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Granzyme H (EC 3.4.21.-) (CCP-X) (Cathepsin G-like 2) (CTSGL2) (Cytotoxic T-lymphocyte proteinase) (Cytotoxic serine protease C) (CSP-C)

 GRAH_HUMAN              Reviewed;         246 AA.
P20718; G3V2C5; Q6XGZ0; Q6XGZ1;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
28-FEB-2018, entry version 161.
RecName: Full=Granzyme H;
EC=3.4.21.-;
AltName: Full=CCP-X;
AltName: Full=Cathepsin G-like 2;
Short=CTSGL2;
AltName: Full=Cytotoxic T-lymphocyte proteinase;
AltName: Full=Cytotoxic serine protease C;
Short=CSP-C;
Flags: Precursor;
Name=GZMH; Synonyms=CGL2, CTSGL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2193684; DOI=10.1021/bi00469a003;
Meier M., Kwong P.C., Fregeau C.J., Atkinson E.A., Burrington M.,
Ehrman N., Sorensen O., Lin C.C., Wilkins J., Bleackley R.C.;
"Cloning of a gene that encodes a new member of the human cytotoxic
cell protease family.";
Biochemistry 29:4042-4049(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2049336; DOI=10.1093/intimm/3.1.57;
Haddad P., Jenne D.E., Tschopp J., Clement M.-V., Mathieu-Mahul D.,
Sasportes M.;
"Structure and evolutionary origin of the human granzyme H gene.";
Int. Immunol. 3:57-66(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2402757; DOI=10.1111/j.1399-0039.1990.tb01787.x;
Klein J.L., Selvakumar A., Trapani J.A., Dupont B.;
"Characterization of a novel, human cytotoxic lymphocyte-specific
serine protease cDNA clone (CSP-C).";
Tissue Antigens 35:220-228(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Leukemic T-cell;
Kothapalli R., Kusmartseva I., Loughran T.P. Jr.;
"Identification and characterization of granzyme H splice variants 2
and 3 from large granular lymphocyte leukemia.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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).
[8]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-246 OF MUTANT ASN-102
ALONE AND IN COMPLEX WITH SUBSTRATE PEPTIDE AND INHIBITOR, FUNCTION,
SUBSTRATE SPECIFICITY, AND DISULFIDE BONDS.
PubMed=22156497; DOI=10.4049/jimmunol.1101381;
Wang L., Zhang K., Wu L., Liu S., Zhang H., Zhou Q., Tong L., Sun F.,
Fan Z.;
"Structural insights into the substrate specificity of human granzyme
H: the functional roles of a novel RKR motif.";
J. Immunol. 188:765-773(2012).
[9]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-246 IN COMPLEX WITH
SERPINB1, FUNCTION, DISULFIDE BONDS, TISSUE SPECIFICITY, AND ENZYME
REGULATION.
PubMed=23269243; DOI=10.4049/jimmunol.1202542;
Wang L., Li Q., Wu L., Liu S., Zhang Y., Yang X., Zhu P., Zhang H.,
Zhang K., Lou J., Liu P., Tong L., Sun F., Fan Z.;
"Identification of SERPINB1 as a physiological inhibitor of human
granzyme H.";
J. Immunol. 190:1319-1330(2013).
-!- FUNCTION: Cytotoxic chymotrypsin-like serine protease with
preference for bulky and aromatic residues at the P1 position and
acidic residues at the P3' and P4' sites. Probably necessary for
target cell lysis in cell-mediated immune responses. Participates
in the antiviral response via direct cleavage of several proteins
essential for viral replication. {ECO:0000269|PubMed:22156497,
ECO:0000269|PubMed:23269243}.
-!- ENZYME REGULATION: Inhibited by SERPINB1.
{ECO:0000269|PubMed:23269243}.
-!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic
granules of cytolytic T-lymphocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P20718-1; Sequence=Displayed;
Name=2;
IsoId=P20718-2; Sequence=VSP_047073;
Name=3;
IsoId=P20718-3; Sequence=VSP_047573;
-!- TISSUE SPECIFICITY: Constitutively expressed in NK cells.
{ECO:0000269|PubMed:23269243}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; J02907; AAA76859.1; -; Genomic_DNA.
EMBL; M57888; AAA03514.1; -; Genomic_DNA.
EMBL; M36118; AAA03248.1; -; mRNA.
EMBL; M72150; AAA74885.1; -; Genomic_DNA.
EMBL; AY232657; AAP70247.1; -; mRNA.
EMBL; AY232658; AAP70248.1; -; mRNA.
EMBL; AL136018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW66004.1; -; Genomic_DNA.
EMBL; BC027974; AAH27974.1; -; mRNA.
CCDS; CCDS59243.1; -. [P20718-2]
CCDS; CCDS9632.1; -. [P20718-1]
PIR; A32692; A32692.
RefSeq; NP_001257710.1; NM_001270781.1. [P20718-2]
RefSeq; NP_219491.1; NM_033423.4. [P20718-1]
UniGene; Hs.348264; -.
PDB; 1LXV; Model; -; A=21-246.
PDB; 3TJU; X-ray; 2.70 A; A=21-246.
PDB; 3TJV; X-ray; 2.40 A; A=21-246.
PDB; 3TK9; X-ray; 2.20 A; A=21-246.
PDB; 4GAW; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=21-246.
PDBsum; 1LXV; -.
