ID   PEPAF_RABIT             Reviewed;         388 AA.
AC   P27823;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Pepsin F;
DE            EC=3.4.23.1;
DE   Flags: Precursor;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Japanese white; TISSUE=Gastric mucosa;
RX   PubMed=2129536; DOI=10.1016/s0021-9258(17)44864-2;
RA   Kageyama T., Tanabe K., Koiwai O.;
RT   "Structure and development of rabbit pepsinogens. Stage-specific zymogens,
RT   nucleotide sequences of cDNAs, molecular evolution, and gene expression
RT   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 also
CC       cleaved to some extent.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: hydrophobic, preferably aromatic,
CC         residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-
CC         5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-
CC         17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the
CC         B chain of insulin.; EC=3.4.23.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10094};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DEVELOPMENTAL STAGE: Early postnatal.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; M59238; AAA31440.1; -; mRNA.
DR   PIR; A38302; A38302.
DR   RefSeq; NP_001076165.1; NM_001082696.1.
DR   AlphaFoldDB; P27823; -.
DR   SMR; P27823; -.
DR   STRING; 9986.ENSOCUP00000006601; -.
DR   MEROPS; A01.051; -.
DR   PRIDE; P27823; -.
DR   Ensembl; ENSOCUT00000007632; ENSOCUP00000006601; ENSOCUG00000007632.
DR   GeneID; 100009429; -.
DR   KEGG; ocu:100009429; -.
DR   CTD; 5222; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000153747; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   Bgee; ENSOCUG00000007632; Expressed in ovary and 1 other tissue.
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; 2.
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..15
FT   PROPEP          16..58
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026036"
FT   CHAIN           59..388
FT                   /note="Pepsin F"
FT                   /id="PRO_0000026037"
FT   DOMAIN          74..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        105..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..270
FT                   /evidence="ECO:0000250"
FT   DISULFID        309..343
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  42786 MW;  24792BE393594B3A CRC64;
     MKWLGLLGLV ALSECLVTIP LMKVKSMREN LRENDILLDY LEKHPYRPTY KLLSGQQDPD
     VSFEPLRNYL DLAYIGIISI GTPPQEFKVV LDTGSADLWV PSIYCSSPAC GKHNTFNPLL
     SSTFLVSGRP INIVYGSGRM SGFLAYDTVQ IAGLVDVAQA FGLSLQEPGK FMEYAVFDGI
     LGLSYPSLSF EGITPVFDNL WAQGLISQNL FAFYLSSKEE RGSMLMLGGV DPSYYSGDLH
     WVPVSRPLYW QLAVDRISMN GEAIGCDSGC QGIVDTGTSL LIGPRDPVLN IQKIINAQHS
     HGGEYIIDCD TISTLPDIIF TIDGVDYPVP ASAYIRKSSV HGCYSNFDES AAHESEPYEV
     WVLGDVFLRL YFTVFDRANN RIGLAPAV