GRAA_HUMAN
ID GRAA_HUMAN Reviewed; 262 AA.
AC P12544; A4PHN1; Q6IB36;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Granzyme A {ECO:0000303|PubMed:3263427};
DE EC=3.4.21.78 {ECO:0000269|PubMed:12819770, ECO:0000269|PubMed:32299851};
DE AltName: Full=CTL tryptase {ECO:0000303|PubMed:3047119};
DE AltName: Full=Cytotoxic T-lymphocyte proteinase 1 {ECO:0000303|PubMed:3047119};
DE AltName: Full=Fragmentin-1;
DE AltName: Full=Granzyme-1 {ECO:0000303|PubMed:3262682};
DE AltName: Full=Hanukkah factor {ECO:0000303|PubMed:3257574};
DE Short=H factor {ECO:0000303|PubMed:3257574};
DE Short=HF {ECO:0000303|PubMed:3257574};
DE Flags: Precursor;
GN Name=GZMA {ECO:0000303|PubMed:32299851, ECO:0000312|HGNC:HGNC:4708};
GN Synonyms=CTLA3, HFSP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION, SUBCELLULAR LOCATION,
RP AND VARIANT THR-121.
RC TISSUE=T-cell;
RX PubMed=3257574; DOI=10.1073/pnas.85.4.1184;
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 cell- and
RT natural killer cell-specific trypsin-like serine protease.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1184-1188(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
RP THR-121.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
RP THR-121.
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72, NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-34 (ISOFORM BETA), ALTERNATIVE PROMOTER USAGE, AND INDUCTION.
RX PubMed=17180578; DOI=10.1007/s10038-006-0099-9;
RA Ruike Y., Katsuma S., Hirasawa A., Tsujimoto G.;
RT "Glucocorticoid-induced alternative promoter usage for a novel 5' variant
RT of granzyme A.";
RL J. Hum. Genet. 52:172-178(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RA Goralski T.J., Krensky A.M.;
RT "The upstream region of the human granzyme A locus contains both positive
RT and negative transcriptional regulatory elements.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 29-53.
RX PubMed=3047119; DOI=10.1016/s0021-9258(18)37694-4;
RA Poe M., Bennett C.D., Biddison W.E., Blake J.T., Norton G.P., Rodkey J.A.,
RA Sigal N.H., Turner R.V., Wu J.K., Zweerink H.J.;
RT "Human cytotoxic lymphocyte tryptase. Its purification from granules and
RT the characterization of inhibitor and substrate specificity.";
RL J. Biol. Chem. 263:13215-13222(1988).
RN [8]
RP PROTEIN SEQUENCE OF 29-40, AND FUNCTION.
RX PubMed=3262682;
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 [9]
RP PROTEIN SEQUENCE OF 29-39, AND FUNCTION.
RX PubMed=3263427;
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 cloned
RT human cytotoxic T lymphocytes.";
RL J. Immunol. 141:3471-3477(1988).
RN [10]
RP FUNCTION AS SET PROTEASE.
RX PubMed=11555662; DOI=10.1074/jbc.m108137200;
RA Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M.,
RA Lieberman J.;
RT "Granzyme A activates an endoplasmic reticulum-associated caspase-
RT independent nuclease to induce single-stranded DNA nicks.";
RL J. Biol. Chem. 276:43285-43293(2001).
RN [11]
RP FUNCTION AS SET PROTEASE.
RX PubMed=12628186; DOI=10.1016/s0092-8674(03)00150-8;
RA Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.;
RT "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-
RT mediated apoptosis, and the nucleosome assembly protein SET is its
RT inhibitor.";
RL Cell 112:659-672(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH APEX1.
RX PubMed=12524539; DOI=10.1038/ni885;
RA Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A.,
RA Pommier Y., Lieberman J.;
RT "Cleaving the oxidative repair protein Ape1 enhances cell death mediated by
RT granzyme A.";
RL Nat. Immunol. 4:145-153(2003).
RN [13]
RP FUNCTION AS SET PROTEASE.
