PEPC_RAT
ID PEPC_RAT Reviewed; 392 AA.
AC P04073;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Gastricsin;
DE EC=3.4.23.3;
DE AltName: Full=Pepsinogen C;
DE Flags: Precursor;
GN Name=Pgc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=3780741; DOI=10.1111/j.1432-1033.1986.tb10117.x;
RA Ichihara Y., Sogawa K., Morohashi K., Fujii-Kuriyama Y., Takahashi K.;
RT "Nucleotide sequence of a nearly full-length cDNA coding for pepsinogen of
RT rat gastric mucosa.";
RL Eur. J. Biochem. 161:7-12(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar;
RX PubMed=2722863; DOI=10.1016/s0021-9258(18)81784-7;
RA Ishihara T., Ichihara Y., Hayano T., Katsura I., Sogawa K.,
RA Fujii-Kuriyama Y., Takahashi K.;
RT "Primary structure and transcriptional regulation of rat pepsinogen C
RT gene.";
RL J. Biol. Chem. 264:10193-10199(1989).
RN [3]
RP PROTEIN SEQUENCE OF 17-112.
RC STRAIN=Wistar;
RX PubMed=6743670; DOI=10.1016/0167-4838(84)90269-3;
RA Arai K.M., Muto N., Tani S., Akahane K.;
RT "The N-terminal sequence of rat pepsinogen.";
RL Biochim. Biophys. Acta 788:256-261(1984).
CC -!- FUNCTION: Hydrolyzes a variety of proteins.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=More restricted specificity than pepsin A, but shows
CC preferential cleavage at Tyr-|-Xaa bonds. High activity on
CC hemoglobin.; EC=3.4.23.3;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; X04644; CAA28305.1; -; mRNA.
DR EMBL; M25993; AAA41827.1; -; Genomic_DNA.
DR EMBL; M25985; AAA41827.1; JOINED; Genomic_DNA.
DR EMBL; M25986; AAA41827.1; JOINED; Genomic_DNA.
DR EMBL; M25987; AAA41827.1; JOINED; Genomic_DNA.
DR EMBL; M25988; AAA41827.1; JOINED; Genomic_DNA.
DR EMBL; M25989; AAA41827.1; JOINED; Genomic_DNA.
DR EMBL; M25990; AAA41827.1; JOINED; Genomic_DNA.
DR EMBL; M25991; AAA41827.1; JOINED; Genomic_DNA.
DR EMBL; M25992; AAA41827.1; JOINED; Genomic_DNA.
DR PIR; A33510; A24608.
DR RefSeq; NP_579818.1; NM_133284.2.
DR AlphaFoldDB; P04073; -.
DR SMR; P04073; -.
DR STRING; 10116.ENSRNOP00000019650; -.
DR BindingDB; P04073; -.
DR ChEMBL; CHEMBL2152; -.
DR MEROPS; A01.003; -.
DR iPTMnet; P04073; -.
DR PhosphoSitePlus; P04073; -.
DR PaxDb; P04073; -.
DR Ensembl; ENSRNOT00000019650; ENSRNOP00000019650; ENSRNOG00000014492.
DR GeneID; 24864; -.
DR KEGG; rno:24864; -.
DR UCSC; RGD:3943; rat.
DR CTD; 5225; -.
DR RGD; 3943; Pgc.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000160626; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; P04073; -.
DR OMA; LSNNGYC; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; P04073; -.
DR TreeFam; TF314990; -.
DR PRO; PR:P04073; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000014492; Expressed in stomach and 16 other tissues.
DR Genevisible; P04073; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; ISO:RGD.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0002803; P:positive regulation of antibacterial peptide production; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033735; Gastricsin.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR13683; PTHR13683; 1.
DR PANTHER; PTHR13683:SF292; PTHR13683:SF292; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Digestion; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Protease; Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:3780741,
FT ECO:0000269|PubMed:6743670"
FT PROPEP 17..62
FT /note="Activation peptide"
FT /id="PRO_0000026069"
FT CHAIN 63..392
FT /note="Gastricsin"
FT /id="PRO_0000026070"
FT DOMAIN 76..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 94
FT ACT_SITE 280
FT DISULFID 107..112
FT /evidence="ECO:0000250"
FT DISULFID 270..275
FT /evidence="ECO:0000250"
FT DISULFID 314..347
FT /evidence="ECO:0000250"
FT CONFLICT 31
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="S -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="S -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 42833 MW; 092A5EAF2783EDD1 CRC64;
MKWMVVALLC LPLLEASLLR VPLRKMKSIR ETMKEQGVLK DFLKTHKYDP GQKYHFGNFG
DYSVLYEPMA YMDASYFGEI SIGTPPQNFL VLFDTGSSNL WVSSVYCQSE ACTTHARFNP
SKSSTYYTEG QTFSLQYGTG SLTGFFGYDT LTVQSIQVPN QEFGLSENEP GTNFVYAQFD
GIMGLAYPGL SSGGATTALQ GMLGEGALSQ PLFGVYLGSQ QGSNGGQIVF GGVDKNLYTG
EITWVPVTQE LYWQITIDDF LIGDQASGWC SSQGCQGIVD TGTSLLVMPA QYLSELLQTI
GAQEGEYGEY FVSCDSVSSL PTLSFVLNGV QFPLSPSSYI IQEDNFCMVG LESISLTSES
GQPLWILGDV FLRSYYAIFD MGNNKVGLAT SV
