TRY1_RAT
ID TRY1_RAT Reviewed; 246 AA.
AC P00762;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Serine protease 1 {ECO:0000312|RGD:3417};
DE EC=3.4.21.4;
DE AltName: Full=Anionic trypsin I {ECO:0000312|RGD:3417};
DE AltName: Full=Anionic trypsin-1 {ECO:0000312|RGD:3417};
DE AltName: Full=Beta-trypsin;
DE AltName: Full=Cationic trypsinogen;
DE AltName: Full=Pretrypsinogen I {ECO:0000312|RGD:3417};
DE AltName: Full=Trypsin I {ECO:0000250|UniProtKB:P07477};
DE AltName: Full=Trypsin-1;
DE Flags: Precursor;
GN Name=Prss1 {ECO:0000312|RGD:3417};
GN Synonyms=Trp1, Try1 {ECO:0000250|UniProtKB:P07477}, Tryp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=6896710; DOI=10.1016/s0021-9258(18)34133-4;
RA MacDonald R.J., Stary S.J., Swift G.H.;
RT "Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide
RT sequences of the cloned cDNAs.";
RL J. Biol. Chem. 257:9724-9732(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6094547; DOI=10.1016/s0021-9258(18)89886-6;
RA Craik C.S., Choo Q.L., Swift G.H., Quinto C., MacDonald R.J., Rutter W.J.;
RT "Structure of two related rat pancreatic trypsin genes.";
RL J. Biol. Chem. 259:14255-14264(1984).
RN [3]
RP PROTEIN SEQUENCE OF 73-92 AND 96-112, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Lubec S., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- SUBUNIT: Interacts with SERPINA1. {ECO:0000250|UniProtKB:P00760}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- MISCELLANEOUS: This sequence represents the precursor of the major form
CC of trypsin produced by the adult pancreas.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; V01273; CAA24580.1; -; mRNA.
DR EMBL; J00778; AAA98518.1; -; Genomic_DNA.
DR PIR; B22657; TRRT1.
DR RefSeq; NP_036767.1; NM_012635.1.
DR AlphaFoldDB; P00762; -.
DR SMR; P00762; -.
DR BioGRID; 246823; 3.
DR IntAct; P00762; 1.
DR STRING; 10116.ENSRNOP00000043068; -.
DR BindingDB; P00762; -.
DR ChEMBL; CHEMBL3638328; -.
DR MEROPS; S01.094; -.
DR iPTMnet; P00762; -.
DR PhosphoSitePlus; P00762; -.
DR jPOST; P00762; -.
DR PaxDb; P00762; -.
DR PRIDE; P00762; -.
DR Ensembl; ENSRNOT00000108811; ENSRNOP00000086707; ENSRNOG00000063605.
DR GeneID; 24691; -.
DR KEGG; rno:24691; -.
DR UCSC; RGD:3417; rat.
DR CTD; 5644; -.
DR RGD; 3417; Prss1.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01050000244883; -.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; P00762; -.
DR OMA; MMIITET; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P00762; -.
DR TreeFam; TF331065; -.
DR PRO; PR:P00762; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000032156; Expressed in pancreas and 11 other tissues.
DR Genevisible; P00762; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; TAS:RGD.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0031000; P:response to caffeine; IDA:RGD.
DR GO; GO:0035094; P:response to nicotine; IDA:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
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 Calcium; Digestion; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000250"
FT PROPEP 16..23
FT /note="Activation peptide"
FT /id="PRO_0000028207"
FT CHAIN 24..246
FT /note="Serine protease 1"
FT /id="PRO_0000028208"
FT DOMAIN 24..244
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 63
FT /note="Charge relay system"
FT ACT_SITE 107
FT /note="Charge relay system"
FT ACT_SITE 200
FT /note="Charge relay system"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT SITE 194
FT /note="Required for specificity"
FT DISULFID 30..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 48..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 132..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 139..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 171..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 196..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 246 AA; 25959 MW; 6AFA0DAD11943FB5 CRC64;
MSALLILALV GAAVAFPLED DDKIVGGYTC PEHSVPYQVS LNSGYHFCGG SLINDQWVVS
AAHCYKSRIQ VRLGEHNINV LEGDEQFINA AKIIKHPNYS SWTLNNDIML IKLSSPVKLN
ARVAPVALPS ACAPAGTQCL ISGWGNTLSN GVNNPDLLQC VDAPVLSQAD CEAAYPGEIT
SSMICVGFLE GGKDSCQGDS GGPVVCNGQL QGIVSWGYGC ALPDNPGVYT KVCNFVGWIQ
DTIAAN
