GRAB_HUMAN
ID GRAB_HUMAN Reviewed; 247 AA.
AC P10144; Q8N1D2; Q9UCC1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Granzyme B {ECO:0000303|PubMed:2332171};
DE EC=3.4.21.79 {ECO:0000269|PubMed:1985927, ECO:0000269|PubMed:32188940, ECO:0000269|PubMed:8258716, ECO:0000269|PubMed:9852092};
DE AltName: Full=C11;
DE AltName: Full=CTLA-1 {ECO:0000303|PubMed:2332171};
DE AltName: Full=Cathepsin G-like 1;
DE Short=CTSGL1;
DE AltName: Full=Cytotoxic T-lymphocyte proteinase 2;
DE Short=Lymphocyte protease;
DE AltName: Full=Fragmentin-2;
DE AltName: Full=Granzyme-2;
DE AltName: Full=Human lymphocyte protein;
DE Short=HLP;
DE AltName: Full=SECT;
DE AltName: Full=T-cell serine protease 1-3E;
DE Flags: Precursor;
GN Name=GZMB {ECO:0000303|PubMed:32188940, ECO:0000312|HGNC:HGNC:4709};
GN Synonyms=CGL1, CSPB, CTLA1 {ECO:0000303|PubMed:2332171},
GN GRB {ECO:0000303|PubMed:9852092};
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], AND VARIANT GLN-55.
RX PubMed=2953813;
RA Schmid J., Weissmann C.;
RT "Induction of mRNA for a serine protease and a beta-thromboglobulin-like
RT protein in mitogen-stimulated human leukocytes.";
RL J. Immunol. 139:250-256(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-94.
RX PubMed=3258865; DOI=10.1016/s0021-9258(18)68794-0;
RA Caputo A., Fahey D., Lloyd C., Vozab R., McCairns E., Rowe P.B.;
RT "Structure and differential mechanisms of regulation of expression of a
RT serine esterase gene in activated human T lymphocytes.";
RL J. Biol. Chem. 263:6363-6369(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-55.
RX PubMed=3261871; DOI=10.1073/pnas.85.18.6924;
RA Trapani J.A., Klein J.L., White P.C., Dupont B.;
RT "Molecular cloning of an inducible serine esterase gene from human
RT cytotoxic lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6924-6928(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-55.
RX PubMed=2788607; DOI=10.1016/0888-7543(89)90093-1;
RA Klein J.L., Shows T.B., Dupont B., Trapani J.A.;
RT "Genomic organization and chromosomal assignment for a serine protease gene
RT (CSPB) expressed by human cytotoxic lymphocytes.";
RL Genomics 5:110-117(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-55.
RX PubMed=2365998;
RA Caputo A., Sauer D.E., Rowe P.B.;
RT "Nucleotide sequence and genomic organization of a human T lymphocyte
RT serine protease gene.";
RL J. Immunol. 145:737-744(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-55 AND ALA-94.
RX PubMed=2332171; DOI=10.1016/0378-1119(90)90311-e;
RA Haddad P., Clement M.-V., Bernard O., Larsen C.-J., Degos L., Sasportes M.,
RA Mathieu-Mahul D.;
RT "Structural organization of the hCTLA-1 gene encoding human granzyme B.";
RL Gene 87:265-271(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-55 AND HIS-247.
RC TISSUE=Pancreas;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-23.
RX PubMed=2323780; DOI=10.1007/bf00195821;
RA Dahl C.A., Bach F.H., Chan W., Huebner K., Russo G., Croce C.M.,
RA Herfurth T., Cairns J.S.;
RT "Isolation of a cDNA clone encoding a novel form of granzyme B from human
RT NK cells and mapping to chromosome 14.";
RL Hum. Genet. 84:465-470(1990).
RN [10]
RP PROTEIN SEQUENCE OF 21-40, 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 [11]
RP PROTEIN SEQUENCE OF 21-40, 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 [12]
RP PROTEIN SEQUENCE OF 21-39, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RC TISSUE=Lymphocyte;
RX PubMed=8258716;
RA Froelich C.J., Zhang X., Turbov J., Hudig D., Winkler U., Hanna W.L.;
RT "Human granzyme B degrades aggrecan proteoglycan in matrix synthesized by
RT chondrocytes.";
RL J. Immunol. 151:7161-7171(1993).
