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Database: UniProt
Entry: L5KQ85_PTEAL
LinkDB: L5KQ85_PTEAL
Original site: L5KQ85_PTEAL 
ID   L5KQ85_PTEAL            Unreviewed;       386 AA.
AC   L5KQ85;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Pepsin A {ECO:0000256|ARBA:ARBA00039700};
DE            EC=3.4.23.1 {ECO:0000256|ARBA:ARBA00011924};
GN   ORFNames=PAL_GLEAN10011520 {ECO:0000313|EMBL:ELK13482.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13482.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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; KB030625; ELK13482.1; -; Genomic_DNA.
DR   RefSeq; XP_006911295.1; XM_006911233.1.
DR   AlphaFoldDB; L5KQ85; -.
DR   STRING; 9402.L5KQ85; -.
DR   MEROPS; A01.001; -.
DR   GeneID; 102897755; -.
DR   KEGG; pale:102897755; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; L5KQ85; -.
DR   OrthoDB; 1120702at2759; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
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   CDD; cd05478; pepsin_A; 1.
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; IPR034162; Pepsin_A.
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; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Digestion {ECO:0000256|ARBA:ARBA00022757};
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:UP000010552};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..386
FT                   /note="Pepsin A"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012113247"
FT   DOMAIN          74..383
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        105..110
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        266..270
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        309..342
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   386 AA;  41477 MW;  97B047AA8E507BB4 CRC64;
     MKWLLLLGLV ALSECLIYKV PLVKKKSLRR NLIEHGLLAD YLKTHKLNPA SKYLKEAASF
     TDTETLENYL DMEYFGTIGI GTPAQEFTVI FDTGSSNLWV PSVYCSSLAC YNHNVFNPED
     SSTFEATSET VSITYGTGSM TGILGYDTVQ VGGISDTNQI FGLSETEPGS FLYYAPFDGI
     LGLAYPSISA SGATPVFDNL WDQGLVSQDL FSVYLSSDDD SGSVVIFGGI DSSYYSGSLN
     WVPLSSETYW QITVDSVILD GEAIACSATC QAIVDTGTSL LAGPTTAISS IQKYIGASEN
     SDGDMVVSCS AASELPNIIF TINGVQYPLP SSAYILESDD VCISGFQGMD LPTSSGDLWI
     LGDVFIRQYF TVFDRANNQV GLASAA
//
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