ID GRAA_HUMAN STANDARD; PRT; 262 AA.
AC P12544;
DT 01-OCT-1989 (Rel. 12, Created)
DT 01-OCT-1989 (Rel. 12, Last sequence update)
DT 15-DEC-1998 (Rel. 37, Last annotation update)
DE GRANZYME A PRECURSOR (EC 3.4.21.78) (CYTOTOXIC T-LYMPHOCYTE PROTEINASE
DE 1) (HANUKKAH FACTOR) (H FACTOR) (HF) (GRANZYME 1) (CTL TRYPTASE)
DE (FRAGMENTIN 1).
GN GZMA OR CTLA3 OR HFSP.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN [1]
RP SEQUENCE FROM N.A.
RC TISSUE=T-cell;
RX MEDLINE; 88125000.
RA Gershenfeld H.K., Hershberger R.J., Shows T.B., Weissman I.L.;
RT "Cloning and chromosomal assignment of a human cDNA encoding a T
RT cell- and natural killer cell-specific trypsin-like serine
RT protease.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1184-1188(1988).
RN [2]
RP SEQUENCE OF 29-53.
RX MEDLINE; 88330824.
RA Poe M., Bennett C.D., Biddison W.E., Blake J.T., Norton G.P.,
RA Rodkey J.A., Sigal N.H., Turner R.V., Wu J.K., Zweerink H.J.;
RT "Human cytotoxic lymphocyte tryptase. Its purification from granules
RT and the characterization of inhibitor and substrate specificity.";
RL J. Biol. Chem. 263:13215-13222(1988).
RN [3]
RP SEQUENCE OF 29-40, AND CHARACTERIZATION.
RX MEDLINE; 89009866.
RA Hameed A., Lowrey D.M., Lichtenheld M., Podack E.R.;
RT "Characterization of three serine esterases isolated from human IL-2
RT activated killer cells.";
RL J. Immunol. 141:3142-3147(1988).
RN [4]
RP SEQUENCE OF 29-39, AND CHARACTERIZATION.
RX MEDLINE; 89035468.
RA Kraehenbuhl O., Rey C., Jenne D.E., Lanzavecchia A., Groscurth P.,
RA Carrel S., Tschopp J.;
RT "Characterization of granzymes A and B isolated from granules of
RT cloned human cytotoxic T lymphocytes.";
RL J. Immunol. 141:3471-3477(1988).
RN [5]
RP 3D-STRUCTURE MODELING.
RX MEDLINE; 89184501.
RA Murphy M.E.P., Moult J., Bleackley R.C., Gershenfeld H.,
RA Weissman I.L., James M.N.G.;
RT "Comparative molecular model building of two serine proteinases from
RT cytotoxic T lymphocytes.";
RL Proteins 4:190-204(1988).
CC -!- FUNCTION: THIS ENZYME IS NECESSARY FOR TARGET CELL LYSIS IN CELL-
CC MEDIATED IMMUNE RESPONSES. IT CLEAVES AFTER LYS OR ARG. MAY BE
CC INVOLVED IN APOPTOSIS.
CC -!- CATALYTIC ACTIVITY: HYDROLYSIS OF PROTEINS, INCLUDING FIBRONECTIN,
CC TYPE IV COLLAGEN AND NUCLEOLIN. PREFERENTIAL CLEAVAGE: ARG-|-XAA,
CC LYS-|-XAA >> PHE-|-XAA IN SMALL MOLECULE SUBSTRATES.
CC -!- SUBUNIT: HOMODIMER, DISULFIDE-LINKED.
CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC GRANULES.
CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S1; ALSO KNOWN AS THE
CC TRYPSIN FAMILY. STRONGEST TO OTHER GRANZYMES AND TO MAST CELL
CC PROTEASES.
DR EMBL; M18737; AAA52647.1; -.
DR PIR; A28943; A28943.
DR PIR; A30525; A30525.
DR PIR; A30526; A30526.
DR PIR; A31372; A31372.
DR PDB; 1HF1; 15-OCT-94.
DR MIM; 140050; -.
DR INTERPRO; IPR001254; -.
DR PFAM; PF00089; trypsin; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
KW Hydrolase; Serine protease; Zymogen; Signal; T-cell; Cytolysis;
KW Apoptosis; 3D-structure.
FT SIGNAL 1 26
FT PROPEP 27 28 ACTIVATION PEPTIDE.
FT CHAIN 29 262 GRANZYME A.
FT ACT_SITE 69 69 CHARGE RELAY SYSTEM (BY SIMILARITY).
FT ACT_SITE 114 114 CHARGE RELAY SYSTEM (BY SIMILARITY).
FT ACT_SITE 212 212 CHARGE RELAY SYSTEM (BY SIMILARITY).
FT DISULFID 54 70 BY SIMILARITY.
FT DISULFID 148 218 BY SIMILARITY.
FT DISULFID 179 197 BY SIMILARITY.
FT DISULFID 208 234 BY SIMILARITY.
FT CARBOHYD 170 170 N-LINKED (GLCNAC...) (POTENTIAL).
SQ SEQUENCE 262 AA; 28968 MW; DA87363A0D92BAF4 CRC64;
MRNSYRFLAS SLSVVVSLLL IPEDVCEKII GGNEVTPHSR PYMVLLSLDR KTICAGALIA
KDWVLTAAHC NLNKRSQVIL GAHSITREEP TKQIMLVKKE FPYPCYDPAT REGDLKLLQL
TEKAKINKYV TILHLPKKGD DVKPGTMCQV AGWGRTHNSA SWSDTLREVN ITIIDRKVCN
DRNHYNFNPV IGMNMVCAGS LRGGRDSCNG DSGSPLLCEG VFRGVTSFGL ENKCGDPRGP
GVYILLSKKH LNWIIMTIKG AV
//
Each line begins with a two-character line code, which indicates the type
of data contained in the line. The current line types and line codes and
the order in which they appear in an entry, are shown in the table below.
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Line code Content Occurrence in an entry
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ID Identification Once; starts the entry
AC Accession number(s) One or more
DT Date Three times
DE Description One or more
GN Gene name(s) Optional
OS Organism species One or more
OG Organelle Optional
OC Organism classification One or more
RN Reference number One or more
RP Reference position One or more
RC Reference comment(s) Optional
RX Reference cross-reference(s) Optional
RA Reference authors One or more
RT Reference title Optional
RL Reference location One or more
CC Comments or notes Optional
DR Database cross-references Optional
KW Keywords Optional
FT Feature table data Optional
SQ Sequence header Once
(blanks) sequence data One or more
// Termination line Once; ends the entry
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Feature table keys
.1 Change indicators
.2 Amino acid modifications
.3 Regions
.4 Secondary structure
.5 Others
Most useful annotation about a protein can be found in either comment line or
feature table line, there are also several conserved words used to describe the
derivation of such information, see more in entry format.
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