GenomeNet

Database: UniProt
Entry: F1N373_BOVIN
LinkDB: F1N373_BOVIN
Original site: F1N373_BOVIN 
ID   F1N373_BOVIN            Unreviewed;       386 AA.
AC   F1N373;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=Pepsin A {ECO:0000256|ARBA:ARBA00039700};
DE            EC=3.4.23.1 {ECO:0000256|ARBA:ARBA00011924};
GN   Name=PGA5 {ECO:0000313|Ensembl:ENSBTAP00000019640.5};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000019640.5, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000019640.5, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000019640.5,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000019640.5}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000019640.5};
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   RefSeq; NP_001001600.2; NM_001001600.2.
DR   AlphaFoldDB; F1N373; -.
DR   SMR; F1N373; -.
DR   MEROPS; A01.001; -.
DR   Ensembl; ENSBTAT00000019640.6; ENSBTAP00000019640.5; ENSBTAG00000014761.6.
DR   GeneID; 414350; -.
DR   KEGG; bta:414350; -.
DR   CTD; 5222; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014761; -.
DR   GeneTree; ENSGT00940000155036; -.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   InParanoid; F1N373; -.
DR   OMA; ENYMDME; -.
DR   OrthoDB; 1120702at2759; -.
DR   TreeFam; TF314990; -.
DR   Reactome; R-BTA-5683826; Surfactant metabolism.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000014761; Expressed in abomasum and 63 other cell types or tissues.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:UP000009136};
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_5013084799"
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;  41557 MW;  5114491D5F282E05 CRC64;
     MKWLLLLALV ALSECSVVKI PLVKKKSLRQ NLIENGKLKE FMRTHKYNLG SKYIREAATL
     VSEQPLQNYL DTEYFGTIGI GTPAQDFTVI FDTGSSNLWV PSIYCSSEAC TNHNRFNPQD
     SSTYEATSET LSITYGTGSM TGILGYDTVQ VGGISDTNQI FGLSETEPGS FLYYAPFDGI
     LGLAYPSISS SGATPVFDNI WDQGLVSQDL FSVYLSSNEE SGSVVIFGDI DSSYYSGSLN
     WVPVSVEGYW QITVDSITMN GESIACSDGC QAIVDTGTSL LAGPTTAISN IQSYIGASED
     SSGEVVISCS SIDSLPDIVF TINGVQYPVP PSAYILQSNG ICSSGFEGMD ISTSSGDLWI
     LGDVFIRQYF TVFDRGNNQI GLAPVA
//
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