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Database: UniProt/TrEMBL
Entry: Q547S4_BOVIN
LinkDB: Q547S4_BOVIN
Original site: Q547S4_BOVIN 
ID   Q547S4_BOVIN            Unreviewed;       247 AA.
AC   Q547S4;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   31-JAN-2018, entry version 74.
DE   SubName: Full=Pancreatic anionic trypsinogen {ECO:0000313|EMBL:AAM18909.1};
GN   Name=TRYP8 {ECO:0000313|EMBL:AAM18909.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAM18909.1};
RN   [1] {ECO:0000313|EMBL:AAM18909.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12072270; DOI=10.1016/S0165-2427(02)00093-4;
RA   Conrad M.L., Pettman R., Whitehead J., McKinnel L., Davis S.K.,
RA   Koop B.F.;
RT   "Genomic sequencing of the bovine T cell receptor beta locus.";
RL   Vet. Immunol. Immunopathol. 87:439-441(2002).
RN   [2] {ECO:0000313|EMBL:AAM18909.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Conrad M.L., Pettman R., Whitehead J., McKinnel L., Davis S.K.,
RA   Koop B.F.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
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DR   EMBL; AF453325; AAM18909.1; -; Genomic_DNA.
DR   RefSeq; NP_777115.1; NM_174690.1.
DR   UniGene; Bt.1978; -.
DR   ProteinModelPortal; Q547S4; -.
DR   PRIDE; Q547S4; -.
DR   GeneID; 282603; -.
DR   KEGG; bta:282603; -.
DR   CTD; 5645; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOVERGEN; HBG013304; -.
DR   KO; K01312; -.
DR   PMAP-CutDB; Q547S4; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00037407};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     15       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        16    247       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012045374.
FT   DOMAIN       24    244       Peptidase S1. {ECO:0000259|PROSITE:
FT                                PS50240}.
SQ   SEQUENCE   247 AA;  26295 MW;  C819D007ECB520C8 CRC64;
     MHPLLILAFV GAAVAFPSDD DDKIVGGYTC AENSVPYQVS LNAGYHFCGG SLINDQWVVS
     AAHCYQYHIQ VRLGEYNIDV LEGGEQFIDA SKIIRHPKYS SWTLDNDILL IKLSTPAVIN
     ARVSTLALPS ACASGSTECL ISGWGNTLSS GVNYPDLLQC LEAPLLSHAD CEASYPGEIT
     NNMICAGFLE GGKDSCQGDS GGPVACNGQL QGIVSWGYGC AQKGKPGVYT KVCNYVDWIQ
     ETIAANS
//
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