TRYG1_HUMAN
ID TRYG1_HUMAN Reviewed; 321 AA.
AC Q9NRR2; Q96RZ8; Q9C015; Q9NRQ8; Q9UBB2;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Tryptase gamma {ECO:0000305};
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 31;
DE AltName: Full=Transmembrane tryptase;
DE Contains:
DE RecName: Full=Tryptase gamma light chain;
DE Contains:
DE RecName: Full=Tryptase gamma heavy chain;
DE Flags: Precursor;
GN Name=TPSG1 {ECO:0000312|HGNC:HGNC:14134}; Synonyms=PRSS31, TMT;
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 [GENOMIC DNA / MRNA], AND VARIANTS MET-60; ILE-239 AND
RP LEU-288.
RX PubMed=10521469; DOI=10.1074/jbc.274.43.30784;
RA Wong G.W., Tang Y., Feyfant E., Sali A., Li L., Li Y., Huang C.,
RA Friend D.S., Krilis S.A., Stevens R.L.;
RT "Identification of a new member of the tryptase family of mouse and human
RT mast cell proteases which possesses a novel COOH-terminal hydrophobic
RT extension.";
RL J. Biol. Chem. 274:30784-30793(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-60; MET-126; THR-132;
RP SER-160; ILE-204; ILE-239 AND LEU-288.
RX PubMed=10843716; DOI=10.4049/jimmunol.164.12.6566;
RA Caughey G.H., Raymond W.W., Blount J.L., Hau L.W., Pallaoro M.,
RA Wolters P.J., Verghese G.M.;
RT "Characterization of human gamma-tryptases, novel members of the chromosome
RT 16p mast cell tryptase and prostasin gene families.";
RL J. Immunol. 164:6566-6575(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-239.
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 220-321, AND VARIANTS ILE-239 AND
RP LEU-288.
RA Mittman S., Agnew W.S.;
RT "Organization and alternative splicing of CACNA1H.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- INTERACTION:
CC Q9NRR2; P37235: HPCAL1; NbExp=3; IntAct=EBI-17210651, EBI-749311;
CC Q9NRR2; P61601: NCALD; NbExp=3; IntAct=EBI-17210651, EBI-749635;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC -!- POLYMORPHISM: There are two alleles; gamma-I and gamma-II which differ
CC by 5 residues. {ECO:0000269|PubMed:10843716,
CC ECO:0000269|PubMed:11157797}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF175522; AAF03695.1; -; mRNA.
DR EMBL; AF175759; AAF03697.1; -; Genomic_DNA.
DR EMBL; AF191031; AAF76457.1; -; Genomic_DNA.
DR EMBL; AF195508; AAF76458.1; -; Genomic_DNA.
DR EMBL; AE006466; AAK61269.1; -; Genomic_DNA.
DR EMBL; AC120498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF223563; AAG48852.2; -; Genomic_DNA.
DR CCDS; CCDS10430.1; -.
DR RefSeq; NP_036599.3; NM_012467.3.
DR AlphaFoldDB; Q9NRR2; -.
DR BioGRID; 117351; 14.
DR IntAct; Q9NRR2; 3.
DR STRING; 9606.ENSP00000234798; -.
DR BindingDB; Q9NRR2; -.
DR ChEMBL; CHEMBL4955; -.
DR MEROPS; S01.028; -.
DR GlyGen; Q9NRR2; 1 site.
DR iPTMnet; Q9NRR2; -.
DR PhosphoSitePlus; Q9NRR2; -.
DR BioMuta; TPSG1; -.
DR DMDM; 296453005; -.
DR MassIVE; Q9NRR2; -.
DR PaxDb; Q9NRR2; -.
DR PeptideAtlas; Q9NRR2; -.
DR PRIDE; Q9NRR2; -.
DR ProteomicsDB; 82407; -.
DR Antibodypedia; 22993; 219 antibodies from 16 providers.
DR DNASU; 25823; -.
DR Ensembl; ENST00000234798.5; ENSP00000234798.4; ENSG00000116176.7.
DR GeneID; 25823; -.
DR KEGG; hsa:25823; -.
