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IBBR_ORYSJ
ID   IBBR_ORYSJ              Reviewed;         254 AA.
AC   Q0JR25; A0A0P0UXL8; C7IWR7; P07084; P93432; Q5ZCA7; Q7XZC9; Q9AWV9; Q9M3W2;
AC   Q9SAS2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Bowman-Birk type bran trypsin inhibitor;
DE   AltName: Full=OSE727A;
DE   AltName: Full=Protein RBBI3-3;
DE   AltName: Full=RBTI;
DE   Flags: Precursor;
GN   Name=RBBI3.3; OrderedLocusNames=Os01g0124401, Os01g0124400, LOC_Os01g03360;
GN   ORFNames=P0037C04.19, P0044F08.1;
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=Embryo;
RA   Masumura T., Fujioka M., Matsui Y., Kumazawa Y., Tashiro M., Morita S.,
RA   Tanaka K.;
RT   "Cloning, expression and localization pattern of a trypsin inhibitor gene
RT   from rice.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(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 [MRNA] OF 7-254.
RC   STRAIN=cv. Lomello; TISSUE=Embryo;
RA   Chen P.-W., Chow S.-H., Chen L.-J.;
RT   "Nucleotide sequence of a cDNA encoding rice Bowman-Birk proteinase
RT   inhibitor.";
RL   (er) Plant Gene Register PGR97-015(1997).
RN   [7]
RP   PROTEIN SEQUENCE OF 119-251.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=3667571; DOI=10.1093/oxfordjournals.jbchem.a122054;
RA   Tashiro M., Hashino K., Shiozaki M., Ibuki F., Maki Z.;
RT   "The complete amino acid sequence of rice bran trypsin inhibitor.";
RL   J. Biochem. 102:297-306(1987).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 119-251, AND DISULFIDE BONDS.
RX   PubMed=16754971; DOI=10.1107/s1744309106014795;
RA   Lin Y.H., Li H.T., Huang Y.C., Hsieh Y.C., Guan H.H., Liu M.Y., Chang T.,
RA   Wang A.H., Chen C.J.;
RT   "Purification, crystallization and preliminary X-ray crystallographic
RT   analysis of rice Bowman-Birk inhibitor from Oryza sativa.";
RL   Acta Crystallogr. F 62:522-524(2006).
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB68026.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAD10378.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Its N-terminal part is derived from the gene LOC_Os01g03390, which coded for an RBBI2.3 protein.; Evidence={ECO:0000305};
CC       Sequence=BAD52869.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB098712; BAC78439.1; -; mRNA.
DR   EMBL; AP002909; BAB21173.1; -; Genomic_DNA.
DR   EMBL; AP003233; BAD52869.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008207; BAH90883.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS70158.1; -; Genomic_DNA.
DR   EMBL; U57640; AAD10378.1; ALT_SEQ; mRNA.
DR   EMBL; U76004; AAB68026.1; ALT_INIT; mRNA.
DR   PIR; A27193; TIRZBR.
DR   PIR; T04161; T04161.
DR   RefSeq; XP_015622026.1; XM_015766540.1.
DR   PDB; 2QN5; X-ray; 3.00 A; B=119-251.
DR   PDBsum; 2QN5; -.
DR   AlphaFoldDB; Q0JR25; -.
DR   SMR; Q0JR25; -.
DR   STRING; 4530.OS01T0124401-01; -.
DR   MEROPS; I12.007; -.
DR   PaxDb; Q0JR25; -.
DR   PRIDE; Q0JR25; -.
DR   EnsemblPlants; Os01t0124401-01; Os01t0124401-01; Os01g0124401.
DR   GeneID; 9271230; -.
DR   Gramene; Os01t0124401-01; Os01t0124401-01; Os01g0124401.
DR   KEGG; osa:9271230; -.
DR   eggNOG; ENOG502R48J; Eukaryota.
DR   HOGENOM; CLU_059102_0_0_1; -.
DR   InParanoid; Q0JR25; -.
DR   OMA; HPGPVCK; -.
DR   OrthoDB; 12226at2759; -.
DR   EvolutionaryTrace; Q0JR25; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q0JR25; OS.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00023; BBI; 3.
DR   Gene3D; 2.10.69.10; -; 3.
DR   InterPro; IPR035995; Bowman-Birk_prot_inh.
DR   InterPro; IPR000877; Prot_inh_BBI.
DR   Pfam; PF00228; Bowman-Birk_leg; 4.
DR   SMART; SM00269; BowB; 3.
DR   SUPFAM; SSF57247; SSF57247; 3.
DR   PROSITE; PS00281; BOWMAN_BIRK; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Reference proteome; Repeat; Serine protease inhibitor;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..118
FT                   /evidence="ECO:0000269|PubMed:3667571"
FT                   /id="PRO_0000003286"
FT   CHAIN           119..251
FT                   /note="Bowman-Birk type bran trypsin inhibitor"
FT                   /id="PRO_0000003287"
FT   PROPEP          252..254
FT                   /id="PRO_0000003288"
FT   REPEAT          46..120
FT   REPEAT          121..187
FT   REPEAT          188..251
FT   SITE            135..136
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            201..202
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        125..185
FT                   /evidence="ECO:0000269|PubMed:16754971"
FT   DISULFID        126..143
FT                   /evidence="ECO:0000269|PubMed:16754971"
FT   DISULFID        152..159
FT                   /evidence="ECO:0000269|PubMed:16754971"
FT   DISULFID        156..172
FT                   /evidence="ECO:0000269|PubMed:16754971"
FT   DISULFID        193..248
FT                   /evidence="ECO:0000269|PubMed:16754971"
FT   DISULFID        194..209
FT                   /evidence="ECO:0000269|PubMed:16754971"
FT   DISULFID        199..207
FT                   /evidence="ECO:0000269|PubMed:16754971"
FT   DISULFID        216..223
FT                   /evidence="ECO:0000269|PubMed:16754971"
FT   DISULFID        220..236
FT                   /evidence="ECO:0000269|PubMed:16754971"
FT   CONFLICT        121
FT                   /note="R -> K (in Ref. 6; AAB68026/AAD10378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="K -> E (in Ref. 6; AAB68026/AAD10378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136..137
FT                   /note="PD -> TN (in Ref. 6; AAB68026/AAD10378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="P -> T (in Ref. 6; AAB68026/AAD10378)"
FT                   /evidence="ECO:0000305"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:2QN5"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:2QN5"
FT   STRAND          172..179
FT                   /evidence="ECO:0007829|PDB:2QN5"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:2QN5"
SQ   SEQUENCE   254 AA;  27790 MW;  32630D7DE579C1E8 CRC64;
     MSNTTMATST ILLFLLAGLA AAHGDGDTTI RLPSDGAKAS RPRAAKPWDC CDNIEISRLM
     IYPPLYRCND EVKQCAAACK ECVEAPGGDF NGGAFVCSDW FSTVDPGPKC TAALDGLSME
     RPWKCCDNIK RLPTKPDPPQ WRCNDELEPS QCTAACKSCR EAPGPFPGKL ICEDIYWGAD
     PGPFCTPRPW GDCCDKAFCN KMNPPTCRCM DEVKECADAC KDCQRVESSE PPRYVCKDRF
     TGHPGPVCKP RAEN
 
 
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