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Granzyme A (EC 3.4.21.78)

 GRAA_BOVIN              Reviewed;         258 AA.
Q7YRZ7;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
07-JUN-2017, entry version 95.
RecName: Full=Granzyme A;
EC=3.4.21.78;
Flags: Precursor;
Name=GZMA;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Jenne D.E.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
-!- 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 {ECO:0000250}. Cytoplasmic granule
{ECO:0000250}. Note=Cytoplasmic granules of cytolytic T-
lymphocytes. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AJ544059; CAD66427.1; -; mRNA.
RefSeq; NP_001001142.1; NM_001001142.1.
UniGene; Bt.29672; -.
ProteinModelPortal; Q7YRZ7; -.
SMR; Q7YRZ7; -.
STRING; 9913.ENSBTAP00000039959; -.
MEROPS; S01.135; -.
PaxDb; Q7YRZ7; -.
PRIDE; Q7YRZ7; -.
Ensembl; ENSBTAT00000040181; ENSBTAP00000039959; ENSBTAG00000027865.
GeneID; 407178; -.
KEGG; bta:407178; -.
CTD; 3001; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q7YRZ7; -.
KO; K01352; -.
OMA; AGWGSTK; -.
OrthoDB; EOG091G0AH5; -.
TreeFam; TF333630; -.
Proteomes; UP000009136; Chromosome 20.
Bgee; ENSBTAG00000027865; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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.
2: Evidence at transcript level;
Apoptosis; Complete proteome; Cytolysis; Disulfide bond; Glycoprotein;
Hydrolase; Protease; Reference proteome; Secreted; Serine protease;
Signal; Zymogen.
SIGNAL 1 26 {ECO:0000250}.
PROPEP 27 28 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000027397.
CHAIN 29 258 Granzyme A.
/FTId=PRO_0000027398.
DOMAIN 29 255 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 67 67 Charge relay system. {ECO:0000250}.
ACT_SITE 112 112 Charge relay system. {ECO:0000250}.
ACT_SITE 211 211 Charge relay system. {ECO:0000250}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 52 68 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 146 217 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 178 196 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 207 230 {ECO:0000255|PROSITE-ProRule:PRU00274}.
SEQUENCE 258 AA; 28070 MW; 042707AD8C87624E CRC64;
MNIPFPFSFP PAICLLLIPG VFPVSCEGII GGNEVAPHTR RYMALIKGLK LCAGALIKEN
WVLTAAHCDL KGNPQVILGA HSTSHKEKLD QVFSIKKAIP YPCFDPQTFE GDLQLLQLEG
KATMTKAVGI LQLPRTEDDV KPHTKCHVAG WGSTKKDACQ MSNALREANV TVIDRKICND
AQHYNFNPVI DLSMICAGGR KGEDDSCEGD SGSPLICDNV FRGVTSFGKC GNPQKPGIYI
LLTKKHLNWI KKTIAGAI


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