ID   PEPC_SUNMU              Reviewed;         389 AA.
AC   P81498; Q9GMY5;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   22-FEB-2023, entry version 100.
DE   RecName: Full=Gastricsin;
DE            EC=3.4.23.3;
DE   AltName: Full=Pepsinogen C-1;
DE   Flags: Precursor;
GN   Name=PGC; Synonyms=PGNC;
OS   Suncus murinus (Asian house shrew) (Musk shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Crocidurinae; Suncus.
OX   NCBI_TaxID=9378;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11603935; DOI=10.1006/mpev.2001.0996;
RA   Narita Y., Oda S., Takenaka O., Kageyama T.;
RT   "Phylogenetic position of Eulipotyphla inferred from the cDNA sequences of
RT   pepsinogens A and C.";
RL   Mol. Phylogenet. Evol. 21:32-42(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 17-80.
RC   TISSUE=Gastric mucosa;
RX   PubMed=9354369; DOI=10.1093/oxfordjournals.jbchem.a021687;
RA   Narita Y., Oda S., Moriyama A., Takenaka O., Kageyama T.;
RT   "Pepsinogens and pepsins from house musk shrew, Suncus murinus:
RT   purification, characterization, determination of the amino-acid sequences
RT   of the activation segments, and analysis of proteolytic specificities.";
RL   J. Biochem. 121:1010-1017(1997).
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; AB047247; BAB11753.1; -; mRNA.
DR   PIR; PC4361; PC4361.
DR   AlphaFoldDB; P81498; -.
DR   SMR; P81498; -.
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; 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; 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:SF72; GASTRICSIN; 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   1: Evidence at protein level;
KW   Aspartyl protease; Digestion; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Protease; Secreted; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:9354369"
FT   PROPEP          17..59
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026075"
FT   CHAIN           60..389
FT                   /note="Gastricsin"
FT                   /id="PRO_0000026076"
FT   DOMAIN          73..386
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        104..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        268..272
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..344
FT                   /evidence="ECO:0000250"
FT   CONFLICT        68
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  42667 MW;  F253B63A72CAA728 CRC64;
     MKWMVVALVC LQLLEAKVTK VTLKKFKSIR ENLREQGLLE DFLKTNHYDP AQKYHFGDFS
     VAYEPMAYMD ASYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQSQACT GHARFNPNQS
     STYSTNGQTF SLQYGSGSLT GFFGYDTMTV QNIKVPHQEF GLSQNEPGTN FIYAQFDGIM
     GMAYPSLAMG GATTALQGML QEGALTSPVF SFYLSNQQGS QNGGAVIFGG VDNSLYTGQI
     FWAPVTQELY WQIGVEEFLI GGQATGWCQQ GCQAIVDTGT SLLTVPQQFM SALQQATGAQ
     QDQYGQLAVN CNSIQSLPTL TFIINGVQFP LPPSAYVLNT NGYCFLGVEP TYLPSQNGQP
     LWILGDVFLR SYYSVYDMGN NRVGFATAA
//