TRY3_CHICK
ID TRY3_CHICK Reviewed; 248 AA.
AC Q90629;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Trypsin II-P29;
DE EC=3.4.21.4;
DE Flags: Precursor;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=7733885; DOI=10.1042/bj3070471;
RA Wang K., Gan L., Lee I., Hood L.E.;
RT "Isolation and characterization of the chicken trypsinogen gene family.";
RL Biochem. J. 307:471-479(1995).
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 -!- TISSUE SPECIFICITY: High levels are seen in the pancreas while lower
CC levels are found in the liver, spleen and thymus.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; U15157; AAA79914.1; -; mRNA.
DR PIR; S55066; S55066.
DR RefSeq; NP_990715.1; NM_205384.1.
DR AlphaFoldDB; Q90629; -.
DR SMR; Q90629; -.
DR STRING; 9031.ENSGALP00000029849; -.
DR PaxDb; Q90629; -.
DR GeneID; 396344; -.
DR KEGG; gga:396344; -.
DR CTD; 5645; -.
DR VEuPathDB; HostDB:geneid_396344; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_13_1_1; -.
DR OrthoDB; 1314811at2759; -.
DR PRO; PR:Q90629; -.
DR Proteomes; UP000000539; Unplaced.
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..16
FT /evidence="ECO:0000250"
FT PROPEP 17..25
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028223"
FT CHAIN 26..248
FT /note="Trypsin II-P29"
FT /id="PRO_0000028224"
FT DOMAIN 26..246
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 32..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 134..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 141..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 173..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 198..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 248 AA; 26622 MW; E5E16B07622B588E CRC64;
MKFLFLILSC LGAAVAFPGG ADDDKIVGGY TCPEHSVPYQ VSLNSGYHFC GGSLINSQWV
LSAAHCYKSR IQVRLGEYNI DVQEDSEVVR SSSVIIRHPK YSSITLNNDI MLIKLASAVE
YSADIQPIAL PSSCAKAGTE CLISGWGNTL SNGYNYPELL QCLNAPILSD QECQEAYPGD
ITSNMICVGF LEGGKDSCQG DSGGPVVCNG ELQGIVSWGI GCALKGYPGV YTKVCNYVDW
IQETIAAY
