ID TRY1_CHICK Reviewed; 248 AA.
AC Q90627;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-APR-2013, entry version 85.
DE RecName: Full=Trypsin I-P1;
DE EC=3.4.21.4;
DE Flags: Precursor;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=7733885;
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: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
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 -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR EMBL; U15155; AAA79912.1; -; mRNA.
DR IPI; IPI00573152; -.
DR PIR; S55067; S55067.
DR RefSeq; NP_990716.1; NM_205385.1.
DR UniGene; Gga.4442; -.
DR UniGene; Gga.51254; -.
DR ProteinModelPortal; Q90627; -.
DR SMR; Q90627; 26-248.
DR STRING; 9031.ENSGALP00000016613; -.
DR PaxDb; Q90627; -.
DR GeneID; 396345; -.
DR KEGG; gga:396345; -.
DR CTD; 5646; -.
DR eggNOG; COG5640; -.
DR HOGENOM; HOG000251820; -.
DR HOVERGEN; HBG013304; -.
DR InParanoid; Q90627; -.
DR KO; K01312; -.
DR OrthoDB; EOG4SJ5FV; -.
DR NextBio; 20816393; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Pept_Ser_Cys; 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 15 By similarity.
FT PROPEP 16 25 Activation peptide (By similarity).
FT /FTId=PRO_0000028219.
FT CHAIN 26 248 Trypsin I-P1.
FT /FTId=PRO_0000028220.
FT DOMAIN 26 246 Peptidase S1.
FT ACT_SITE 65 65 Charge relay system (By similarity).
FT ACT_SITE 109 109 Charge relay system (By similarity).
FT ACT_SITE 202 202 Charge relay system (By similarity).
FT METAL 77 77 Calcium (By similarity).
FT METAL 79 79 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 87 87 Calcium (By similarity).
FT SITE 196 196 Required for specificity (By similarity).
FT DISULFID 32 162 By similarity.
FT DISULFID 50 66 By similarity.
FT DISULFID 134 235 By similarity.
FT DISULFID 141 208 By similarity.
FT DISULFID 173 187 By similarity.
FT DISULFID 198 222 By similarity.
SQ SEQUENCE 248 AA; 26070 MW; C4CF589912B23D98 CRC64;
MKFLVLVAFV GVTVAFPISD EDDDKIVGGY SCARSAAPYQ VSLNSGYHFC GGSLISSQWV
LSAAHCYKSS IQVKLGEYNL AAQDGSEQTI SSSKVIRHSG YNANTLNNDI MLIKLSKAAT
LNSYVNTVPL PTSCVTAGTT CLISGWGNTL SSGSLYPDVL QCLNAPVLSS SQCSSAYPGR
ITSNMICIGY LNGGKDSCQG DSGGPVVCNG QLQGIVSWGI GCAQKGYPGV YTKVCNYVSW
IKTTMSSN
//
