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

 GRAM_HUMAN              Reviewed;         257 AA.
P51124;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
07-JUN-2017, entry version 143.
RecName: Full=Granzyme M;
EC=3.4.21.-;
AltName: Full=Met-1 serine protease;
Short=Hu-Met-1;
AltName: Full=Met-ase;
AltName: Full=Natural killer cell granular protease;
Flags: Precursor;
Name=GZMM; Synonyms=MET1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-221.
PubMed=8245461;
Smyth M.J., Sayers T.J., Wiltrout T., Powers J.C., Trapani J.A.;
"Met-ase: cloning and distinct chromosomal location of a serine
protease preferentially expressed in human natural killer cells.";
J. Immunol. 151:6195-6205(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-221.
PubMed=7713495; DOI=10.1006/geno.1994.1651;
Pilat D., Fink T.M., Obermaier-Skrobanek B., Zimmer M., Wekerle H.,
Lichter P., Jenne D.E.;
"The human Met-ase gene (GZMM): structure, sequence, and close
physical linkage to the serine protease gene cluster on 19p13.3.";
Genomics 24:445-450(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-221.
TISSUE=Pancreas, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, TISSUE SPECIFICITY, AND SUBSTRATES.
PubMed=18523284; DOI=10.4049/jimmunol.180.12.8184;
Bovenschen N., de Koning P.J., Quadir R., Broekhuizen R., Damen J.M.,
Froelich C.J., Slijper M., Kummer J.A.;
"NK cell protease granzyme M targets alpha-tubulin and disorganizes
the microtubule network.";
J. Immunol. 180:8184-8191(2008).
[6]
FUNCTION.
PubMed=20406824; DOI=10.1074/jbc.M109.083170;
Hu D., Liu S., Shi L., Li C., Wu L., Fan Z.;
"Cleavage of survivin by Granzyme M triggers degradation of the
survivin-X-linked inhibitor of apoptosis protein (XIAP) complex to
free caspase activity leading to cytolysis of target tumor cells.";
J. Biol. Chem. 285:18326-18335(2010).
[7]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 26-257, ACTIVE SITE, AND
DISULFIDE BONDS.
PubMed=19542453; DOI=10.4049/jimmunol.0803088;
Wu L., Wang L., Hua G., Liu K., Yang X., Zhai Y., Bartlam M., Sun F.,
Fan Z.;
"Structural basis for proteolytic specificity of the human apoptosis-
inducing granzyme M.";
J. Immunol. 183:421-429(2009).
-!- 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.
{ECO:0000269|PubMed:18523284, ECO:0000269|PubMed:20406824}.
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Granules
of large granular lymphocytes.
-!- TISSUE SPECIFICITY: Highly and constitutively expressed in
activated natural killer (NK) cells.
{ECO:0000269|PubMed:18523284}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L23134; AAA59582.1; -; mRNA.
EMBL; L36922; AAA57262.1; -; Genomic_DNA.
EMBL; L36936; AAA57257.1; -; Genomic_DNA.
EMBL; AC011556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC025701; AAH25701.1; -; mRNA.
CCDS; CCDS12031.1; -.
PIR; A55634; A55634.
RefSeq; NP_001245280.1; NM_001258351.1.
RefSeq; NP_005308.1; NM_005317.3.
UniGene; Hs.465511; -.
PDB; 1LZP; Model; -; A=26-257.
PDB; 2ZGC; X-ray; 1.96 A; A=26-257.
PDB; 2ZGH; X-ray; 2.17 A; A=26-257.
PDB; 2ZGJ; X-ray; 2.30 A; A=26-257.
PDB; 2ZKS; X-ray; 2.70 A; A=26-257.
PDBsum; 1LZP; -.
PDBsum; 2ZGC; -.
PDBsum; 2ZGH; -.
PDBsum; 2ZGJ; -.
PDBsum; 2ZKS; -.
ProteinModelPortal; P51124; -.
SMR; P51124; -.
BioGrid; 109259; 5.
IntAct; P51124; 1.
STRING; 9606.ENSP00000264553; -.
MEROPS; S01.139; -.
iPTMnet; P51124; -.
PhosphoSitePlus; P51124; -.
BioMuta; GZMM; -.
DMDM; 296434527; -.
PaxDb; P51124; -.
PeptideAtlas; P51124; -.
PRIDE; P51124; -.
DNASU; 3004; -.
Ensembl; ENST00000264553; ENSP00000264553; ENSG00000197540.
GeneID; 3004; -.
KEGG; hsa:3004; -.
UCSC; uc002low.3; human.
