PEPB_PIG
ID PEPB_PIG Reviewed; 67 AA.
AC Q10735;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Pepsin B;
DE EC=3.4.23.2 {ECO:0000269|PubMed:7574716};
DE AltName: Full=Parapepsin I;
DE Flags: Precursor; Fragment;
GN Name=PGB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RC TISSUE=Gastric mucosa;
RX PubMed=7574716; DOI=10.1006/abbi.1995.1483;
RA Nielsen P.K., Foltmann B.;
RT "Purification and characterization of porcine pepsinogen B and pepsin B.";
RL Arch. Biochem. Biophys. 322:417-422(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Degradation of gelatin, little activity on hemoglobin.
CC Specificity on B chain of insulin more restricted than that of pepsin
CC A. Does not cleave 1-Phe-|-Val-2, 4-Gln-|-His-5 or 23-Gly-|-Phe-24.;
CC EC=3.4.23.2; Evidence={ECO:0000269|PubMed:7574716};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S68032; S68032.
DR AlphaFoldDB; Q10735; -.
DR STRING; 9823.ENSSSCP00000007245; -.
DR PaxDb; Q10735; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; Q10735; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Digestion; Direct protein sequencing; Hydrolase;
KW Protease; Reference proteome; Secreted; Zymogen.
FT PROPEP 1..43
FT /note="Activation peptide"
FT /id="PRO_0000026050"
FT CHAIN 44..>67
FT /note="Pepsin B"
FT /id="PRO_0000026051"
FT NON_TER 67
SQ SEQUENCE 67 AA; 7799 MW; DC0F8859801562C6 CRC64;
MERIILRKGK SIREAMEEQG VLEKFLKNRP KIDPAAKYHF NNDAVAYEPF TNYLDSFYFG
EISIGTP