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
//