IAAS_ORYSJ
ID IAAS_ORYSJ Reviewed; 200 AA.
AC P29421; Q0JBL0; Q7XKJ3; Q8GRN7; Q8W3L5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Alpha-amylase/subtilisin inhibitor;
DE AltName: Full=RASI;
DE Flags: Precursor;
GN Name=RASI; OrderedLocusNames=Os04g0526600, LOC_Os04g44470;
GN ORFNames=OSJNBa0038O10.14;
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 [GENOMIC DNA].
RA Ohtsubo K., Nakamura S., Murakami Y., Hashimoto J., Kurita A., Kawasaki S.;
RT "DNA sequence of RASI and its effect on bacterial growth.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare;
RA Yamagata H., Yamasaki T.;
RT "Molecular cloning and characterization of a cDNA for alpha-
RT amylase/subtilisin inhibitor (RASI) from rice and expression of the
RT recombinant protein.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP PROTEIN SEQUENCE OF 23-198.
RC TISSUE=Seed;
RX PubMed=1511747; DOI=10.1016/0014-5793(92)80741-x;
RA Ohtsubo K., Richardson M.;
RT "The amino acid sequence of a 20 kDa bifunctional subtilisin/alpha-amylase
RT inhibitor from bran of rice (Oryza sativa L.) seeds.";
RL FEBS Lett. 309:68-72(1992).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND DISULFIDE BONDS.
RA Peng W.Y., Lin Y.H., Huang Y.C., Guan H.H., Hsieh Y.C., Liu M.Y., Chang T.,
RA Chen C.J.;
RT "Structure and function study of rice bifunctional alpha-amylase/subtilisin
RT inhibitor from Oryza sativa.";
RL Submitted (JUL-2007) to the PDB data bank.
CC -!- FUNCTION: This protein inhibits independently subtilisin and
CC T.castaneum alpha-amylase but not barley alpha-amylase.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR EMBL; AB075524; BAB78730.1; -; Genomic_DNA.
DR EMBL; AY166458; AAN86549.1; -; mRNA.
DR EMBL; AL663019; CAE05648.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF15277.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90170.1; -; Genomic_DNA.
DR EMBL; AK106723; BAG97809.1; -; mRNA.
DR EMBL; AY166459; AAN86550.1; -; Genomic_DNA.
DR PIR; S24131; S24131.
DR RefSeq; XP_015634500.1; XM_015779014.1.
DR PDB; 2QN4; X-ray; 1.80 A; A/B=1-200.
DR PDBsum; 2QN4; -.
DR AlphaFoldDB; P29421; -.
DR SMR; P29421; -.
DR STRING; 4530.OS04T0526600-01; -.
DR MEROPS; I03.004; -.
DR PaxDb; P29421; -.
DR PRIDE; P29421; -.
DR EnsemblPlants; Os04t0526600-01; Os04t0526600-01; Os04g0526600.
DR GeneID; 4336455; -.
DR Gramene; Os04t0526600-01; Os04t0526600-01; Os04g0526600.
DR KEGG; osa:4336455; -.
DR eggNOG; ENOG502S0PJ; Eukaryota.
DR HOGENOM; CLU_090145_0_0_1; -.
DR InParanoid; P29421; -.
DR OMA; STEWHIG; -.
DR OrthoDB; 1343928at2759; -.
DR EvolutionaryTrace; P29421; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; P29421; OS.
DR GO; GO:0015066; F:alpha-amylase inhibitor activity; IDA:Gramene.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:Gramene.
DR CDD; cd00178; STI; 1.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR PRINTS; PR00291; KUNITZINHBTR.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alpha-amylase inhibitor; Direct protein sequencing;
KW Disulfide bond; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:1511747"
FT CHAIN 23..200
FT /note="Alpha-amylase/subtilisin inhibitor"
FT /id="PRO_0000083321"
FT SITE 88..89
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT DISULFID 63..112
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PDB:2QN4"
FT DISULFID 162..166
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PDB:2QN4"
FT CONFLICT 60..61
FT /note="VL -> RVI (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="A -> S (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="Missing (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="I -> L (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="I -> L (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="R -> GA (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="L -> I (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2QN4"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:2QN4"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2QN4"
SQ SEQUENCE 200 AA; 21417 MW; D3F9A2B32F52C34B CRC64;
MVSLRLPLIL LSLLAISFSC SAAPPPVYDT EGHELSADGS YYVLPASPGH GGGLTMAPRV
LPCPLLVAQE TDERRKGFPV RFTPWGGAAA PEDRTIRVST DVRIRFNAAT ICVQSTEWHV
GDEPLTGARR VVTGPLIGPS PSGRENAFRV EKYGGGYKLV SCRDSCQDLG VSRDGARAWL
GASQPPHVVV FKKARPSPPE
