Sequence of ASPR_HORVU
EC Number:3.4.23.40
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-/-Asp- and -Asp-/-Asp- bonds in 2S albumin from plant seeds
Other sequences found for EC No. 3.4.23.40
General information:
Sequence
0 MGTRGLALAL LAAVLLLQTV LPAASEAEGL VRIALKKRPI DRNSRVATGL SGGEEQPLLS
60 GANPLRSEEE GDIVALKNYM NAQYFGEIGV GTPPQKFTVI FDTGSSNLWV PSAKCYFSIA
120 CYLHSRYKAG ASSTYKKNGK PAAIQYGTGS IAGYFSEDSV TVGDLVVKDQ EFIEATKEPG
180 ITFLVAKFDG ILGLGFKEIS VGKAVPVWYK MIEQGLVSDP VFSFWLNRHV DEGEGGEIIF
240 GGMDPKHYVG EHTYVPVTQK GYWQFDMGDV LVGGKSTGFC AGGCAAIADS GTSLLAGPTA
300 IITEINEKIG AAGVVSQECK TIVSQYGQQI LDLLLAETQP KKICSQVGLC TFDGTRGVSA
360 GIRSVVDDEP VKSNGLRADP MCSACEMAVV WMQNQLAQNK TQDLILDYVN QLCNRLPSPM
420 GESAVDCGSL GSMPDIEFTI GGKKFALKPE EYILKVGEGA AAQCISGFTA MDIPPPRGPL
480 WILGDVFMGP YHTVFDYGKL RIGFAKAA
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1031305
Runeberg-Roos P.,Toermaekangas K.,Oestman A.
Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D.
Eur. J. Biochem.
202
1021-1027
1991
1031306
Toermaekangas K.,Runeberg-Roos P.,Oestman A.,Tilgmann C.,Sarkkinen P.,Kervinen J.,Mikola L.,Kalkkinen N.
Aspartic proteinase from barley seeds is related to animal cathepsin D.
Adv. Exp. Med. Biol.
306
355-359
1991
1031307
Paris N.,Stanley C.M.,Jones R.L.,Rogers J.C.
Plant cells contain two functionally distinct vacuolar compartments.
Cell
85
563-572
1996
1031308
Kervinen J.,Tobin G.J.,Costa J.,Waugh D.S.,Wlodawer A.,Zdanov A.
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.
EMBO J.
18
3947-3955
1999
