPGLTFY IKQAIKHPGY NLKYENDLAL LKLDGRVKPS
KNVKPLALPR KPRDKPAEGS RCSTAGWGIT HQRGQLAKSL QELDLRLLDT RMCNNSRFWN
GVLTDSMLCL KAGAKGQAPC KGDSGGPLVC GKGKVDGILS FSSKNCTDIF KPTVATAVAP
YSSWIRKVIG RWSPQPLT


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