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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
 
 
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