CTD; 3004; -.
DisGeNET; 3004; -.
GeneCards; GZMM; -.
HGNC; HGNC:4712; GZMM.
HPA; HPA015624; -.
MIM; 600311; gene.
neXtProt; NX_P51124; -.
OpenTargets; ENSG00000197540; -.
PharmGKB; PA29090; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P51124; -.
KO; K08649; -.
OMA; CNNSRFW; -.
OrthoDB; EOG091G0HUQ; -.
PhylomeDB; P51124; -.
TreeFam; TF335738; -.
BRENDA; 3.4.21.78; 2681.
BRENDA; 3.4.21.B2; 2681.
Reactome; R-HSA-173736; Alternative complement activation.
EvolutionaryTrace; P51124; -.
GeneWiki; GZMM; -.
GenomeRNAi; 3004; -.
PRO; PR:P51124; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000197540; -.
CleanEx; HS_GZMM; -.
ExpressionAtlas; P51124; baseline and differential.
Genevisible; P51124; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0008219; P:cell death; IMP:UniProtKB.
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;
3D-structure; Apoptosis; Complete proteome; Cytolysis; Disulfide bond;
Glycoprotein; Hydrolase; Immunity; Innate immunity; Polymorphism;
Protease; Reference proteome; Secreted; Serine protease; Signal;
Zymogen.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 25 Activation peptide. {ECO:0000255}.
/FTId=PRO_0000027421.
CHAIN 26 257 Granzyme M.
/FTId=PRO_0000027422.
DOMAIN 26 254 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 66 66 Charge relay system.
{ECO:0000269|PubMed:19542453}.
ACT_SITE 111 111 Charge relay system.
{ECO:0000269|PubMed:19542453}.
ACT_SITE 207 207 Charge relay system.
{ECO:0000269|PubMed:19542453}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 51 67 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:19542453}.
DISULFID 145 213 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:19542453}.
DISULFID 176 192 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:19542453}.
DISULFID 203 230 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:19542453}.
VARIANT 221 221 R -> G (in dbSNP:rs1599882).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7713495,
ECO:0000269|PubMed:8245461}.
/FTId=VAR_051829.
STRAND 40 45 {ECO:0000244|PDB:2ZGC}.
STRAND 48 57 {ECO:0000244|PDB:2ZGC}.
STRAND 60 63 {ECO:0000244|PDB:2ZGC}.
HELIX 65 68 {ECO:0000244|PDB:2ZGC}.
HELIX 72 74 {ECO:0000244|PDB:2ZGC}.
STRAND 75 80 {ECO:0000244|PDB:2ZGC}.
STRAND 82 86 {ECO:0000244|PDB:2ZGC}.
STRAND 89 98 {ECO:0000244|PDB:2ZGC}.
TURN 105 107 {ECO:0000244|PDB:2ZGJ}.
STRAND 113 119 {ECO:0000244|PDB:2ZGC}.
STRAND 144 149 {ECO:0000244|PDB:2ZGC}.
STRAND 152 154 {ECO:0000244|PDB:2ZGC}.
STRAND 164 170 {ECO:0000244|PDB:2ZGC}.
HELIX 173 176 {ECO:0000244|PDB:2ZGC}.
TURN 179 184 {ECO:0000244|PDB:2ZGC}.
STRAND 190 194 {ECO:0000244|PDB:2ZGC}.
STRAND 210 213 {ECO:0000244|PDB:2ZGC}.
TURN 214 217 {ECO:0000244|PDB:2ZGC}.
STRAND 218 223 {ECO:0000244|PDB:2ZGC}.
STRAND 238 242 {ECO:0000244|PDB:2ZGC}.
HELIX 243 245 {ECO:0000244|PDB:2ZGC}.
HELIX 246 253 {ECO:0000244|PDB:2ZGC}.
SEQUENCE 257 AA; 27545 MW; B4E815CE455F7371 CRC64;
MEACVSSLLV LALGALSVGS SFGTQIIGGR EVIPHSRPYM ASLQRNGSHL CGGVLVHPKW
VLTAAHCLAQ RMAQLRLVLG LHTLDSPGLT FHIKAAIQHP RYKPVPALEN DLALLQLDGK
VKPSRTIRPL ALPSKRQVVA AGTRCSMAGW GLTHQGGRLS RVLRELDLQV LDTRMCNNSR
FWNGSLSPSM VCLAADSKDQ APCKGDSGGP LVCGKGRVLA RVLSFSSRVC TDIFKPPVAT
AVAPYVSWIR KVTGRSA


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