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IBBR_ORYSI
ID   IBBR_ORYSI              Reviewed;         254 AA.
AC   A2WK50; P07084; P93432; Q5ZCA7; Q7XZC9; Q9AWV9; Q9M3W2; Q9SAS2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 60.
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; ORFNames=OsI_000193;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Teqing; TISSUE=Leaf;
RX   PubMed=12972663; DOI=10.1104/pp.103.024810;
RA   Qu L.-J., Chen J., Liu M., Pan N., Okamoto H., Lin Z., Li C., Li D.,
RA   Wang J., Zhu G., Zhao X., Chen X., Gu H., Chen Z.;
RT   "Molecular cloning and functional analysis of a novel type of Bowman-Birk
RT   inhibitor gene family in rice.";
RL   Plant Physiol. 133:560-570(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC       {ECO:0000269|PubMed:12972663}.
CC   -!- INDUCTION: By wounding. {ECO:0000269|PubMed:12972663}.
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAY72346.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ277469; CAB88209.1; -; Genomic_DNA.
DR   EMBL; CM000126; EAY72346.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A2WK50; -.
DR   SMR; A2WK50; -.
DR   STRING; 39946.A2WK50; -.
DR   MEROPS; I12.007; -.
DR   HOGENOM; CLU_059102_0_0_1; -.
DR   Proteomes; UP000007015; Chromosome 1.
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   2: Evidence at transcript level;
KW   Disulfide bond; Protease inhibitor; Reference proteome; Repeat;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..118
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000293077"
FT   CHAIN           119..251
FT                   /note="Bowman-Birk type bran trypsin inhibitor"
FT                   /id="PRO_0000293078"
FT   PROPEP          252..254
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000293079"
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        51..248
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        125..185
FT                   /evidence="ECO:0000250"
FT   DISULFID        126..143
FT                   /evidence="ECO:0000250"
FT   DISULFID        152..159
FT                   /evidence="ECO:0000250"
FT   DISULFID        156..172
FT                   /evidence="ECO:0000250"
FT   DISULFID        193..248
FT                   /evidence="ECO:0000250"
FT   DISULFID        194..209
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        199..207
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        216..223
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        220..236
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
SQ   SEQUENCE   254 AA;  27756 MW;  B06BA7DFE579CF06 CRC64;
     MSNTTMATST ILLFLLAGLA AAHGDGDTTI RLPSDGAKAS RPRAAKPWDC CDNIEISRLM
     IYPPLYRCND EVKQCAAACK ECVEAPGGDF NGGAFVCSDW FSTVDPGPKC TAALDGLSME
     RPWKCCDNIK RLPTKPDPPQ WRCNDELEPS QCTAACKSCR EAPGPFPGKL ICEDIYWGAD
     PGPLCTPRPW GDCCDKAFCN KMNPPTCRCM DEVKECADAC KDCQRVESSE PPRYVCKDRF
     TGHPGPVCKP RAEN
 
 
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