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ASPRX_ORYSJ
ID   ASPRX_ORYSJ             Reviewed;         496 AA.
AC   P42211; Q0DKX3; Q75L35; Q9XIV3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Aspartic proteinase;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=RAP; OrderedLocusNames=Os05g0137400, LOC_Os05g04630;
GN   ORFNames=OJ1127_B08.13;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hashimoto H., Nishi R., Uchimiya H., Kato A.;
RT   "Nucleotide sequence of a cDNA encoding aspartic proteinase in rice.";
RL   Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 405-496.
RA   Tao Y., Li L.;
RT   "Chilling sensitive rice partial mRNA for aspartic protease.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the breakdown of propeptides of storage proteins
CC       in protein-storage vacuoles. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; D12777; BAA02242.1; -; mRNA.
DR   EMBL; AC093490; AAS98423.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF16500.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS92166.1; -; Genomic_DNA.
DR   EMBL; AK065206; BAG89416.1; -; mRNA.
DR   EMBL; AB028888; BAA78908.1; -; mRNA.
DR   PIR; JS0732; JS0732.
DR   AlphaFoldDB; P42211; -.
DR   SMR; P42211; -.
DR   STRING; 4530.OS05T0137400-01; -.
DR   PaxDb; P42211; -.
DR   PRIDE; P42211; -.
DR   EnsemblPlants; Os05t0137400-01; Os05t0137400-01; Os05g0137400.
DR   Gramene; Os05t0137400-01; Os05t0137400-01; Os05g0137400.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_1_1; -.
DR   InParanoid; P42211; -.
DR   OMA; DKSHYTG; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   Genevisible; P42211; OS.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; 2.
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   2: Evidence at transcript level;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Signal; Vacuole; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..59
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025910"
FT   CHAIN           60..496
FT                   /note="Aspartic proteinase"
FT                   /id="PRO_0000025911"
FT   DOMAIN          77..493
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   DOMAIN          307..407
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   ACT_SITE        95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        108..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        273..277
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        312..401
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        337..373
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        343..370
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        415..452
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   CONFLICT        158
FT                   /note="L -> Q (in Ref. 1; BAA02242)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        431
FT                   /note="K -> R (in Ref. 7; BAA78908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        492
FT                   /note="F -> V (in Ref. 7; BAA78908)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   496 AA;  54090 MW;  82F5AE431A833FE0 CRC64;
     MAKRHLLLVT TCLWALSCAL LLHASSDGFL RVNLNKKRLD KEDLTAAKLA QQGNRLLKTG
     SSDSDPVPLV DYLNTQYYGV IGLGSPPQNF TVIFDTGSSN LWVPSAKCYF SIACYLHSRY
     NSKKSSSYKA DGETCKITYG SGAISGFFSK DNVLVGDLVV KNQKFIEATR ETSVTFIIGK
     FDGILGLGYP EISVGKAPPI WQSMQEQELL ADDVFSFWLN RDPDASSGGE LVFGGMDPKH
     YKGDHTYVPV SRKGYWQFNM GDLLIDGHST GFCAKGCAAI VDSGTSLLAG PTAIVAQVNH
     AIGAEGIIST ECKEVVSEYG EMILNLLIAQ TDPQKVCSQV GLCMFDGKRS VSNGIESVVD
     KENLGSDAMC SVCEMAVVWI ENQLRENKTK ELILNYANQL CERLPSPNGE STVSCHQISK
     MPNLAFTIAN KTFILTPEQY IVKLEQGGQT VCISGFMAFD IPPPRGPLWI LGDVFMGAYH
     TVFDFGKDRI GFAKSA
 
 
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