PEPC_MACFU
ID PEPC_MACFU Reviewed; 377 AA.
AC P03955;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Gastricsin;
DE EC=3.4.23.3;
DE AltName: Full=Pepsinogen C;
DE Flags: Precursor; Fragment;
GN Name=PGC;
OS Macaca fuscata fuscata (Japanese macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9543;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gastric mucosa;
RX PubMed=1935977; DOI=10.1111/j.1432-1033.1991.tb16364.x;
RA Kageyama T., Tanabe K., Koiwai O.;
RT "Development-dependent expression of isozymogens of monkey pepsinogens and
RT structural differences between them.";
RL Eur. J. Biochem. 202:205-215(1991).
RN [2]
RP PROTEIN SEQUENCE OF 6-377.
RX PubMed=3514597; DOI=10.1016/s0021-9258(17)38515-0;
RA Kageyama T., Takahashi K.;
RT "The complete amino acid sequence of monkey progastricsin.";
RL J. Biol. Chem. 261:4406-4419(1986).
RN [3]
RP PROTEIN SEQUENCE OF 6-65.
RX PubMed=3928607; DOI=10.1093/oxfordjournals.jbchem.a135169;
RA Kageyama T., Takahashi K.;
RT "Monkey pepsinogens and pepsins. VII. Analysis of the activation process
RT and determination of the NH2-terminal 60-residue sequence of Japanese
RT monkey progastricsin, and molecular evolution of pepsinogens.";
RL J. Biochem. 97:1235-1246(1985).
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 -!- PTM: Each pepsinogen is converted to corresponding pepsin at pH 2.0 in
CC part as a result of the release of a 47 AA activation segment and in
CC part as a result of stepwise proteolytic cleavage via an intermediate
CC form(s).
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; X59754; CAA42426.1; -; mRNA.
DR PIR; S19683; PEMQCJ.
DR AlphaFoldDB; P03955; -.
DR SMR; P03955; -.
DR MEROPS; A01.003; -.
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 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; Secreted; Signal; Zymogen.
FT SIGNAL <1..5
FT /evidence="ECO:0000269|PubMed:3514597,
FT ECO:0000269|PubMed:3928607"
FT PROPEP 6..31
FT /note="Activation peptide"
FT /id="PRO_0000026058"
FT PROPEP 32..48
FT /note="Activation peptide"
FT /id="PRO_0000026059"
FT CHAIN 49..377
FT /note="Gastricsin"
FT /id="PRO_0000026060"
FT DOMAIN 62..374
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 80
FT ACT_SITE 265
FT DISULFID 93..98
FT DISULFID 256..260
FT DISULFID 299..332
FT CONFLICT 331
FT /note="Y -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="L -> LVY (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 377 AA; 41148 MW; 2CFB8F8BF26D77CE CRC64;
QLLEAAVVKV PLKKFKSIRE TMKEKGLLGE FLRTHKYDPA WKYHFGDLSV SYEPMAYMDA
AYFGEISIGT PPQNFLVLFD TGSSNLWVPS VYCQSQACTS HSRFNPSESS TYSTNGQTFS
LQYGSGSLTG FFGYDTLTVQ SIQVPNQEFG LSENEPGTNF VYAQFDGIMG LAYPTLSVDG
ATTAMQGMVQ EGALTSPIFS VYLSDQQGSS GGAVVFGGVD SSLYTGQIYW APVTQELYWQ
IGIEEFLIGG QASGWCSEGC QAIVDTGTSL LTVPQQYMSA LLQATGAQED EYGQFLVNCN
SIQNLPTLTF IINGVEFPLP PSSYILNNNG YCTVGVEPTY LSAQNSQPLW ILGDVFLRSY
YSVYDLSNNR VGFATAA