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Database: UniProt
Entry: B9A837_PONAB
LinkDB: B9A837_PONAB
Original site: B9A837_PONAB 
ID   B9A837_PONAB            Unreviewed;       388 AA.
AC   B9A837; H2ND88;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=pepsin A {ECO:0000256|ARBA:ARBA00011924};
DE            EC=3.4.23.1 {ECO:0000256|ARBA:ARBA00011924};
GN   Name=pg {ECO:0000313|EMBL:BAH20538.1};
GN   Synonyms=LOC100454826 {ECO:0000313|Ensembl:ENSPPYP00000003685.2}, PG
GN   {ECO:0000313|Ensembl:ENSPPYP00000025639.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|EMBL:BAH20538.1};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000003685.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH20538.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Gastric mucosa {ECO:0000313|EMBL:BAH20538.1};
RX   PubMed=20349055; DOI=10.1007/s00239-010-9320-8;
RA   Narita Y., Oda S., Takenaka O., Kageyama T.;
RT   "Lineage-specific duplication and loss of pepsinogen genes in hominoid
RT   evolution.";
RL   J. Mol. Evol. 70:313-324(2010).
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000003685.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; AB458301; BAH20538.1; -; mRNA.
DR   RefSeq; NP_001138942.1; NM_001145470.1.
DR   MEROPS; A01.001; -.
DR   Ensembl; ENSPPYT00000003817.2; ENSPPYP00000003685.2; ENSPPYG00000003195.2.
DR   Ensembl; ENSPPYT00000036180.1; ENSPPYP00000025639.1; ENSPPYG00000030830.1.
DR   GeneID; 100271705; -.
DR   KEGG; pon:100271705; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000155036; -.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   OMA; INNINAW; -.
DR   OrthoDB; 1120702at2759; -.
DR   TreeFam; TF314990; -.
DR   Proteomes; UP000001595; Unplaced.
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   2: Evidence at transcript level;
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, ECO:0000313|EMBL:BAH20538.1};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..388
FT                   /note="pepsin A"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041198426"
FT   DOMAIN          76..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        107..112
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        268..272
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   388 AA;  41828 MW;  F4560558A5CE27A8 CRC64;
     MKWLLLLGLV ALSECIMYKV PLIRKKSLRR TLSERGLLKD FLKKHNLNPA SKYFPQGKAP
     TLLHEQPLEN YLDVEYFGTI GIGTPAQDFT VVFDTGSSNL WVPSVYCYSL ACMDHNLFNP
     QDSSTYKSTS ETVSITYGTG SMTGILGYDT VKVGGISDTN QIFGLSESEP GSFLFFAPFD
     GILGLAYPSI SSSGATPVFD NIWNQGLVSQ DLFSVYLSAD DKSGSVVIFG GIDSSYYTGS
     LNWVPVTVEG YWQITVDSIT MNGKTIACAE GCQAIVDTGT SLLTGPTSPI ANIQSDIGAS
     ENSDGDMVVS CSAISSLPDI VFTINGVQYP LPPSAYILKS EGSCISGFQG MNVPTESGEL
     WILGDVFIRQ YFTVFDRANN QVGLAPVA
//
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