ORYB_ORYSJ
ID ORYB_ORYSJ Reviewed; 466 AA.
AC P25777; B7F253; Q0J962; Q259Q5; Q7XR57; Q8S4X9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Oryzain beta chain;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN OrderedLocusNames=Os04g0670200, LOC_Os04g57440;
GN ORFNames=H0818H01.14, OSJNBa0043A12.28;
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], TISSUE SPECIFICITY, AND INDUCTION BY
RP GIBBERELLIN.
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
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 344-465.
RA Pillai A., Seiji Y.;
RT "Molecular cloning of salt responsive gene in rice, OSSRIII.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP STRUCTURE BY NMR OF 383-417, AND DISULFIDE BONDS.
RX PubMed=11298924; DOI=10.1111/j.1399-3011.2001.00828.x;
RA Tolkatchev D., Xu P., Ni F.;
RT "A peptide derived from the C-terminal part of a plant cysteine protease
RT folds into a stack of two beta-hairpins, a scaffold present in the emerging
RT family of granulin-like growth factors.";
RL J. Pept. Res. 57:227-233(2001).
CC -!- FUNCTION: Probable thiol protease. {ECO:0000250|UniProtKB:P43297}.
CC -!- TISSUE SPECIFICITY: Expressed only in seeds.
CC {ECO:0000269|PubMed:1885617}.
CC -!- INDUCTION: By gibberellic acid (GA). {ECO:0000269|PubMed:1885617}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA14403.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D90407; BAA14403.1; ALT_FRAME; mRNA.
DR EMBL; AL606619; CAE02823.1; -; Genomic_DNA.
DR EMBL; AL732346; CAJ86092.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF16125.2; -; Genomic_DNA.
DR EMBL; AP014960; BAS91553.1; -; Genomic_DNA.
DR EMBL; AK109371; BAG98700.1; -; mRNA.
DR EMBL; AF366556; AAM00365.1; -; mRNA.
DR PIR; JU0389; KHRZOB.
DR RefSeq; XP_015636103.1; XM_015780617.1.
DR PDB; 1FWO; NMR; -; A=383-417.
DR PDBsum; 1FWO; -.
DR AlphaFoldDB; P25777; -.
DR SMR; P25777; -.
DR STRING; 4530.OS04T0670200-02; -.
DR MEROPS; C01.029; -.
DR PaxDb; P25777; -.
DR PRIDE; P25777; -.
DR EnsemblPlants; Os04t0670200-01; Os04t0670200-01; Os04g0670200.
DR GeneID; 4337351; -.
DR Gramene; Os04t0670200-01; Os04t0670200-01; Os04g0670200.
DR KEGG; osa:4337351; -.
DR eggNOG; KOG1543; Eukaryota.
DR eggNOG; KOG4296; Eukaryota.
DR HOGENOM; CLU_012184_0_2_1; -.
DR InParanoid; P25777; -.
DR OrthoDB; 1275401at2759; -.
DR EvolutionaryTrace; P25777; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; P25777; baseline and differential.
DR Genevisible; P25777; 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 Gene3D; 2.10.25.160; -; 1.
DR InterPro; IPR000118; Granulin.
DR InterPro; IPR037277; Granulin_sf.
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; PF00396; Granulin; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00277; GRAN; 1.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..140
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026434"
FT CHAIN 141..361
FT /note="Oryzain beta chain"
FT /id="PRO_0000026435"
FT PROPEP 362..466
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000046021"
FT REGION 358..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 162..205
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 196..238
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 296..347
FT /evidence="ECO:0000250|UniProtKB:P84346"
FT DISULFID 386..398
FT /evidence="ECO:0000269|PubMed:11298924,
FT ECO:0007744|PDB:1FWO"
FT DISULFID 392..413
FT /evidence="ECO:0000269|PubMed:11298924,
FT ECO:0007744|PDB:1FWO"
FT CONFLICT 95
FT /note="R -> G (in Ref. 1; BAA14403)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="D -> A (in Ref. 1; BAA14403)"
FT /evidence="ECO:0000305"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:1FWO"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:1FWO"
SQ SEQUENCE 466 AA; 49799 MW; 830531BD39144598 CRC64;
MAARAAAAAF LLLLIVGAAT AAPDMSIISY NAEHGARGLE EGPTEAEARA AYDLWLAENG
GGSPNALGGE HERRFLVFWD NLKFVDAHNA RADERGGFRL GMNRFADLTN EEFRATFLGA
KVAERSRAAG ERYRHDGVEE LPESVDWREK GAVAPVKNQG QCGSCWAFSA VSTVESINQL
VTGEMITLSE QELVECSTNG QNSGCNGGLM DDAFDFIIKN GGIDTEDDYP YKAVDGKCDI
NRENAKVVSI DGFEDVPQND EKSLQKAVAH QPVSVAIEAG GREFQLYHSG VFSGRCGTSL
DHGVVAVGYG TDNGKDYWIV RNSWGPKWGE SGYVRMERNI NVTTGKCGIA MMASYPTKSG
ANPPKPSPTP PTPPTPPPPS APDHVCDDNF SCPAGSTCCC AFGFRNLCLV WGCCPVEGAT
CCKDHASCCP PDYPVCNTRA GTCSASKNSP LSVKALKRTL AKLNTA
