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Granzyme A (EC 3.4.21.78) (Autocrine thymic lymphoma granzyme-like serine protease) (CTLA-3) (Fragmentin-1) (T cell-specific serine protease 1) (TSP-1)

 GRAA_MOUSE              Reviewed;         260 AA.
P11032; P15118;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 2.
07-JUN-2017, entry version 167.
RecName: Full=Granzyme A;
EC=3.4.21.78;
AltName: Full=Autocrine thymic lymphoma granzyme-like serine protease;
AltName: Full=CTLA-3;
AltName: Full=Fragmentin-1;
AltName: Full=T cell-specific serine protease 1;
Short=TSP-1;
Flags: Precursor;
Name=Gzma; Synonyms=Ctla-3, Ctla3, Mtsp-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=2976140;
Bogenberger J., Haas M.;
"cDNA clones from autocrine thymic lymphoma cells encode two mitogenic
proteins, a serine protease and a truncated T-cell receptor beta-
chain.";
Oncogene Res. 3:301-312(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=1639378; DOI=10.1016/0888-7543(92)90117-B;
Ebnet K., Kramer M.D., Simon M.M.;
"Organization of the gene encoding the mouse T-cell-specific serine
proteinase 'granzyme A'.";
Genomics 13:502-508(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS HF1 AND HF2).
PubMed=1460043;
Hershberger R.J., Gershenfeld H.K., Weissman I.L., Su L.;
"Genomic organization of the mouse granzyme A gene. Two mRNAs encode
the same mature granzyme A with different leader peptides.";
J. Biol. Chem. 267:25488-25493(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HF1).
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-37.
PubMed=3292396; DOI=10.1111/j.1600-065X.1988.tb00749.x;
Jenne D.E., Tschopp J.;
"Granzymes, a family of serine proteases released from granules of
cytolytic T lymphocytes upon T cell receptor stimulation.";
Immunol. Rev. 103:53-71(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-260.
PubMed=2422755; DOI=10.1126/science.2422755;
Gershenfeld H.K., Weissman I.L.;
"Cloning of a cDNA for a T cell-specific serine protease from a
cytotoxic T lymphocyte.";
Science 232:854-858(1986).
[7]
PROTEIN SEQUENCE OF 29-48.
PubMed=3555842; DOI=10.1016/0092-8674(87)90544-7;
Masson D., Tschopp J.;
"A family of serine esterases in lytic granules of cytolytic T
lymphocytes.";
Cell 49:679-685(1987).
[8]
PROTEIN SEQUENCE OF 29-53.
PubMed=3533635; DOI=10.1016/0014-5793(86)81537-X;
Masson D., Zamai M., Tschopp J.;
"Identification of granzyme A isolated from cytotoxic T-lymphocyte-
granules as one of the proteases encoded by CTL-specific genes.";
FEBS Lett. 208:84-88(1986).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 29-46.
PubMed=3260181; DOI=10.1002/eji.1830180605;
Simon H.G., Fruth U., Eckerskorn C., Lottspeich F., Kramer M.D.,
Nerz G., Simon M.M.;
"Induction of T cell serine proteinase 1 (TSP-1)-specific mRNA in
mouse T lymphocytes.";
Eur. J. Immunol. 18:855-861(1988).
-!- FUNCTION: Abundant protease in the cytosolic granules of cytotoxic
T-cells and NK-cells which activates caspase-independent cell
death with morphological features of apoptosis when delivered into
the target cell through the immunological synapse. It cleaves
after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its
oxidative repair activity. Cleaves the nucleosome assembly protein
SET after 'Lys-189', which disrupts its nucleosome assembly
activity and allows the SET complex to translocate into the
nucleus to nick and degrade the DNA (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins, including fibronectin,
type IV collagen and nucleolin. Preferential cleavage: -Arg-|-
Xaa-, -Lys-|-Xaa- >> -Phe-|-Xaa- in small molecule substrates.
-!- SUBUNIT: Interacts with APEX1 (By similarity). Homodimer;
disulfide-linked. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule.
Note=Cytoplasmic granules of cytolytic T-lymphocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=HF1;
IsoId=P11032-1; Sequence=Displayed;
Note=More abundant in lymphoid tissues than isoform HF2.;
Name=HF2;
IsoId=P11032-2; Sequence=VSP_005373;
-!- TISSUE SPECIFICITY: Found in cytotoxic lymphocytes and in normal
lymphoid tissues such as thymus and spleen.
-!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- CAUTION: The predicted cleavage site for the activation peptide of
HF2 is uncertain. It could have either 2 (ER) or 7 (KRGGCER) AA.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X14799; CAA32905.1; -; mRNA.