RN [13]
RP PROTEIN SEQUENCE OF 21-38, FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=1985927; DOI=10.1016/s0021-9258(18)52407-8;
RA Poe M., Blake J.T., Boulton D.A., Gammon M., Sigal N.H., Wu J.K.,
RA Zweerink H.J.;
RT "Human cytotoxic lymphocyte granzyme B. Its purification from granules and
RT the characterization of substrate and inhibitor specificity.";
RL J. Biol. Chem. 266:98-103(1991).
RN [14]
RP PROTEIN SEQUENCE OF 19-33.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9852092; DOI=10.1074/jbc.273.51.34278;
RA Yang X., Stennicke H.R., Wang B., Green D.R., Jaenicke R.U., Srinivasan A.,
RA Seth P., Salvesen G.S., Froelich C.J.;
RT "Granzyme B mimics apical caspases. Description of a unified pathway for
RT trans-activation of executioner caspase-3 and -7.";
RL J. Biol. Chem. 273:34278-34283(1998).
RN [16]
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 [17]
RP SUBCELLULAR LOCATION.
RX PubMed=24088571; DOI=10.1091/mbc.e13-05-0259;
RA Tuli A., Thiery J., James A.M., Michelet X., Sharma M., Garg S.,
RA Sanborn K.B., Orange J.S., Lieberman J., Brenner M.B.;
RT "Arf-like GTPase Arl8b regulates lytic granule polarization and natural
RT killer cell-mediated cytotoxicity.";
RL Mol. Biol. Cell 24:3721-3735(2013).
RN [18]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32188940; DOI=10.1038/s41586-020-2071-9;
RA Zhang Z., Zhang Y., Xia S., Kong Q., Li S., Liu X., Junqueira C.,
RA Meza-Sosa K.F., Mok T.M.Y., Ansara J., Sengupta S., Yao Y., Wu H.,
RA Lieberman J.;
RT "Gasdermin E suppresses tumour growth by activating anti-tumour immunity.";
RL Nature 579:415-420(2020).
RN [19]
RP FUNCTION.
RX PubMed=31953257; DOI=10.1126/sciimmunol.aax7969;
RA Liu Y., Fang Y., Chen X., Wang Z., Liang X., Zhang T., Liu M., Zhou N.,
RA Lv J., Tang K., Xie J., Gao Y., Cheng F., Zhou Y., Zhang Z., Hu Y.,
RA Zhang X., Gao Q., Zhang Y., Huang B.;
RT "Gasdermin E-mediated target cell pyroptosis by CAR T cells triggers
RT cytokine release syndrome.";
RL Sci. Immunol. 5:0-0(2020).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 21-247.
RX PubMed=11209755; DOI=10.1515/bc.2000.148;
RA Estebanez-Perpina E., Fuentes-Prior P., Belorgey D., Braun M.,
RA Kiefersauer R., Maskos K., Huber R., Rubin H., Bode W.;
RT "Crystal structure of the caspase activator human granzyme B, a proteinase
RT highly specific for an Asp-P1 residue.";
RL Biol. Chem. 381:1203-1214(2000).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-247, AND GLYCOSYLATION AT
RP ASN-71 AND ASN-104.
RX PubMed=11325591; DOI=10.1016/s1074-5521(01)00018-7;
RA Rotonda J., Garcia-Calvo M., Bull H.G., Geissler W.M., McKeever B.M.,
RA Willoughby C.A., Thornberry N.A., Becker J.W.;
RT "The three-dimensional structure of human granzyme B compared to caspase-3,
RT key mediators of cell death with cleavage specificity for aspartic acid in
RT P1.";
RL Chem. Biol. 8:357-368(2001).
RN [22]
RP VARIANTS GLN-55 AND HIS-247.
RX PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
RA Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
RA Nakamura Y.;
RT "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine
RT esterase genes, and two other genes in the Japanese population.";
RL J. Hum. Genet. 48:249-270(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:3262682, PubMed:3263427, PubMed:1985927). It cleaves after Asp
CC (PubMed:8258716, PubMed:1985927). Once delivered into the target cell,
CC acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-
CC forming moiety of GSDME, thereby triggering pyroptosis and target cell
CC death (PubMed:32188940, PubMed:31953257). Seems to be linked to an
CC activation cascade of caspases (aspartate-specific cysteine proteases)
CC responsible for apoptosis execution. Cleaves caspase-3, -7, -9 and 10
CC to give rise to active enzymes mediating apoptosis (PubMed:9852092).