RX PubMed=16818237; DOI=10.1016/j.molcel.2006.06.005;
RA Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B.,
RA Perrino F.W., Lieberman J.;
RT "The exonuclease TREX1 is in the SET complex and acts in concert with NM23-
RT H1 to degrade DNA during granzyme A-mediated cell death.";
RL Mol. Cell 23:133-142(2006).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-170.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=20038786; DOI=10.1182/blood-2009-10-246116;
RA Thiery J., Keefe D., Saffarian S., Martinvalet D., Walch M., Boucrot E.,
RA Kirchhausen T., Lieberman J.;
RT "Perforin activates clathrin- and dynamin-dependent endocytosis, which is
RT required for plasma membrane repair and delivery of granzyme B for
RT granzyme-mediated apoptosis.";
RL Blood 115:1582-1593(2010).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ACTIVE SITE, AND
RP MUTAGENESIS OF SER-212.
RX PubMed=32299851; DOI=10.1126/science.aaz7548;
RA Zhou Z., He H., Wang K., Shi X., Wang Y., Su Y., Wang Y., Li D., Liu W.,
RA Zhang Y., Shen L., Han W., Shen L., Ding J., Shao F.;
RT "Granzyme A from cytotoxic lymphocytes cleaves GSDMB to trigger pyroptosis
RT in target cells.";
RL Science 368:0-0(2020).
RN [17]
RP 3D-STRUCTURE MODELING OF 29-262.
RX PubMed=3237717; DOI=10.1002/prot.340040306;
RA Murphy M.E.P., Moult J., Bleackley R.C., Gershenfeld H., Weissman I.L.,
RA James M.N.G.;
RT "Comparative molecular model building of two serine proteinases from
RT cytotoxic T lymphocytes.";
RL Proteins 4:190-204(1988).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-262 IN COMPLEX WITH A
RP TRIPEPTIDE CMK INHIBITOR, AND DISULFIDE BONDS.
RX PubMed=12819769; DOI=10.1038/nsb944;
RA Bell J.K., Goetz D.H., Mahrus S., Harris J.L., Fletterick R.J., Craik C.S.;
RT "The oligomeric structure of human granzyme A is a determinant of its
RT extended substrate specificity.";
RL Nat. Struct. Biol. 10:527-534(2003).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 29-262 IN COMPLEX WITH SUBSTRATE,
RP FUNCTION, CATALYTIC ACTIVITY, AND DISULFIDE BONDS.
RX PubMed=12819770; DOI=10.1038/nsb945;
RA Hink-Schauer C., Estebanez-Perpina E., Kurschus F.C., Bode W., Jenne D.E.;
RT "Crystal structure of the apoptosis-inducing human granzyme A dimer.";
RL Nat. Struct. Biol. 10:535-540(2003).
CC -!- FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-
CC cells and NK-cells which activates caspase-independent pyroptosis when
CC delivered into the target cell through the immunological synapse
CC (PubMed:3257574, PubMed:3262682, PubMed:3263427, PubMed:32299851,
CC PubMed:12819770). It cleaves after Lys or Arg (PubMed:32299851,
CC PubMed:12819770). Once delivered into the target cell, acts by
CC catalyzing cleavage of gasdermin-B (GSDMB), releasing the pore-forming
CC moiety of GSDMB, thereby triggering pyroptosis and target cell death
CC (PubMed:32299851). Cleaves APEX1 after 'Lys-31' and destroys its
CC oxidative repair activity (PubMed:12524539). Cleaves the nucleosome
CC assembly protein SET after 'Lys-189', which disrupts its nucleosome
CC assembly activity and allows the SET complex to translocate into the
CC nucleus to nick and degrade the DNA (PubMed:11555662, PubMed:12628186,
CC PubMed:16818237). {ECO:0000269|PubMed:11555662,
CC ECO:0000269|PubMed:12524539, ECO:0000269|PubMed:12628186,
CC ECO:0000269|PubMed:12819770, ECO:0000269|PubMed:16818237,
CC ECO:0000269|PubMed:32299851, ECO:0000269|PubMed:3257574,
CC ECO:0000269|PubMed:3262682, ECO:0000269|PubMed:3263427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, including fibronectin, type IV
CC collagen and nucleolin. Preferential cleavage: -Arg-|-Xaa-, -Lys-|-
CC Xaa- >> -Phe-|-Xaa- in small molecule substrates.; EC=3.4.21.78;
CC Evidence={ECO:0000269|PubMed:12819770, ECO:0000269|PubMed:32299851};
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:12819769,
CC PubMed:12819770). Interacts with APEX1 (PubMed:12524539).