DR MANE-Select; ENST00000234798.5; ENSP00000234798.4; NM_012467.4; NP_036599.4.
DR UCSC; uc002ckw.3; human.
DR CTD; 25823; -.
DR DisGeNET; 25823; -.
DR GeneCards; TPSG1; -.
DR HGNC; HGNC:14134; TPSG1.
DR HPA; ENSG00000116176; Tissue enriched (intestine).
DR MIM; 609341; gene.
DR neXtProt; NX_Q9NRR2; -.
DR OpenTargets; ENSG00000116176; -.
DR PharmGKB; PA37849; -.
DR VEuPathDB; HostDB:ENSG00000116176; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000163349; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q9NRR2; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9NRR2; -.
DR TreeFam; TF351676; -.
DR PathwayCommons; Q9NRR2; -.
DR SignaLink; Q9NRR2; -.
DR BioGRID-ORCS; 25823; 19 hits in 1069 CRISPR screens.
DR GeneWiki; TPSG1; -.
DR GenomeRNAi; 25823; -.
DR Pharos; Q9NRR2; Tchem.
DR PRO; PR:Q9NRR2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NRR2; protein.
DR Bgee; ENSG00000116176; Expressed in mucosa of transverse colon and 128 other tissues.
DR Genevisible; Q9NRR2; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 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.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..321
FT /note="Tryptase gamma"
FT /id="PRO_0000027498"
FT CHAIN 20..36
FT /note="Tryptase gamma light chain"
FT /id="PRO_0000027499"
FT CHAIN 38..321
FT /note="Tryptase gamma heavy chain"
FT /id="PRO_0000027500"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 38..270
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 78
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..145
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 63..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 159..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 192..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 218..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 60
FT /note="V -> M (in allele gamma-II; dbSNP:rs760357)"
FT /evidence="ECO:0000269|PubMed:10521469,
FT ECO:0000269|PubMed:10843716"
FT /id="VAR_012097"
FT VARIANT 126
FT /note="I -> M (in allele gamma-II)"
FT /evidence="ECO:0000269|PubMed:10843716"
FT /id="VAR_012098"
FT VARIANT 132
FT /note="S -> T (in allele gamma-II)"
FT /evidence="ECO:0000269|PubMed:10843716"
FT /id="VAR_012099"
FT VARIANT 160
FT /note="W -> S (in dbSNP:rs4984638)"
FT /evidence="ECO:0000269|PubMed:10843716"
FT /id="VAR_025012"
FT VARIANT 204
FT /note="L -> I (in allele gamma-II)"
FT /evidence="ECO:0000269|PubMed:10843716"
FT /id="VAR_012100"
FT VARIANT 239
FT /note="T -> I (in dbSNP:rs11248860)"
FT /evidence="ECO:0000269|PubMed:10521469,
FT ECO:0000269|PubMed:10843716, ECO:0000269|PubMed:11157797,
FT ECO:0000269|Ref.5"
FT /id="VAR_061773"
FT VARIANT 288
FT /note="F -> L (in allele gamma-II; dbSNP:rs1004041)"
FT /evidence="ECO:0000269|PubMed:10521469,
FT ECO:0000269|PubMed:10843716, ECO:0000269|Ref.5"
FT /id="VAR_012101"
SQ SEQUENCE 321 AA; 33817 MW; D2F51D51366A08D7 CRC64;
MALGACGLLL LLAVPGVSLR TLQPGCGRPQ VSDAGGRIVG GHAAPAGAWP WQASLRLRRV
HVCGGSLLSP QWVLTAAHCF SGSLNSSDYQ VHLGELEITL SPHFSTVRQI ILHSSPSGQP
GTSGDIALVE LSVPVTLSSR ILPVCLPEAS DDFCPGIRCW VTGWGYTREG EPLPPPYSLR
EVKVSVVDTE TCRRDYPGPG GSILQPDMLC ARGPGDACQD DSGGPLVCQV NGAWVQAGTV
SWGEGCGRPN RPGVYTRVPA YVNWIRRHIT ASGGSESGYP RLPLLAGFFL PGLFLLLVSC
VLLAKCLLHP SADGTPFPAP D
