TRYG1_MOUSE
ID TRYG1_MOUSE Reviewed; 311 AA.
AC Q9QUL7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Tryptase gamma;
DE EC=3.4.21.-;
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; Synonyms=Tmt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv, and BALB/cJ;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Tryptase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF175760; AAF03698.1; -; Genomic_DNA.
DR EMBL; AF175523; AAF03696.1; -; mRNA.
DR EMBL; BC019974; AAH19974.1; -; mRNA.
DR EMBL; BC052325; AAH52325.1; -; mRNA.
DR CCDS; CCDS28518.1; -.
DR AlphaFoldDB; Q9QUL7; -.
DR SMR; Q9QUL7; -.
DR STRING; 10090.ENSMUSP00000024999; -.
DR MEROPS; S01.028; -.
DR GlyGen; Q9QUL7; 2 sites.
DR PhosphoSitePlus; Q9QUL7; -.
DR PaxDb; Q9QUL7; -.
DR PRIDE; Q9QUL7; -.
DR UCSC; uc008bat.1; mouse.
DR MGI; MGI:1349391; Tpsg1.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q9QUL7; -.
DR PhylomeDB; Q9QUL7; -.
DR ChiTaRS; Tpsg1; mouse.
DR PRO; PR:Q9QUL7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QUL7; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:MGI.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..311
FT /note="Tryptase gamma"
FT /id="PRO_0000027501"
FT CHAIN 17..28
FT /note="Tryptase gamma light chain"
FT /id="PRO_0000027502"
FT CHAIN 30..311
FT /note="Tryptase gamma heavy chain"
FT /id="PRO_0000027503"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 30..262
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 70
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 117
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 18..137
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 55..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 151..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 184..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 210..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 311 AA; 32656 MW; 7FC9D6EF6A2A8808 CRC64;
MALGPNCGIL LFLAVSGCGH PQVSNSGSRI VGGHAAPAGT WPWQASLRLH KVHVCGGSLL
SPEWVLTAAH CFSGSVNSSD YQVHLGELTV TLSPHFSTVK RIIMYTGSPG PPGSSGDIAL
VQLSSPVALS SQVQPVCLPE ASADFYPGMQ CWVTGWGYTG EGEPLKPPYN LQEAKVSVVD
VKTCSQAYNS PNGSLIQPDM LCARGPGDAC QDDSGGPLVC QVAGTWQQAG VVSWGEGCGR
PDRPGVYARV TAYVNWIHHH IPEAGGSGMQ GLPWAPLLAA LFWPSLFLLL VSGVLMAKYW
LSSPSHAASE L