PDBsum; 3TJU; -.
PDBsum; 3TJV; -.
PDBsum; 3TK9; -.
PDBsum; 4GAW; -.
ProteinModelPortal; P20718; -.
SMR; P20718; -.
BioGrid; 109254; 1.
IntAct; P20718; 1.
MINT; P20718; -.
STRING; 9606.ENSP00000216338; -.
MEROPS; S01.147; -.
PhosphoSitePlus; P20718; -.
DMDM; 121590; -.
PaxDb; P20718; -.
PeptideAtlas; P20718; -.
PRIDE; P20718; -.
DNASU; 2999; -.
Ensembl; ENST00000216338; ENSP00000216338; ENSG00000100450. [P20718-1]
Ensembl; ENST00000382548; ENSP00000371988; ENSG00000100450. [P20718-2]
GeneID; 2999; -.
KEGG; hsa:2999; -.
UCSC; uc001wpr.3; human. [P20718-1]
CTD; 2999; -.
DisGeNET; 2999; -.
EuPathDB; HostDB:ENSG00000100450.12; -.
GeneCards; GZMH; -.
HGNC; HGNC:4710; GZMH.
HPA; HPA029200; -.
MIM; 116831; gene.
neXtProt; NX_P20718; -.
OpenTargets; ENSG00000100450; -.
PharmGKB; PA29088; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P20718; -.
KO; K09616; -.
OMA; YIKVSHF; -.
OrthoDB; EOG091G0G5F; -.
PhylomeDB; P20718; -.
TreeFam; TF333630; -.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
GeneWiki; GZMH; -.
GenomeRNAi; 2999; -.
PRO; PR:P20718; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100450; -.
CleanEx; HS_GZMH; -.
ExpressionAtlas; P20718; baseline and differential.
Genevisible; P20718; HS.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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;
3D-structure; Alternative splicing; Complete proteome; Cytolysis;
Disulfide bond; Glycoprotein; Hydrolase; Polymorphism; Protease;
Reference proteome; Serine protease; Signal; Zymogen.
SIGNAL 1 18
PROPEP 19 20 Activation peptide.
/FTId=PRO_0000027413.
CHAIN 21 246 Granzyme H.
/FTId=PRO_0000027414.
DOMAIN 21 244 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 46 48 Mediates the preference for acidic
residues at the P3' and P4' sites.
ACT_SITE 64 64 Charge relay system. {ECO:0000250}.
ACT_SITE 108 108 Charge relay system. {ECO:0000250}.
ACT_SITE 202 202 Charge relay system. {ECO:0000250}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 65
DISULFID 142 208
DISULFID 172 187
VAR_SEQ 69 199 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_047573.
VAR_SEQ 114 199 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_047073.
VARIANT 84 84 R -> Q (in dbSNP:rs20545).
/FTId=VAR_014556.
CONFLICT 68 68 S -> R (in Ref. 4; AAP70248).
{ECO:0000305}.
STRAND 35 44 {ECO:0000244|PDB:3TK9}.
STRAND 46 55 {ECO:0000244|PDB:3TK9}.
STRAND 58 61 {ECO:0000244|PDB:3TK9}.
HELIX 63 65 {ECO:0000244|PDB:3TJV}.
STRAND 68 75 {ECO:0000244|PDB:3TK9}.
STRAND 87 96 {ECO:0000244|PDB:3TK9}.
HELIX 98 100 {ECO:0000244|PDB:4GAW}.
TURN 102 105 {ECO:0000244|PDB:3TK9}.
STRAND 110 116 {ECO:0000244|PDB:3TK9}.
STRAND 121 123 {ECO:0000244|PDB:4GAW}.
STRAND 141 147 {ECO:0000244|PDB:3TK9}.
STRAND 149 153 {ECO:0000244|PDB:3TK9}.
STRAND 160 167 {ECO:0000244|PDB:3TK9}.
HELIX 169 175 {ECO:0000244|PDB:3TK9}.
TURN 176 178 {ECO:0000244|PDB:3TK9}.
TURN 182 184 {ECO:0000244|PDB:3TK9}.
STRAND 185 189 {ECO:0000244|PDB:3TK9}.
TURN 199 203 {ECO:0000244|PDB:3TK9}.
STRAND 205 208 {ECO:0000244|PDB:3TK9}.
STRAND 211 218 {ECO:0000244|PDB:3TK9}.
STRAND 221 223 {ECO:0000244|PDB:4GAW}.
STRAND 227 231 {ECO:0000244|PDB:3TK9}.
TURN 232 235 {ECO:0000244|PDB:3TK9}.
HELIX 236 244 {ECO:0000244|PDB:3TK9}.
SEQUENCE 246 AA; 27315 MW; CA6A87F3DA5F1E71 CRC64;
MQPFLLLLAF LLTPGAGTEE IIGGHEAKPH SRPYMAFVQF LQEKSRKRCG GILVRKDFVL
TAAHCQGSSI NVTLGAHNIK EQERTQQFIP VKRPIPHPAY NPKNFSNDIM LLQLERKAKW
TTAVRPLRLP SSKAQVKPGQ LCSVAGWGYV SMSTLATTLQ EVLLTVQKDC QCERLFHGNY
SRATEICVGD PKKTQTGFKG DSGGPLVCKD VAQGILSYGN KKGTPPGVYI KVSHFLPWIK
RTMKRL


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