ID   PEPB_MONDO              Reviewed;         391 AA.
AC   Q689Z7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Pepsin B;
DE            EC=3.4.23.2 {ECO:0000250|UniProtKB:Q8SQ41};
DE   Flags: Precursor;
GN   Name=PGB {ECO:0000305};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Narita Y., Oda S., Kageyama T.;
RT   "The monophyly of rodentia inferred from biochemical analyses of gastric
RT   aspartic proteinases and molecular phylogenetic analyses of pepsinogen-C
RT   cDNA sequences.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes various peptides including beta-endorphin, insulin
CC       B chain, dynorphin A, and neurokinin A, with high specificity for the
CC       cleavage of the Phe-Xaa bonds. {ECO:0000250|UniProtKB:Q8SQ41}.
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:0000250|UniProtKB:Q8SQ41};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; AB188678; BAD36918.1; -; mRNA.
DR   RefSeq; NP_001028152.1; NM_001032980.1.
DR   AlphaFoldDB; Q689Z7; -.
DR   SMR; Q689Z7; -.
DR   STRING; 13616.ENSMODP00000001655; -.
DR   MEROPS; A01.002; -.
DR   GeneID; 554184; -.
DR   KEGG; mdo:554184; -.
DR   CTD; 5225; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; Q689Z7; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000002280; 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   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Digestion; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..60
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026061"
FT   CHAIN           61..391
FT                   /note="Pepsin B"
FT                   /id="PRO_0000026062"
FT   DOMAIN          75..388
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        106..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..274
FT                   /evidence="ECO:0000250"
FT   DISULFID        313..346
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  43281 MW;  5E13064A27469C2D CRC64;
     MKCLILALIC LQLSEGLVVR QILHKGKSIR ERMEENGVLE DFLRYNKKAD PAAKFLFNKD
     AVAYEPITNY LDSFYFGEIS IGTPPQNFLV LFDTGSSNLW VPSTYCQSQA CSNHNRFSPS
     QSSTFTNGGQ TYTLSYGSGS LTVVLGYDTV TVQNIVVSNQ EFGLSESEPT SPFYYSDFDG
     ILGMAYPAMA VGNSPTVMQG MLQQGQLSEP IFSFYFSRQP THQYGGELIL GGVDPQLYSG
     QITWTPVTQE VYWQIGIEEF AIGNQATGWC SQGCQAIVDT GTFLLAVPQQ YMSAFLQATG
     AQQAQNGDFM VNCNYIQDMP TITFVINGSQ FPLPPSAYVF NNNGYCRLGI EATYLPSPNG
     QPLWILGDVF LKEYYSVYDM ANNRVGFAYS A