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Database: UniProt
Entry: W5N1A5_LEPOC
LinkDB: W5N1A5_LEPOC
Original site: W5N1A5_LEPOC 
ID   W5N1A5_LEPOC            Unreviewed;       389 AA.
AC   W5N1A5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=pepsin A {ECO:0000256|ARBA:ARBA00011924};
DE            EC=3.4.23.1 {ECO:0000256|ARBA:ARBA00011924};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000014414.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000014414.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Shows particularly broad specificity; although bonds
CC       involving phenylalanine and leucine are preferred, many others are also
CC       cleaved to some extent. {ECO:0000256|ARBA:ARBA00002318}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; AHAT01016714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5N1A5; -.
DR   STRING; 7918.ENSLOCP00000014414; -.
DR   Ensembl; ENSLOCT00000014443.1; ENSLOCP00000014414.1; ENSLOCG00000011725.1.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000155036; -.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   InParanoid; W5N1A5; -.
DR   OMA; NMVQQGH; -.
DR   Proteomes; UP000018468; Linkage group LG3.
DR   Bgee; ENSLOCG00000011725; Expressed in larva.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 6.10.140.60; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF22; PEPSIN A-3-RELATED; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..389
FT                   /note="pepsin A"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004867026"
FT   DOMAIN          72..386
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        103..108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        266..270
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   389 AA;  42528 MW;  444F9E2EC905D7B8 CRC64;
     MKWAIVLLGL VALSECMTKV PLLKRKSMRK ALMEQGKLEE FLQKYPYDLA SKYSRYATTS
     NLPMHNYMDI EYIATISIGT PPQSFIVLPD TGSANLWVPS IYCSSLACSN HHKYNPSLSS
     TYRALNTPVS IAYGTGSMTG FLAYDTVTVG GIIDSNQEFG LSQTEPGNFL YYSPFDGIMG
     LSYPYISASG ATPVFDNMMQ QGLVSQDLFS IYLTNARNGA SGSVVTFGGY DSSYFTGQIN
     WVPVTYMGYW QIAIENVMVN GQVVACAQGC QGIVDSGTSL IAGPPSEIST IQQYIGATQN
     SYQQYSINCQ NMGSMPNVVF TINGLQYTLT PSAYVRQDSQ LYGACTSGFQ SMALPSAQGD
     LWILGDVFIR EYYAIFDRGN NRVGLAQAV
//
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