ASPR_HORVU
ID ASPR_HORVU Reviewed; 508 AA.
AC P42210;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phytepsin;
DE EC=3.4.23.40;
DE AltName: Full=Aspartic proteinase;
DE Contains:
DE RecName: Full=Phytepsin 32 kDa subunit;
DE Contains:
DE RecName: Full=Phytepsin 29 kDa subunit;
DE Contains:
DE RecName: Full=Phytepsin 16 kDa subunit;
DE Contains:
DE RecName: Full=Phytepsin 11 kDa subunit;
DE Flags: Precursor;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Kustaa; TISSUE=Embryo;
RX PubMed=1722454; DOI=10.1111/j.1432-1033.1991.tb16465.x;
RA Runeberg-Roos P., Toermaekangas K., Oestman A.;
RT "Primary structure of a barley-grain aspartic proteinase. A plant aspartic
RT proteinase resembling mammalian cathepsin D.";
RL Eur. J. Biochem. 202:1021-1027(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Kustaa; TISSUE=Embryo;
RX PubMed=1812727; DOI=10.1007/978-1-4684-6012-4_43;
RA Toermaekangas K., Runeberg-Roos P., Oestman A., Tilgmann C., Sarkkinen P.,
RA Kervinen J., Mikola L., Kalkkinen N.;
RT "Aspartic proteinase from barley seeds is related to animal cathepsin D.";
RL Adv. Exp. Med. Biol. 306:355-359(1991).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=8653791; DOI=10.1016/s0092-8674(00)81256-8;
RA Paris N., Stanley C.M., Jones R.L., Rogers J.C.;
RT "Plant cells contain two functionally distinct vacuolar compartments.";
RL Cell 85:563-572(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 31-508, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=10406799; DOI=10.1093/emboj/18.14.3947;
RA Kervinen J., Tobin G.J., Costa J., Waugh D.S., Wlodawer A., Zdanov A.;
RT "Crystal structure of plant aspartic proteinase prophytepsin: inactivation
RT and vacuolar targeting.";
RL EMBO J. 18:3947-3955(1999).
CC -!- FUNCTION: Involved in the breakdown of propeptides of storage proteins
CC in protein-storage vacuoles. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1
CC and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S
CC albumin from plant seeds.; EC=3.4.23.40;
CC -!- SUBUNIT: Heterodimer of two subunits (29 kDa and 11 kDa) processed from
CC the precursor molecule. A large enzyme (32 kDa and 16 kDa) is an
CC intermediate precursor form. {ECO:0000269|PubMed:10406799}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:8653791}.
CC -!- TISSUE SPECIFICITY: Embryo and leaf.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X56136; CAA39602.1; -; mRNA.
DR PIR; S19697; S19697.
DR PDB; 1QDM; X-ray; 2.30 A; A/B/C=31-508.
DR PDBsum; 1QDM; -.
DR AlphaFoldDB; P42210; -.
DR SMR; P42210; -.
DR MEROPS; A01.020; -.
DR PRIDE; P42210; -.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0073640.1; HORVU.MOREX.r2.1HG0073640.1; HORVU.MOREX.r2.1HG0073640.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1.
DR Gramene; HORVU.MOREX.r2.1HG0073640.1; HORVU.MOREX.r2.1HG0073640.1; HORVU.MOREX.r2.1HG0073640.
DR Gramene; HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1.mrna1; HORVU.MOREX.r2.1HG0073640.1.
DR KEGG; ag:CAA39602; -.
DR OMA; GVECANL; -.
DR EvolutionaryTrace; P42210; -.
DR ExpressionAtlas; P42210; baseline and differential.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06098; phytepsin; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033869; Phytepsin.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SMART; SM00741; SapB; 1.
DR SUPFAM; SSF47862; SSF47862; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Protease; Signal; Vacuole; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..66
FT /note="Activation peptide"
FT /id="PRO_0000025903"
FT CHAIN 67..377
FT /note="Phytepsin 32 kDa subunit"
FT /id="PRO_0000025904"
FT CHAIN 67..?
FT /note="Phytepsin 29 kDa subunit"
FT /id="PRO_0000025905"
FT CHAIN 378..508
FT /note="Phytepsin 16 kDa subunit"
FT /id="PRO_0000025906"
FT CHAIN 422..508
FT /note="Phytepsin 11 kDa subunit"
FT /id="PRO_0000025907"
FT DOMAIN 84..505
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DOMAIN 314..419
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT ACT_SITE 102
FT ACT_SITE 289
FT SITE 377..378
FT /note="Cleavage"
FT SITE 421..422
FT /note="Cleavage"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 115..121
FT /evidence="ECO:0000269|PubMed:10406799,
FT ECO:0007744|PDB:1QDM"
FT DISULFID 280..284
FT /evidence="ECO:0000269|PubMed:10406799,
FT ECO:0007744|PDB:1QDM"
FT DISULFID 319..413
FT /evidence="ECO:0000269|PubMed:10406799,
FT ECO:0007744|PDB:1QDM"
FT DISULFID 344..385
FT /evidence="ECO:0000269|PubMed:10406799,
FT ECO:0007744|PDB:1QDM"
FT DISULFID 350..382
FT /evidence="ECO:0000269|PubMed:10406799,
FT ECO:0007744|PDB:1QDM"
FT DISULFID 427..464
FT /evidence="ECO:0000269|PubMed:10406799,
FT ECO:0007744|PDB:1QDM"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1QDM"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 149..162
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 165..177
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:1QDM"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 247..259
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1QDM"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 379..397
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 402..412
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:1QDM"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:1QDM"
FT TURN 497..500
FT /evidence="ECO:0007829|PDB:1QDM"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:1QDM"
SQ SEQUENCE 508 AA; 54226 MW; 87F2C9F93369B962 CRC64;
MGTRGLALAL LAAVLLLQTV LPAASEAEGL VRIALKKRPI DRNSRVATGL SGGEEQPLLS
GANPLRSEEE GDIVALKNYM NAQYFGEIGV GTPPQKFTVI FDTGSSNLWV PSAKCYFSIA
CYLHSRYKAG ASSTYKKNGK PAAIQYGTGS IAGYFSEDSV TVGDLVVKDQ EFIEATKEPG
ITFLVAKFDG ILGLGFKEIS VGKAVPVWYK MIEQGLVSDP VFSFWLNRHV DEGEGGEIIF
GGMDPKHYVG EHTYVPVTQK GYWQFDMGDV LVGGKSTGFC AGGCAAIADS GTSLLAGPTA
IITEINEKIG AAGVVSQECK TIVSQYGQQI LDLLLAETQP KKICSQVGLC TFDGTRGVSA
GIRSVVDDEP VKSNGLRADP MCSACEMAVV WMQNQLAQNK TQDLILDYVN QLCNRLPSPM
GESAVDCGSL GSMPDIEFTI GGKKFALKPE EYILKVGEGA AAQCISGFTA MDIPPPRGPL
WILGDVFMGP YHTVFDYGKL RIGFAKAA
