ID   PEPA3_RABIT             Reviewed;         387 AA.
AC   P27822;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Pepsin-3;
DE            EC=3.4.23.1;
DE   AltName: Full=Pepsin III;
DE   AltName: Full=Pepsin A;
DE   Flags: Precursor;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Japanese white; TISSUE=Gastric mucosa;
RX   MEDLINE=91009127; PubMed=2129536;
RA   Kageyama T., Tanabe K., Koiwai O.;
RT   "Structure and development of rabbit pepsinogens. Stage-specific
RT   zymogens, nucleotide sequences of cDNAs, molecular evolution, and gene
RT   expression during development.";
RL   J. Biol. Chem. 265:17031-17038(1990).
CC   -!- FUNCTION: Shows particularly broad specificity; although bonds
CC       involving phenylalanine and leucine are preferred, many others are
CC       also cleaved to some extent.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: hydrophobic, preferably
CC       aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2,
CC       4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16,
CC       16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-
CC       Tyr-26 bonds in the B chain of insulin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DEVELOPMENTAL STAGE: Pepsinogens in group I, II, and III where the
CC       predominant zymogens at late postnatal stage.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
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DR   EMBL; M59237; AAA85370.1; -; mRNA.
DR   PIR; E38302; E38302.
DR   HSSP; P00791; 4PEP.
DR   SMR; P27822; 19-387.
DR   MEROPS; A01.001; -.
DR   Ensembl; ENSOCUG00000011717; Oryctolagus cuniculus.
DR   HOVERGEN; P27822; -.
DR   BRENDA; 3.4.23.1; 255.
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:InterPro.
DR   InterPro; IPR001461; Peptidase_A1.
DR   InterPro; IPR001969; Peptidase_aspartic_AS.
DR   InterPro; IPR009007; Peptidase_aspartic_catalytic.
DR   InterPro; IPR012848; Propep_A1.
DR   Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 2.
DR   PANTHER; PTHR13683; Peptidase_A1; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Digestion; Disulfide bond; Hydrolase;
KW   Phosphoprotein; Protease; Secreted; Signal; Zymogen.
FT   SIGNAL        1     15
FT   PROPEP       16     59       Activation peptide.
FT                                /FTId=PRO_0000026034.
FT   CHAIN        60    387       Pepsin-3.
FT                                /FTId=PRO_0000026035.
FT   ACT_SITE     93     93       By similarity.
FT   ACT_SITE    276    276       By similarity.
FT   MOD_RES     129    129       Phosphoserine (By similarity).
FT   DISULFID    106    111       By similarity.
FT   DISULFID    267    271       By similarity.
FT   DISULFID    310    343       By similarity.
SQ   SEQUENCE   387 AA;  41969 MW;  15A59AC81F36F9EF CRC64;
     MKWLLLLGLL ALSECIIHKV PLVRKKSLRK NLIEKGLLKD YLKTHTPNLA TKYLPKAAFD
     SVPTETLENY LDTEYFGTIG IGTPAQDFTV IFDTGSSNLW VPSVYCSSAA CSVHNQFNPE
     DSSTFQATSE SLSITYGTGS MTGFLGYDTV KVGNIEDTNQ IFGLSESEPG SFLYYAPFDG
     ILGLAYPSIS SSDATPVFDN MWNEGLVSED LFSVYLSSDD ESGSVVMFGG IDSSYYTGSL
     NWVPVSYEGY WQITLDSITM DGETIACADS CQAIVDTGTS LLAGPTSAIS NIQSYIGASE
     NSDGEMIVSC SSMYSLPNIV FTINGVQYPV PASAYILEED DACISGFEGM NLDTYTGELW
     ILGDVFIRQY FTVFDRANNQ LGLAAAA
//