TRY4_RAT
ID TRY4_RAT Reviewed; 247 AA.
AC P12788;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Trypsin-4;
DE EC=3.4.21.4;
DE AltName: Full=Pretrypsinogen IV;
DE AltName: Full=Trypsin IV;
DE Flags: Precursor;
GN Name=Try4;
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 [MRNA].
RC STRAIN=Wistar; TISSUE=Pancreas;
RX PubMed=2780302; DOI=10.1093/nar/17.16.6736;
RA Luetcke H.A., Rausch U., Vasiloudes P., Scheele G.A., Kern H.F.;
RT "A fourth trypsinogen (P23) in the rat pancreas induced by CCK.";
RL Nucleic Acids Res. 17:6736-6736(1989).
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; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- INDUCTION: By CCK.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15679; CAA33718.1; -; mRNA.
DR PIR; S05494; S05494.
DR RefSeq; NP_775423.1; NM_173301.1.
DR AlphaFoldDB; P12788; -.
DR SMR; P12788; -.
DR STRING; 10116.ENSRNOP00000017852; -.
DR MEROPS; S01.183; -.
DR PaxDb; P12788; -.
DR Ensembl; ENSRNOT00000017852; ENSRNOP00000017852; ENSRNOG00000013245.
DR GeneID; 286960; -.
DR KEGG; rno:286960; -.
DR UCSC; RGD:708585; rat.
DR RGD; 708585; LOC286960.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01050000244883; -.
DR HOGENOM; CLU_006842_7_0_1; -.
DR InParanoid; P12788; -.
DR OMA; SDASCHE; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P12788; -.
DR TreeFam; TF331065; -.
DR PRO; PR:P12788; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000013245; Expressed in pancreas and 2 other tissues.
DR Genevisible; P12788; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IEA:UniProtKB-KW.
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 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 2: Evidence at transcript level;
KW Calcium; Digestion; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..15
FT PROPEP 16..23
FT /note="Activation peptide"
FT /id="PRO_0000028213"
FT CHAIN 24..247
FT /note="Trypsin-4"
FT /id="PRO_0000028214"
FT DOMAIN 24..245
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 30..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 49..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 133..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 140..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 172..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 197..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 247 AA; 26573 MW; AE987B9D32D58F93 CRC64;
MKISIFFAFL GAAVALPVND DDKIVGGYTC PKHLVPYQVS LHDGISHQCG GSLISDQWVL
SAAHCYKRKL QVRLGEHNIH VLEGGEQFID AEKIIRHPEY NKDTLDNDIM LIKLKSPAVL
NSQVSTVSLP RSCASTDAQC LVSGWGNTVS IGGKYPALLQ CLEAPVLSAS SCKKSYPGQI
TSNMFCLGFL EGGKDSCDGD SGGPVVCNGE IQGIVSWGSV CAMRGKPGVY TKVCNYLSWI
QETMANN
