TRY1_GADMO
ID TRY1_GADMO Reviewed; 241 AA.
AC P16049; Q91040; Q92156;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Trypsin-1;
DE EC=3.4.21.4;
DE AltName: Full=Trypsin I;
DE Flags: Precursor;
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pyloric caecum;
RX PubMed=8223632; DOI=10.1111/j.1432-1033.1993.tb18341.x;
RA Gudmundsdottir A., Gudmundsdottir E., Oskarsson S., Bjarnason J.B.,
RA Eakin A.E., Craik C.S.;
RT "Isolation and characterization of cDNAs from Atlantic cod encoding two
RT different forms of trypsinogen.";
RL Eur. J. Biochem. 217:1091-1097(1993).
RN [2]
RP PROTEIN SEQUENCE OF 20-58.
RC TISSUE=Pyloric caecum;
RX PubMed=2707266; DOI=10.1111/j.1432-1033.1989.tb14618.x;
RA Asgeirsson B., Fox J.W., Bjarnason J.B.;
RT "Purification and characterization of trypsin from the poikilotherm Gadus
RT morhua.";
RL Eur. J. Biochem. 180:85-94(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
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; X76886; CAA54214.1; -; mRNA.
DR PIR; S39047; S39047.
DR PDB; 2EEK; X-ray; 1.85 A; A=20-239.
DR PDBsum; 2EEK; -.
DR AlphaFoldDB; P16049; -.
DR SMR; P16049; -.
DR MEROPS; S01.125; -.
DR EvolutionaryTrace; P16049; -.
DR Proteomes; UP000694546; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 3D-structure; Digestion; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..13
FT /evidence="ECO:0000255"
FT PROPEP 14..19
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2707266"
FT /id="PRO_0000028309"
FT CHAIN 20..241
FT /note="Trypsin-1"
FT /id="PRO_0000028310"
FT DOMAIN 20..239
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 59
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 103
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 189
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 26..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 44..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 128..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 135..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 166..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 191..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 25
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..28
FT /note="TK -> EA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="F -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..52
FT /note="VSKD -> IN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 28..33
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 34..48
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2EEK"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:2EEK"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:2EEK"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:2EEK"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2EEK"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:2EEK"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:2EEK"
SQ SEQUENCE 241 AA; 25941 MW; 44EC9A0106AD1A68 CRC64;
MKSLIFVLLL GAVFAEEDKI VGGYECTKHS QAHQVSLNSG YHFCGGSLVS KDWVVSAAHC
YKSVLRVRLG EHHIRVNEGT EQYISSSSVI RHPNYSSYNI NNDIMLIKLT KPATLNQYVH
AVALPTECAA DATMCTVSGW GNTMSSVADG DKLQCLSLPI LSHADCANSY PGMITQSMFC
AGYLEGGKDS CQGDSGGPVV CNGVLQGVVS WGYGCAERDH PGVYAKVCVL SGWVRDTMAN
Y
