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8.A.32.1.4
Pro-gastricsin, PGC of 388 aas.  It shows a more restricted substrate specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds (Hassan et al. 2010).  It is a member of the aspartic protease family, including pepsin and chymosin (Richter et al. 1998). It is involved in production of pro-antimicrobial substances in seminal plasma. The crystal structure shows that it is quite similar to that of porcine pepsinogen. The tertiary structure of PGC is bilobal with a large active-site cleft between the lobes. Two aspartyl residues in the center of the cleft, namely Asp32 and Asp215, function as catalytic residues (Hassan et al. 2010).

Accession Number:P20142
Protein Name:Gastricsin
Length:388
Molecular Weight:42426.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Secreted1
Substrate

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FASTA formatted sequence
1:	MKWMVVVLVC LQLLEAAVVK VPLKKFKSIR ETMKEKGLLG EFLRTHKYDP AWKYRFGDLS 
61:	VTYEPMAYMD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQSQACT SHSRFNPSES 
121:	STYSTNGQTF SLQYGSGSLT GFFGYDTLTV QSIQVPNQEF GLSENEPGTN FVYAQFDGIM 
181:	GLAYPALSVD EATTAMQGMV QEGALTSPVF SVYLSNQQGS SGGAVVFGGV DSSLYTGQIY 
241:	WAPVTQELYW QIGIEEFLIG GQASGWCSEG CQAIVDTGTS LLTVPQQYMS ALLQATGAQE 
301:	DEYGQFLVNC NSIQNLPSLT FIINGVEFPL PPSSYILSNN GYCTVGVEPT YLSSQNGQPL 
361:	WILGDVFLRS YYSVYDLGNN RVGFATAA