CC {ECO:0000269|PubMed:12524539, ECO:0000269|PubMed:12819769,
CC ECO:0000269|PubMed:12819770}.
CC -!- SUBCELLULAR LOCATION: [Isoform alpha]: Secreted
CC {ECO:0000269|PubMed:3257574}. Cytoplasmic granule
CC {ECO:0000269|PubMed:3257574}. Note=Delivered into the target cell by
CC perforin. {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:32299851}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=alpha {ECO:0000303|PubMed:17180578};
CC IsoId=P12544-1; Sequence=Displayed;
CC Name=beta {ECO:0000303|PubMed:17180578};
CC IsoId=P12544-2; Sequence=VSP_038571, VSP_038572;
CC -!- INDUCTION: Dexamethasone (DEX) induces expression of isoform beta and
CC represses expression of isoform alpha. The alteration in expression is
CC mediated by binding of glucocorticoid receptor to independent promoters
CC adjacent to the alternative first exons of isoform alpha and isoform
CC beta. {ECO:0000269|PubMed:17180578}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Exons 1a and 1b of the sequence reported in PubMed:17180578
CC are of human origin, however exon 2 shows strong similarity to the rat
CC sequence. {ECO:0000305|PubMed:17180578}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GZMAID51130ch5q11.html";
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DR EMBL; M18737; AAA52647.1; -; mRNA.
DR EMBL; CR456968; CAG33249.1; -; mRNA.
DR EMBL; AC091977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015739; AAH15739.1; -; mRNA.
DR EMBL; AB284134; BAF56159.1; -; mRNA.
DR EMBL; U40006; AAD00009.1; -; Genomic_DNA.
DR CCDS; CCDS3965.1; -. [P12544-1]
DR PIR; A31372; A31372.
DR RefSeq; NP_006135.1; NM_006144.3. [P12544-1]
DR PDB; 1OP8; X-ray; 2.50 A; A/B/C/D/E/F=29-262.
DR PDB; 1ORF; X-ray; 2.40 A; A=29-262.
DR PDBsum; 1OP8; -.
DR PDBsum; 1ORF; -.
DR AlphaFoldDB; P12544; -.
DR SMR; P12544; -.
DR BioGRID; 109256; 17.
DR IntAct; P12544; 4.
DR STRING; 9606.ENSP00000274306; -.
DR ChEMBL; CHEMBL4307; -.
DR MEROPS; S01.135; -.
DR GlyGen; P12544; 1 site.
DR iPTMnet; P12544; -.
DR PhosphoSitePlus; P12544; -.
DR BioMuta; GZMA; -.
DR DMDM; 317373360; -.
DR jPOST; P12544; -.
DR MassIVE; P12544; -.
DR MaxQB; P12544; -.
DR PaxDb; P12544; -.
DR PeptideAtlas; P12544; -.
DR PRIDE; P12544; -.
DR ProteomicsDB; 52858; -. [P12544-1]
DR ProteomicsDB; 52859; -. [P12544-2]
DR Antibodypedia; 11050; 383 antibodies from 39 providers.
DR CPTC; P12544; 1 antibody.
DR DNASU; 3001; -.
DR Ensembl; ENST00000274306.7; ENSP00000274306.6; ENSG00000145649.8. [P12544-1]
DR GeneID; 3001; -.
DR KEGG; hsa:3001; -.
DR MANE-Select; ENST00000274306.7; ENSP00000274306.6; NM_006144.4; NP_006135.2.
DR UCSC; uc003jpm.4; human. [P12544-1]
DR CTD; 3001; -.
DR DisGeNET; 3001; -.
DR GeneCards; GZMA; -.
DR HGNC; HGNC:4708; GZMA.
DR HPA; ENSG00000145649; Tissue enhanced (lymphoid).
DR MIM; 140050; gene.
DR neXtProt; NX_P12544; -.
DR OpenTargets; ENSG00000145649; -.
DR PharmGKB; PA29086; -.
DR VEuPathDB; HostDB:ENSG00000145649; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000159928; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P12544; -.
DR OMA; YPCYDPA; -.
DR OrthoDB; 1105435at2759; -.
