UniProt: PEPE

Database: UniProt
Entry: PEPE_CHICK

LinkDB:  PEPE_CHICK 
Original site:  PEPE_CHICK

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Ontology (3)   
   GO (3)   
Gene (8)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (6)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (24)   

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ID   PEPE_CHICK              Reviewed;         383 AA.
AC   P16476;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Embryonic pepsinogen;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3131317; DOI=10.1093/oxfordjournals.jbchem.a122263;
RA   Hayashi K., Agata K., Mochii M., Yasugi S., Eguchi G., Mizuno T.;
RT   "Molecular cloning and the nucleotide sequence of cDNA for embryonic
RT   chicken pepsinogen: phylogenetic relationship with prochymosin.";
RL   J. Biochem. 103:290-296(1988).
CC   -!- DEVELOPMENTAL STAGE: Specifically secreted during the embryonic period
CC       in the chicken proventriculus (glandular stomach).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; D00215; BAA00153.1; -; mRNA.
DR   PIR; A41443; A41443.
DR   RefSeq; NP_990385.1; NM_205054.2.
DR   AlphaFoldDB; P16476; -.
DR   SMR; P16476; -.
DR   STRING; 9031.ENSGALP00000000593; -.
DR   MEROPS; A01.028; -.
DR   PaxDb; 9031-ENSGALP00000000593; -.
DR   Ensembl; ENSGALT00010066315.1; ENSGALP00010040581.1; ENSGALG00010027352.1.
DR   Ensembl; ENSGALT00015051807; ENSGALP00015030115; ENSGALG00015021259.
DR   GeneID; 395926; -.
DR   KEGG; gga:395926; -.
DR   CTD; 643834; -.
DR   VEuPathDB; HostDB:geneid_395926; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000162710; -.
DR   InParanoid; P16476; -.
DR   OMA; LAYTEQN; -.
DR   OrthoDB; 1120702at2759; -.
DR   PhylomeDB; P16476; -.
DR   PRO; PR:P16476; -.
DR   Proteomes; UP000000539; Chromosome 26.
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:SF13; CHYMOSIN; 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; Digestion; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..383
FT                   /note="Embryonic pepsinogen"
FT                   /id="PRO_0000026000"
FT   DOMAIN          76..380
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        107..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        267..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        310..344
FT                   /evidence="ECO:0000250"
FT   VARIANT         51
FT                   /note="T -> S"
SQ   SEQUENCE   383 AA;  41719 MW;  1642796871611F54 CRC64;
     MRSLALLCAV LALSDGITRL PLERGKKLRE ILREKGLLHH FLQHHRYDIG TKFPHAFPDV
     LTVVTEPLLN TLDMEYYGTI SIGTPPQDFT VVFDTGSSNL WVPSVSCTSP ACQSHQMFNP
     SQSSTYKSTG QNLSIHYGTG DMEGTVGCDT VTVASLMDTN QLFGLSTSEP GQFFVYVKFD
     GILGLGYPSL AADGITPVFD NMVNESLLEQ NLFSVYLSRE PMGSMVVFGG IDESYFTGSI
     NWIPVSYQGY WQISMDSIIV NKQEIACSSG CQAIIDTGTS LVAGPASDIN DIQSAVGANQ
     NTYGEYSVNC SHILAMPDVV FVIGGIQYPV PALAYTEQNG QGTCMSSFQN SSADLWILGD
     VFIRVYYSIF DRANNRVGLA KAI
//

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