ID   TRYA_RAT                Reviewed;         246 AA.
AC   P32821;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Trypsin V-A;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
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   TISSUE=Pancreas;
RX   PubMed=1537555; DOI=10.1016/0378-1119(92)90646-7;
RA   Kang J., Wiegand U., Mueller-Hill B.;
RT   "Identification of cDNAs encoding two novel rat pancreatic serine
RT   proteases.";
RL   Gene 110:181-187(1992).
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   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; X59012; CAA41751.1; -; mRNA.
DR   PIR; JQ1471; JQ1471.
DR   RefSeq; NP_001101326.1; NM_001107856.1.
DR   AlphaFoldDB; P32821; -.
DR   SMR; P32821; -.
DR   STRING; 10116.ENSRNOP00000017673; -.
DR   MEROPS; S01.092; -.
DR   PaxDb; P32821; -.
DR   PRIDE; P32821; -.
DR   Ensembl; ENSRNOT00000017673; ENSRNOP00000017673; ENSRNOG00000013203.
DR   GeneID; 312273; -.
DR   KEGG; rno:312273; -.
DR   UCSC; RGD:1563848; rat.
DR   RGD; 1563848; LOC312273.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01050000244883; -.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   InParanoid; P32821; -.
DR   OMA; EHNIWEP; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF331065; -.
DR   PRO; PR:P32821; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000013203; Expressed in pancreas and 10 other tissues.
DR   Genevisible; P32821; 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   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   Calcium; Digestion; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..15
FT   PROPEP          16..24
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028215"
FT   CHAIN           25..246
FT                   /note="Trypsin V-A"
FT                   /id="PRO_0000028216"
FT   DOMAIN          25..244
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        200
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         86
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            194
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        49..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        133..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        140..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;  26901 MW;  1EBE59D88BAB1715 CRC64;
     MKICIFFTLL GTVAAFPTED NDDRIVGGYT CQEHSVPYQV SLNAGSHICG GSLITDQWVL
     SAAHCYHPQL QVRLGEHNIY EIEGAEQFID AAKMILHPDY DKWTVDNDIM LIKLKSPATL
     NSKVSTIPLP QYCPTAGTEC LVSGWGVLKF GFESPSVLQC LDAPVLSDSV CHKAYPRQIT
     NNMFCLGFLE GGKDSCQYDS GGPVVCNGEV QGIVSWGDGC ALEGKPGVYT KVCNYLNWIH
     QTIAEN