EMBL; X62542; CAA44426.1; -; Genomic_DNA.
EMBL; X62543; CAA44426.1; JOINED; Genomic_DNA.
EMBL; X60310; CAA44426.1; JOINED; Genomic_DNA.
EMBL; X60311; CAA44426.1; JOINED; Genomic_DNA.
EMBL; L01429; AAA99898.1; -; Genomic_DNA.
EMBL; L01426; AAA99898.1; JOINED; Genomic_DNA.
EMBL; L01427; AAA99898.1; JOINED; Genomic_DNA.
EMBL; L01441; AAA99898.1; JOINED; Genomic_DNA.
EMBL; L01429; AAA99897.1; -; Genomic_DNA.
EMBL; L01426; AAA99897.1; JOINED; Genomic_DNA.
EMBL; L01427; AAA99897.1; JOINED; Genomic_DNA.
EMBL; L01441; AAA99897.1; JOINED; Genomic_DNA.
EMBL; BC061146; AAH61146.1; -; mRNA.
EMBL; M26183; AAA37735.1; -; mRNA.
EMBL; M13226; AAA40134.1; -; mRNA.
CCDS; CCDS26782.1; -. [P11032-1]
PIR; A24807; A24807.
PIR; A45061; A45061.
PIR; B45061; B45061.
RefSeq; NP_034500.1; NM_010370.2. [P11032-1]
UniGene; Mm.15510; -.
ProteinModelPortal; P11032; -.
SMR; P11032; -.
IntAct; P11032; 1.
MINT; MINT-4096608; -.
STRING; 10090.ENSMUSP00000023897; -.
MEROPS; S01.135; -.
PhosphoSitePlus; P11032; -.
PaxDb; P11032; -.
PeptideAtlas; P11032; -.
PRIDE; P11032; -.
Ensembl; ENSMUST00000023897; ENSMUSP00000023897; ENSMUSG00000023132. [P11032-1]
GeneID; 14938; -.
KEGG; mmu:14938; -.
UCSC; uc007rxc.1; mouse. [P11032-1]
UCSC; uc011zeu.1; mouse. [P11032-2]
CTD; 3001; -.
MGI; MGI:109266; Gzma.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P11032; -.
KO; K01352; -.
OMA; KEFPYPC; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P11032; -.
TreeFam; TF333630; -.
BRENDA; 3.4.21.78; 3474.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000023132; -.
CleanEx; MM_GZMA; -.
ExpressionAtlas; P11032; baseline and differential.
Genevisible; P11032; MM.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; IDA:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0043392; P:negative regulation of DNA binding; ISS:UniProtKB.
GO; GO:0032078; P:negative regulation of endodeoxyribonuclease activity; ISS:UniProtKB.
GO; GO:0051354; P:negative regulation of oxidoreductase activity; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISS:UniProtKB.
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;
Alternative splicing; Apoptosis; Complete proteome; Cytolysis;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Protease; Reference proteome; Secreted; Serine protease; Signal;
Zymogen.
SIGNAL 1 26
PROPEP 27 28 Activation peptide.
{ECO:0000269|PubMed:3533635,
ECO:0000269|PubMed:3555842}.
/FTId=PRO_0000027395.
CHAIN 29 260 Granzyme A.
/FTId=PRO_0000027396.
DOMAIN 29 257 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 69 69 Charge relay system. {ECO:0000250}.
ACT_SITE 113 113 Charge relay system. {ECO:0000250}.
ACT_SITE 211 211 Charge relay system. {ECO:0000250}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 70 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 147 217 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 178 196 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 207 232 {ECO:0000255|PROSITE-ProRule:PRU00274}.
VAR_SEQ 1 23 MRNASGPRGPSLATLLFLLLIPE -> MSKEMNEILLSWEI
NLSSKR (in isoform HF2). {ECO:0000305}.
/FTId=VSP_005373.
SEQUENCE 260 AA; 28599 MW; 7705352F08DEED8D CRC64;
MRNASGPRGP SLATLLFLLL IPEGGCERII GGDTVVPHSR PYMALLKLSS NTICAGALIE
KNWVLTAAHC NVGKRSKFIL GAHSINKEPE QQILTVKKAF PYPCYDEYTR EGDLQLVRLK
KKATVNRNVA ILHLPKKGDD VKPGTRCRVA GWGRFGNKSA PSETLREVNI TVIDRKICND
EKHYNFHPVI GLNMICAGDL RGGKDSCNGD SGSPLLCDGI LRGITSFGGE KCGDRRWPGV
YTFLSDKHLN WIKKIMKGSV


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