CC {ECO:0000269|PubMed:1985927, ECO:0000269|PubMed:31953257,
CC ECO:0000269|PubMed:32188940, ECO:0000269|PubMed:3262682,
CC ECO:0000269|PubMed:3263427, ECO:0000269|PubMed:8258716,
CC ECO:0000269|PubMed:9852092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-
CC Xaa-, -Ser-|-Xaa-.; EC=3.4.21.79;
CC Evidence={ECO:0000269|PubMed:1985927, ECO:0000269|PubMed:32188940,
CC ECO:0000269|PubMed:8258716, ECO:0000269|PubMed:9852092};
CC -!- ACTIVITY REGULATION: Inactivated by the serine protease inhibitor
CC diisopropylfluorophosphate. {ECO:0000269|PubMed:8258716}.
CC -!- INTERACTION:
CC P10144; P14222: PRF1; NbExp=3; IntAct=EBI-2505785, EBI-724466;
CC P10144; P10124: SRGN; NbExp=2; IntAct=EBI-2505785, EBI-744915;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20038786,
CC ECO:0000269|PubMed:8258716}. Cytolytic granule
CC {ECO:0000269|PubMed:1985927, ECO:0000269|PubMed:24088571,
CC ECO:0000269|PubMed:8258716}. Note=Delivered into the target cell by
CC perforin (PubMed:20038786). {ECO:0000269|PubMed:20038786,
CC ECO:0000269|PubMed:8258716}.
CC -!- INDUCTION: By staphylococcal enterotoxin A (SEA) in peripheral blood
CC leukocytes.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; M17016; AAA36627.1; -; mRNA.
DR EMBL; J03189; AAA36603.1; -; mRNA.
DR EMBL; J04071; AAA52118.1; -; mRNA.
DR EMBL; J03072; AAB59528.1; -; Genomic_DNA.
DR EMBL; M38193; AAA67124.1; -; Genomic_DNA.
DR EMBL; M28879; AAA75490.1; -; Genomic_DNA.
DR EMBL; AL136018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030195; AAH30195.1; -; mRNA.
DR CCDS; CCDS9633.1; -.
DR PIR; A61021; A61021.
DR RefSeq; NP_004122.2; NM_004131.5.
DR PDB; 1FQ3; X-ray; 3.10 A; A/B=21-247.
DR PDB; 1IAU; X-ray; 2.00 A; A=21-247.
DR PDBsum; 1FQ3; -.
DR PDBsum; 1IAU; -.
DR AlphaFoldDB; P10144; -.
DR SMR; P10144; -.
DR BioGRID; 109257; 30.
DR IntAct; P10144; 6.
DR MINT; P10144; -.
DR STRING; 9606.ENSP00000216341; -.
DR BindingDB; P10144; -.
DR ChEMBL; CHEMBL2316; -.
DR GuidetoPHARMACOLOGY; 2369; -.
DR MEROPS; S01.010; -.
DR GlyGen; P10144; 3 sites, 2 O-linked glycans (1 site).
DR iPTMnet; P10144; -.
DR PhosphoSitePlus; P10144; -.
DR BioMuta; GZMB; -.
DR DMDM; 317373361; -.
DR jPOST; P10144; -.
DR MassIVE; P10144; -.
DR PaxDb; P10144; -.
DR PeptideAtlas; P10144; -.
DR PRIDE; P10144; -.
DR ProteomicsDB; 52569; -.
DR ABCD; P10144; 3 sequenced antibodies.
DR Antibodypedia; 187; 1171 antibodies from 51 providers.
DR DNASU; 3002; -.
DR Ensembl; ENST00000216341.9; ENSP00000216341.4; ENSG00000100453.14.
DR GeneID; 3002; -.
DR KEGG; hsa:3002; -.
DR MANE-Select; ENST00000216341.9; ENSP00000216341.4; NM_004131.6; NP_004122.2.
DR UCSC; uc001wps.4; human.
DR CTD; 3002; -.
DR DisGeNET; 3002; -.
DR GeneCards; GZMB; -.
DR HGNC; HGNC:4709; GZMB.
DR HPA; ENSG00000100453; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 123910; gene.
DR neXtProt; NX_P10144; -.
DR OpenTargets; ENSG00000100453; -.
