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Database: UniProt
Entry: A0A0D9R1V6_CHLSB
LinkDB: A0A0D9R1V6_CHLSB
Original site: A0A0D9R1V6_CHLSB 
ID   A0A0D9R1V6_CHLSB        Unreviewed;       386 AA.
AC   A0A0D9R1V6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-NOV-2023, entry version 38.
DE   RecName: Full=pepsin A {ECO:0000256|ARBA:ARBA00011924};
DE            EC=3.4.23.1 {ECO:0000256|ARBA:ARBA00011924};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000002595.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000002595.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000002595.1}
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; AQIB01079283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01079284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01079285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01079286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01079287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01079288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01079289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01079290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01079291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9R1V6; -.
DR   STRING; 60711.ENSCSAP00000002595; -.
DR   Ensembl; ENSCSAT00000004340.1; ENSCSAP00000002595.1; ENSCSAG00000006333.1.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000155036; -.
DR   OMA; ENYMDME; -.
DR   Proteomes; UP000029965; Chromosome 1.
DR   Bgee; ENSCSAG00000006333; Expressed in blood.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:UP000029965};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
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_5013108033"
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;  41576 MW;  1813158F5A985427 CRC64;
     MKWLLLLGLV ALSECIIHKV PLVRKKSLRR NLSEHGLLKD FLKKHNRNPA RKYFPQAEAP
     THEQPLENYL DMEYFGTIGI GTPAQDFTVI FDTGSSNLWV PSVYCSSLAC TNHNRFNPQD
     SSTYQSTSGT LSITYGTGSM TGILGYDTVK VGGISDTNQI FGLSETEPGS FLYYAPFDGI
     LGLAYPSISS SGATPVFDNI WNQGLVSQDL FSVYLSADDQ SGSVVIFGGI DSSYYTGSLN
     WVPVSVEGYW HISVDSITMN GEAIACAEGC QAIVDTGTSL LTGPTSPIAN IQSDIGASEN
     SDGEMVVSCS AVSSLPDIVF TINGVQYPLP PSAYILQSQG SCTSGFEGMD VPTESGELWI
     LGDVFIRQYF TVFDRANNQV GLAPVA
//
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