ID   GRAM_RAT                Reviewed;         258 AA.
AC   Q03238;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Granzyme M;
DE            EC=3.4.21.-;
DE   AltName: Full=Met-ase;
DE   AltName: Full=Natural killer cell granular protease;
DE   AltName: Full=RNK-Met-1;
DE   Flags: Precursor; Fragment;
GN   Name=Gzmm;
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 21-44.
RX   PubMed=1447189; DOI=10.1016/s0021-9258(18)35783-1;
RA   Smyth M.J., Wiltrout T., Trapani J.A., Ottaway K.S., Sowder R.,
RA   Henderson L.E., Kam C.-M., Powers J.C., Young H.A., Sayers T.J.;
RT   "Purification and cloning of a novel serine protease, RNK-Met-1, from the
RT   granules of a rat natural killer cell leukemia.";
RL   J. Biol. Chem. 267:24418-24425(1992).
CC   -!- FUNCTION: Cleaves peptide substrates after methionine, leucine, and
CC       norleucine. Physiological substrates include EZR, alpha-tubulins and
CC       the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and
CC       subsequent apoptosis of target cells (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Granules of
CC       large granular lymphocytes.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; L05175; AAA42056.1; -; mRNA.
DR   PIR; A45161; A45161.
DR   AlphaFoldDB; Q03238; -.
DR   SMR; Q03238; -.
DR   IntAct; Q03238; 1.
DR   STRING; 10116.ENSRNOP00000011086; -.
DR   MEROPS; S01.139; -.
DR   GlyGen; Q03238; 2 sites.
DR   PaxDb; Q03238; -.
DR   UCSC; RGD:620022; rat.
DR   RGD; 620022; Gzmm.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; Q03238; -.
DR   PhylomeDB; Q03238; -.
DR   BRENDA; 3.4.21.B2; 5301.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0008219; P:cell death; ISO:RGD.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0001913; P:T cell mediated cytotoxicity; ISO:RGD.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR033040; GZMM.
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:SF51; PTHR24271:SF51; 1.
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   Apoptosis; Cytolysis; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Immunity; Innate immunity; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          <1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..20
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:1447189"
FT                   /id="PRO_0000027423"
FT   CHAIN           21..258
FT                   /note="Granzyme M"
FT                   /id="PRO_0000027424"
FT   DOMAIN          21..250
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          122..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        61
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        107
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        142..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        173..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        200..226
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         1
SQ   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