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
//