CAC3_BOVIN
ID CAC3_BOVIN Reviewed; 253 AA.
AC P05805;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Proproteinase E;
DE AltName: Full=Procarboxypeptidase A complex component III;
DE AltName: Full=Procarboxypeptidase A-S6 subunit III;
DE Short=PROCPA-S6 III;
DE Flags: Precursor;
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 PROTEIN SEQUENCE OF 1-25.
RX PubMed=2269366; DOI=10.1016/0014-5793(90)80804-r;
RA Pascual R., Vendrell J., Aviles F.X., Bonicel J., Wicker C., Puigserver A.;
RT "Autolysis of proproteinase E in bovine procarboxypeptidase A ternary
RT complex gives rise to subunit III.";
RL FEBS Lett. 277:37-41(1990).
RN [2]
RP PROTEIN SEQUENCE OF 14-253, AND DISULFIDE BONDS.
RX PubMed=3519215; DOI=10.1111/j.1432-1033.1986.tb09642.x;
RA Venot N., Sciaky M., Puigserver A., Desnuelle P., Laurent G.;
RT "Amino acid sequence and disulfide bridges of subunit III, a defective
RT endopeptidase present in the bovine pancreatic 6 S procarboxypeptidase A
RT complex.";
RL Eur. J. Biochem. 157:91-99(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=8168476; DOI=10.1002/j.1460-2075.1994.tb06444.x;
RA Pignol D., Gaboriaud C., Michon T., Kerfelec B., Chapus C.,
RA Fontecilla-Camps J.-C.;
RT "Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly
RT structured truncated zymogen E.";
RL EMBO J. 13:1763-1771(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH CTRC AND PPE.
RX PubMed=7556081; DOI=10.1002/j.1460-2075.1995.tb00117.x;
RA Gomis-Rueth F.-X., Gomez M., Bode W., Huber R., Aviles F.X.;
RT "The three-dimensional structure of the native ternary complex of bovine
RT pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen
RT C.";
RL EMBO J. 14:4387-4394(1995).
CC -!- FUNCTION: May protect procarboxypeptidase A against denaturation in the
CC acidic environment of the ruminant duodenum.
CC -!- SUBUNIT: Monomer. The zymogen is secreted as a ternary complex composed
CC of procarboxypeptidase A, chymotrypsinogen C and proproteinase E.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Pancreas.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Defective elastase-like serine protease which does not seem to
CC have protease activity. {ECO:0000305}.
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DR PIR; A25065; CPBOA3.
DR PDB; 1FON; X-ray; 1.70 A; A/B=14-253.
DR PDB; 1PYT; X-ray; 2.35 A; C=1-253.
DR PDBsum; 1FON; -.
DR PDBsum; 1PYT; -.
DR AlphaFoldDB; P05805; -.
DR SMR; P05805; -.
DR STRING; 9913.ENSBTAP00000017401; -.
DR PaxDb; P05805; -.
DR PRIDE; P05805; -.
DR eggNOG; KOG3627; Eukaryota.
DR EvolutionaryTrace; P05805; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Digestion; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Serine protease homolog.
FT PROPEP 1..11
FT /note="Activation peptide"
FT /id="PRO_0000028446"
FT CHAIN 12..253
FT /note="Proproteinase E"
FT /id="PRO_0000028447"
FT DOMAIN 12..251
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 41..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:3519215"
FT DISULFID 100..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:3519215"
FT DISULFID 140..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:3519215"
FT DISULFID 171..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:3519215"
FT DISULFID 196..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:3519215"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 23..33
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1FON"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1FON"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1FON"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1FON"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:1FON"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1FON"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1FON"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1FON"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:1FON"
SQ SEQUENCE 253 AA; 27338 MW; 24663724D8AE409C CRC64;
FSQPFSRPSS RVVNGEDAVP YSWSWQVSLQ YEKDGAFHHT CGGSLIAPDW VVTAGHCIST
SRTYQVVLGE YDRSVLEGSE QVIPINAGDL FVHPLWNSNC VACGNDIALV KLSRSAQLGD
KVQLANLPPA GDILPNEAPC YISGWGRLYT GGPLPDKLQQ ALLPVVDYEH CSQWDWWGIT
VKKTMVCAGG DTRSGCNGDS GGPLNCPAAD GSWQVHGVTS FVSAFGCNTI KKPTVFTRVS
AFIDWIDETI ASN
