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TIRC_ORYSJ
ID   TIRC_ORYSJ              Reviewed;         568 AA.
AC   Q2R3K5; A0A0P0Y2W0; Q0ISI1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Transport inhibitor response 1-like protein Os11g0515500;
DE            Short=TIR1-like protein;
GN   OrderedLocusNames=Os11g0515500, LOC_Os11g31620;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
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=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   [4]
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   [5]
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).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. May
CC       interact with auxin and auxin-responsive proteins (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The F-box is necessary for the interaction with SKP1.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: The myo-inositol hexakisphosphate acts as a structural
CC       cofactor. {ECO:0000250}.
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DR   EMBL; DP000010; ABA93930.1; -; Genomic_DNA.
DR   EMBL; AP008217; BAF28334.2; -; Genomic_DNA.
DR   EMBL; AP014967; BAT14190.1; -; Genomic_DNA.
DR   EMBL; AK072358; BAG92936.1; -; mRNA.
DR   RefSeq; XP_015617534.1; XM_015762048.1.
DR   AlphaFoldDB; Q2R3K5; -.
DR   SMR; Q2R3K5; -.
DR   STRING; 4530.OS11T0515500-01; -.
DR   PaxDb; Q2R3K5; -.
DR   PRIDE; Q2R3K5; -.
DR   EnsemblPlants; Os11t0515500-01; Os11t0515500-01; Os11g0515500.
DR   GeneID; 4350590; -.
DR   Gramene; Os11t0515500-01; Os11t0515500-01; Os11g0515500.
DR   KEGG; osa:4350590; -.
DR   eggNOG; KOG1947; Eukaryota.
DR   HOGENOM; CLU_022456_1_0_1; -.
DR   InParanoid; Q2R3K5; -.
DR   OMA; SRWLGCF; -.
DR   OrthoDB; 1282076at2759; -.
DR   PlantReactome; R-OSA-5608118; Auxin signalling.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
DR   Genevisible; Q2R3K5; OS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0010011; F:auxin binding; ISS:UniProtKB.
DR   GO; GO:0000822; F:inositol hexakisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR041567; COI1_F-box.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR041101; Transp_inhibit.
DR   Pfam; PF18511; F-box_5; 1.
DR   Pfam; PF18791; Transp_inhibit; 1.
DR   SMART; SM00367; LRR_CC; 6.
PE   2: Evidence at transcript level;
KW   Auxin signaling pathway; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..568
FT                   /note="Transport inhibitor response 1-like protein
FT                   Os11g0515500"
FT                   /id="PRO_0000370733"
FT   DOMAIN          1..45
FT                   /note="F-box"
FT   REGION          338..343
FT                   /note="Interaction with auxin-responsive proteins"
FT                   /evidence="ECO:0000250"
FT   REGION          394..398
FT                   /note="Interaction with auxin-responsive proteins"
FT                   /evidence="ECO:0000250"
FT   REGION          453..454
FT                   /note="Interaction with auxin-responsive proteins"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         103..104
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         335
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         390..392
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         473..474
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   BINDING         498
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250"
FT   SITE            155
FT                   /note="Interaction with auxin-responsive proteins"
FT                   /evidence="ECO:0000250"
FT   SITE            369
FT                   /note="Interaction with auxin-responsive proteins"
FT                   /evidence="ECO:0000250"
FT   SITE            478
FT                   /note="Interaction with auxin-responsive proteins"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   568 AA;  62392 MW;  A316D048A26AE8B9 CRC64;
     MVFFPEEVVE HILGFLASHR DRNAVSLVCR EWYRVERLSR RSVLVRNCYA ARPERVHARF
     PGLRSLSVKG RPRFVPAGWG AAARPWVAAC VAACPGLEEL RLKRMVVTDG CLKLLACSFP
     NLKSLVLVGC QGFSTDGLAT VATNCRFMKE LDLQESLVED RDSRWLGCFP KPSTLLESLN
     FSCLTGEVNS PALEILVARS PNLRSLRLNR SVPLDVLARI LCRRPRLVDL CTGSFVRGNI
     VGAYAGLFNS FQHCSLLKSL SGFWDATSLF IPVIAPVCKN LTCLNLSSAP MVRSAYLIEF
     ICQCKKLQQL WVLDHIGDEG LKIVASSCIQ LQELRVFPAN ANARASTVTE EGLVAISAGC
     NKLQSVLYFC QRMTNSALIT VAKNCPRFTS FRLCVLDPGS ADAVTGQPLD EGYGAIVQSC
     KGLRRLCLSG LLTDTVFLYI GMYAERLEML SVAFAGDTDD GMTYVLNGCK NLKKLEIRDS
     PFGDSALLAG MHQYEAMRSL WLSSCNVTLG GCKSLAASMA NLNIEVMNRA ASINEADNAN
     DAKKVKKLYI YRTVAGPRGD APEFISTF
 
 
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