DR PhylomeDB; P12544; -.
DR TreeFam; TF333630; -.
DR BRENDA; 3.4.21.78; 2681.
DR PathwayCommons; P12544; -.
DR SignaLink; P12544; -.
DR SIGNOR; P12544; -.
DR BioGRID-ORCS; 3001; 13 hits in 1072 CRISPR screens.
DR EvolutionaryTrace; P12544; -.
DR GeneWiki; GZMA; -.
DR GenomeRNAi; 3001; -.
DR Pharos; P12544; Tbio.
DR PRO; PR:P12544; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P12544; protein.
DR Bgee; ENSG00000145649; Expressed in granulocyte and 138 other tissues.
DR Genevisible; P12544; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001772; C:immunological synapse; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:1902483; P:cytotoxic T cell pyroptotic process; IDA:UniProtKB.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:UniProtKB.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0032078; P:negative regulation of endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
DR GO; GO:0070269; P:pyroptosis; IDA:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
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 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 3D-structure; Alternative promoter usage; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..28
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:3047119,
FT ECO:0000269|PubMed:3262682, ECO:0000269|PubMed:3263427"
FT /id="PRO_0000027393"
FT CHAIN 29..262
FT /note="Granzyme A"
FT /id="PRO_0000027394"
FT DOMAIN 29..259
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 69
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:12819769,
FT ECO:0000269|PubMed:12819770"
FT ACT_SITE 114
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:12819769,
FT ECO:0000269|PubMed:12819770"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:12819769,
FT ECO:0000269|PubMed:12819770, ECO:0000305|PubMed:32299851"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 54..70
FT /evidence="ECO:0000269|PubMed:12819769,
FT ECO:0000269|PubMed:12819770, ECO:0007744|PDB:1OP8,
FT ECO:0007744|PDB:1ORF"
FT DISULFID 148..218
FT /evidence="ECO:0000269|PubMed:12819769,
FT ECO:0000269|PubMed:12819770, ECO:0007744|PDB:1OP8,
FT ECO:0007744|PDB:1ORF"
FT DISULFID 179..197
FT /evidence="ECO:0000269|PubMed:12819769,
FT ECO:0000269|PubMed:12819770, ECO:0007744|PDB:1OP8,
FT ECO:0007744|PDB:1ORF"
FT DISULFID 208..234
FT /evidence="ECO:0000269|PubMed:12819769,
FT ECO:0000269|PubMed:12819770, ECO:0007744|PDB:1OP8,
FT ECO:0007744|PDB:1ORF"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform beta)"
FT /evidence="ECO:0000303|PubMed:17180578"
FT /id="VSP_038571"
FT VAR_SEQ 18..23
FT /note="LLLIPE -> MTKGLR (in isoform beta)"
FT /evidence="ECO:0000303|PubMed:17180578"
FT /id="VSP_038572"
FT VARIANT 121
FT /note="M -> T (in dbSNP:rs3104233)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3257574, ECO:0000269|Ref.2"
FT /id="VAR_024291"
FT MUTAGEN 212
FT /note="S->A: Abolished protease activity."
FT /evidence="ECO:0000269|PubMed:32299851"
FT CONFLICT 33..34
FT /note="NE -> DT (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="T -> V (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="S -> K (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..52
FT /note="DRKT -> KPDS (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="D -> N (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..72
FT /note="NL -> IP (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1ORF"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1ORF"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:1ORF"
FT TURN 182..189
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:1ORF"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1ORF"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:1ORF"
SQ SEQUENCE 262 AA; 28999 MW; FD773628BA6F301B CRC64;
MRNSYRFLAS SLSVVVSLLL IPEDVCEKII GGNEVTPHSR PYMVLLSLDR KTICAGALIA
KDWVLTAAHC NLNKRSQVIL GAHSITREEP TKQIMLVKKE FPYPCYDPAT REGDLKLLQL
MEKAKINKYV TILHLPKKGD DVKPGTMCQV AGWGRTHNSA SWSDTLREVN ITIIDRKVCN
DRNHYNFNPV IGMNMVCAGS LRGGRDSCNG DSGSPLLCEG VFRGVTSFGL ENKCGDPRGP
GVYILLSKKH LNWIIMTIKG AV