DR VEuPathDB; HostDB:ENSG00000100453; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P10144; -.
DR OMA; PAYNPEK; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P10144; -.
DR TreeFam; TF333630; -.
DR BRENDA; 3.4.21.79; 2681.
DR PathwayCommons; P10144; -.
DR Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
DR Reactome; R-HSA-5620971; Pyroptosis.
DR Reactome; R-HSA-75108; Activation, myristolyation of BID and translocation to mitochondria.
DR SignaLink; P10144; -.
DR SIGNOR; P10144; -.
DR BioGRID-ORCS; 3002; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; GZMB; human.
DR EvolutionaryTrace; P10144; -.
DR GeneWiki; GZMB; -.
DR GenomeRNAi; 3002; -.
DR Pharos; P10144; Tchem.
DR PRO; PR:P10144; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P10144; protein.
DR Bgee; ENSG00000100453; Expressed in granulocyte and 126 other tissues.
DR ExpressionAtlas; P10144; baseline and differential.
DR Genevisible; P10144; HS.
DR GO; GO:0044194; C:cytolytic granule; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001772; C:immunological synapse; TAS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; IDA:UniProtKB.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:CACAO.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
DR GO; GO:0070269; P:pyroptosis; IDA:UniProtKB.
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; Apoptosis; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:15340161"
FT PROPEP 19..20
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1985927,
FT ECO:0000269|PubMed:3262682, ECO:0000269|PubMed:3263427,
FT ECO:0000269|PubMed:8258716"
FT /id="PRO_0000027399"
FT CHAIN 21..247
FT /note="Granzyme B"
FT /id="PRO_0000027400"
FT DOMAIN 21..245
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:11209755,
FT ECO:0000269|PubMed:11325591"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:11209755,
FT ECO:0000269|PubMed:11325591"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:11209755,
FT ECO:0000269|PubMed:11325591"
FT SITE 228
FT /note="Mediates preference for Asp-containing substrates"
FT /evidence="ECO:0000250|UniProtKB:P18291"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11325591"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11325591"
FT DISULFID 49..65
FT /evidence="ECO:0000269|PubMed:11209755,
FT ECO:0000269|PubMed:11325591"
FT DISULFID 142..209
FT /evidence="ECO:0000269|PubMed:11209755,
FT ECO:0000269|PubMed:11325591"
FT DISULFID 173..188
FT /evidence="ECO:0000269|PubMed:11209755,
FT ECO:0000269|PubMed:11325591"
FT VARIANT 55
FT /note="R -> Q (in dbSNP:rs8192917)"
FT /evidence="ECO:0000269|PubMed:12721789,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2332171,
FT ECO:0000269|PubMed:2365998, ECO:0000269|PubMed:2788607,
FT ECO:0000269|PubMed:2953813, ECO:0000269|PubMed:3261871"
FT /id="VAR_018371"
FT VARIANT 94
FT /note="P -> A (in dbSNP:rs11539752)"
FT /evidence="ECO:0000269|PubMed:2332171,
FT ECO:0000269|PubMed:3258865"
FT /id="VAR_047409"
FT VARIANT 247
FT /note="Y -> H (in dbSNP:rs2236338)"
FT /evidence="ECO:0000269|PubMed:12721789,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_018381"
FT CONFLICT 32..33
FT /note="RP -> PR (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="V -> G (in Ref. 3; AAA52118)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="V -> C (in Ref. 4; AAB59528)"
FT /evidence="ECO:0000305"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1IAU"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:1IAU"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:1FQ3"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:1IAU"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:1IAU"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:1IAU"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:1IAU"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:1IAU"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1IAU"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1IAU"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:1IAU"
SQ SEQUENCE 247 AA; 27716 MW; C652271918EF24F9 CRC64;
MQPILLLLAF LLLPRADAGE IIGGHEAKPH SRPYMAYLMI WDQKSLKRCG GFLIRDDFVL
TAAHCWGSSI NVTLGAHNIK EQEPTQQFIP VKRPIPHPAY NPKNFSNDIM LLQLERKAKR
TRAVQPLRLP SNKAQVKPGQ TCSVAGWGQT APLGKHSHTL QEVKMTVQED RKCESDLRHY
YDSTIELCVG DPEIKKTSFK GDSGGPLVCN KVAQGIVSYG RNNGMPPRAC TKVSSFVHWI
KKTMKRY
