DDN1_BOVIN
ID DDN1_BOVIN Reviewed; 251 AA.
AC P80219; Q9GLN2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Duodenase-1;
DE EC=3.4.21.-;
DE AltName: Full=Duodenase I;
DE AltName: Full=Duodenum serine protease;
DE Flags: Precursor;
GN Name=BDMD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Smirnova E.V., Evtodienko A.Y., Zamolodchikova T.S.;
RT "cDNA cloning of duodenase, a serine protease from bovine duodenal
RT mucosa.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 20-246.
RC TISSUE=Duodenum;
RX PubMed=7867649; DOI=10.1111/j.1432-1033.1995.tb20213.x;
RA Zamolodchikova T.S., Vorotyntseva T.I., Nazimov I.V., Grishina G.A.;
RT "Duodenase, a new serine protease of unusual specificity from bovine
RT duodenal mucosa. Primary structure of the enzyme.";
RL Eur. J. Biochem. 227:873-879(1995).
RN [3]
RP PROTEIN SEQUENCE OF 20-43 AND 192-203.
RX PubMed=1425193;
RA Antonov V.K., Vorotyntseva T.I., Zamolodchikova T.S.;
RT "Duodenase -- a new serine proteinase with unusual specificity.";
RL Dokl. Akad. Nauk SSSR 324:1318-1322(1992).
RN [4]
RP PROTEIN SEQUENCE OF 20-43, AND FUNCTION.
RC TISSUE=Duodenum;
RX PubMed=7867648; DOI=10.1111/j.1432-1033.1995.tb20212.x;
RA Zamolodchikova T.S., Vorotyntseva T.I., Antonov V.K.;
RT "Duodenase, a new serine protease of unusual specificity from bovine
RT duodenal mucosa. Purification and properties.";
RL Eur. J. Biochem. 227:866-872(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-246.
RX PubMed=10944388;
RX DOI=10.1002/1097-0134(20001001)41:1<8::aid-prot30>3.0.co;2-2;
RA Pletnev V.Z., Zamolodchikova T.S., Pangborn W.A., Duax W.L.;
RT "Crystal structure of bovine duodenase, a serine protease, with dual
RT trypsin and chymotrypsin-like specificities.";
RL Proteins 41:8-16(2000).
CC -!- FUNCTION: Protease which has both trypsin-like and chymotrypsin-like
CC activities. Shows a preferential cleavage after Lys, Arg, Tyr, Phe, and
CC Leu residues. {ECO:0000269|PubMed:7867648}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0.;
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF198965; AAG28537.1; -; mRNA.
DR PIR; S69370; S69370.
DR PIR; S69371; S69371.
DR RefSeq; NP_776721.1; NM_174296.2.
DR PDB; 1EUF; X-ray; 2.40 A; A=20-246.
DR PDBsum; 1EUF; -.
DR AlphaFoldDB; P80219; -.
DR SMR; P80219; -.
DR STRING; 9913.ENSBTAP00000050126; -.
DR MEROPS; S01.142; -.
DR PaxDb; P80219; -.
DR PeptideAtlas; P80219; -.
DR GeneID; 281731; -.
DR KEGG; bta:281731; -.
DR CTD; 3002; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P80219; -.
DR OrthoDB; 1076876at2759; -.
DR BRENDA; 3.4.21.B3; 908.
DR SABIO-RK; P80219; -.
DR EvolutionaryTrace; P80219; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..19
FT /evidence="ECO:0000269|PubMed:1425193,
FT ECO:0000269|PubMed:7867648, ECO:0000269|PubMed:7867649"
FT /id="PRO_0000244396"
FT CHAIN 20..251
FT /note="Duodenase-1"
FT /id="PRO_0000088659"
FT DOMAIN 20..242
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 63
FT /note="Charge relay system"
FT ACT_SITE 107
FT /note="Charge relay system"
FT ACT_SITE 201
FT /note="Charge relay system"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 48..64
FT DISULFID 141..207
FT DISULFID 172..186
FT CONFLICT 68
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="N -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="K -> R (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="R -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="S -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 239..245
FT /note="HSTMRRY -> KRVMYLF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 34..54
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1EUF"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:1EUF"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:1EUF"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1EUF"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:1EUF"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1EUF"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1EUF"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:1EUF"
SQ SEQUENCE 251 AA; 27556 MW; 2392608CF8BF52B8 CRC64;
MVLLLLLVAL LSPTGEAGKI IGGHEAKPHS RPYMAFLLFK TSGKSHICGG FLVREDFVLT
AAHCLGSSIN VTLGAHNIME RERTQQVIPV RRPIPHPDYN DETLANDIML LKLTRKADIT
DKVSPINLPR SLAEVKPGMM CSVAGWGRLG VNMPSTDNLQ EVDLEVQSEE KCIARFKNYI
PFTQICAGDP SKRKNSFSGD SGGPLVCNGV AQGIVSYGRN DGTTPDVYTR ISSFLSWIHS
TMRRYKRQGS V
