ORYC_ORYSJ
ID ORYC_ORYSJ Reviewed; 362 AA.
AC P25778; Q67UU2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Oryzain gamma chain;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN OrderedLocusNames=Os09g0442300, LOC_Os09g27030; ORFNames=P0046G12.22;
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].
RC STRAIN=cv. Nipponbare; TISSUE=Seed;
RX PubMed=1885617; DOI=10.1016/s0021-9258(18)55387-4;
RA Watanabe H., Abe K., Emori Y., Hosoyama H., Arai S.;
RT "Molecular cloning and gibberellin-induced expression of multiple cysteine
RT proteinases of rice seeds (oryzains).";
RL J. Biol. Chem. 266:16897-16902(1991).
RN [2]
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 [3]
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).
CC -!- TISSUE SPECIFICITY: Expressed only in seeds.
CC -!- INDUCTION: By gibberellic acid (GA).
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; D90408; BAA14404.1; -; mRNA.
DR EMBL; AP005419; BAD38077.1; -; Genomic_DNA.
DR EMBL; AP014965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JU0390; KHRZOG.
DR RefSeq; XP_015611626.1; XM_015756140.1.
DR AlphaFoldDB; P25778; -.
DR SMR; P25778; -.
DR IntAct; P25778; 1.
DR STRING; 4530.OS09T0442300-01; -.
DR MEROPS; C01.041; -.
DR PaxDb; P25778; -.
DR GeneID; 4347180; -.
DR KEGG; osa:4347180; -.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_1_1; -.
DR InParanoid; P25778; -.
DR OrthoDB; 1275401at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; P25778; OS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Thiol protease; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..144
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026436"
FT CHAIN 145..362
FT /note="Oryzain gamma chain"
FT /id="PRO_0000026437"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT ACT_SITE 309
FT /evidence="ECO:0000250"
FT ACT_SITE 329
FT /evidence="ECO:0000250"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 166..209
FT /evidence="ECO:0000250"
FT DISULFID 200..242
FT /evidence="ECO:0000250"
FT DISULFID 300..350
FT /evidence="ECO:0000250"
FT CONFLICT 12
FT /note="A -> V (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="D -> G (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="A -> P (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="T -> P (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> R (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="K -> P (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="V -> A (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> R (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="V -> A (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="G -> V (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="K -> T (in Ref. 1; BAA14404)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 39114 MW; 9D16188CAE844C29 CRC64;
MAHRRIILLL AAAAVAATSA VAAASSGFDD SNPIRSVTDH AASALESTVI AALGRTRDAL
RFARFAVRHG KRYGDAAEVQ RRFRIFSESL ELVRSTNRRG LPYRLGINRF ADMSWEEFQA
SRLGAAQNCS ATLAGNHRMR DAAALPETKD WREDGIVSPV KDQGHCGSCW TFSTTGSLEA
AYTQATGKPV SLSEQQLVDC ATAYNNFGCS GGLPSQAFEY IKYNGGLDTE EAYPYTGVNG
ICHYKPENVG VKVLDSVNIT LGAEDELKNA VGLVRPVSVA FQVINGFRMY KSGVYTSDHC
GTSPMDVNHA VLAVGYGVEN GVPYWLIKNS WGADWGDNGY FKMEMGKNMC GIATCASYPI
VA
