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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}.
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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
 
 
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