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Database: UniProt/SWISS-PROT
Entry: TRY3_CHICK
LinkDB: TRY3_CHICK
Original site: 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   16-JAN-2019, entry version 113.
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;
OC   Phasianidae; 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
RT   family.";
RL   Biochem. J. 307:471-479(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.;
CC         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
CC       lower levels are found in the liver, spleen and thymus.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; U15157; AAA79914.1; -; mRNA.
DR   PIR; S55066; S55066.
DR   RefSeq; NP_990715.1; NM_205384.1.
DR   UniGene; Gga.10164; -.
DR   ProteinModelPortal; Q90629; -.
DR   SMR; Q90629; -.
DR   STRING; 9031.ENSGALP00000029849; -.
DR   PaxDb; Q90629; -.
DR   PRIDE; Q90629; -.
DR   GeneID; 396344; -.
DR   KEGG; gga:396344; -.
DR   CTD; 5645; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251820; -.
DR   HOVERGEN; HBG013304; -.
DR   KO; K01312; -.
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   InterPro; IPR009003; Peptidase_S1_PA.
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; Complete proteome; Digestion; Disulfide bond; Hydrolase;
KW   Metal-binding; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     16       {ECO:0000250}.
FT   PROPEP       17     25       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000028223.
FT   CHAIN        26    248       Trypsin II-P29.
FT                                /FTId=PRO_0000028224.
FT   DOMAIN       26    246       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     65     65       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    109    109       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    202    202       Charge relay system. {ECO:0000250}.
FT   METAL        77     77       Calcium. {ECO:0000250}.
FT   METAL        79     79       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        82     82       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        87     87       Calcium. {ECO:0000250}.
FT   SITE        196    196       Required for specificity. {ECO:0000250}.
FT   DISULFID     32    162       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID     50     66       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    134    235       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    141    208       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    173    187       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    198    222       {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
//
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