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IPI1_ORYSJ
ID   IPI1_ORYSJ              Reviewed;         455 AA.
AC   Q5Z8R1; B7EHI9; Q0JMY2;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=E3 ubiquitin-protein ligase IPI1 {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000269|PubMed:28298520};
DE   AltName: Full=IPA1-interacting protein 1 {ECO:0000303|PubMed:28298520};
GN   Name=IPI1 {ECO:0000303|PubMed:28298520};
GN   OrderedLocusNames=Os01g0350900 {ECO:0000312|EMBL:BAS72030.1},
GN   LOC_Os01g24880 {ECO:0000305};
GN   ORFNames=B1051E10.48-1 {ECO:0000312|EMBL:BAD53853.1},
GN   P0463A02.18-1 {ECO:0000312|EMBL:BAD52927.1};
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 [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   [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] (ISOFORM 2).
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   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SPL14, SUBCELLULAR LOCATION,
RP   MUTAGENESIS OF HIS-74 AND CYS-80, AND DISRUPTION PHENOTYPE.
RX   PubMed=28298520; DOI=10.1105/tpc.16.00879;
RA   Wang J., Yu H., Xiong G., Lu Z., Jiao Y., Meng X., Liu G., Chen X.,
RA   Wang Y., Li J.;
RT   "Tissue-specific ubiquitination by IPA1 INTERACTING PROTEIN1 modulates IPA1
RT   protein levels to regulate plant architecture in rice.";
RL   Plant Cell 29:697-707(2017).
CC   -!- FUNCTION: Functions as an E3 ligase that promotes polyubiquitination of
CC       SPL14/IPA1 for subsequent proteasomal degradation (PubMed:28298520).
CC       Regulates plant architecture by modulating SPL14/IPA1 abundance
CC       (PubMed:28298520). Promotes the degradation of SPL14/IPA1 in panicles,
CC       while it stabilizes SPL14/IPA1 in shoot apices (PubMed:28298520).
CC       Ubiquitinates the SPL14/IPA1-mediated complex with 'Lys-48'-linked
CC       polyubiquitin in panicles and 'Lys-63'-linked polyubiquitin chains in
CC       the shoot apex (PubMed:28298520). {ECO:0000269|PubMed:28298520}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000269|PubMed:28298520};
CC   -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC   -!- SUBUNIT: Interacts with SPL14/IPA1. {ECO:0000269|PubMed:28298520}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28298520}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5Z8R1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5Z8R1-2; Sequence=VSP_061157;
CC   -!- DISRUPTION PHENOTYPE: Altered plant architecture, including increased
CC       number of tillers, enlarged panicles, and increased grain yield per
CC       plant. {ECO:0000269|PubMed:28298520}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF04896.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP003258; BAD52927.1; -; Genomic_DNA.
DR   EMBL; AP003764; BAD53853.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF04896.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014957; BAS72030.1; -; Genomic_DNA.
DR   EMBL; AK070217; BAG91836.1; -; mRNA.
DR   EnsemblPlants; Os01t0350900-01; Os01t0350900-01; Os01g0350900. [Q5Z8R1-2]
DR   EnsemblPlants; Os01t0350900-02; Os01t0350900-02; Os01g0350900. [Q5Z8R1-1]
DR   Gramene; Os01t0350900-01; Os01t0350900-01; Os01g0350900. [Q5Z8R1-2]
DR   Gramene; Os01t0350900-02; Os01t0350900-02; Os01g0350900. [Q5Z8R1-1]
DR   HOGENOM; CLU_037685_0_1_1; -.
DR   InParanoid; Q5Z8R1; -.
DR   PlantReactome; R-OSA-9030908; Underwater shoot and internode elongation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; Q5Z8R1; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0044260; P:cellular macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0048450; P:floral organ structural organization; IMP:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0080050; P:regulation of seed development; IMP:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR044274; RFI2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46798; PTHR46798; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Metal-binding; Nucleus; Reference proteome;
KW   Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..455
FT                   /note="E3 ubiquitin-protein ligase IPI1"
FT                   /id="PRO_0000453486"
FT   ZN_FING         51..97
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         304..455
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_061157"
FT   MUTAGEN         74
FT                   /note="H->Y: Loss of E3 ubiquitin-protein ligase activity."
FT                   /evidence="ECO:0000269|PubMed:28298520"
FT   MUTAGEN         80
FT                   /note="C->S: Loss of E3 ubiquitin-protein ligase activity."
FT                   /evidence="ECO:0000269|PubMed:28298520"
SQ   SEQUENCE   455 AA;  48894 MW;  31ECDF03DAD6ECBD CRC64;
     MGAEEEEEPA SAVGREGGGG GGGARAAGAG AGGDTADDDD SGESAAAVVP CSICLDAVVA
     GGGDRSTARL QCGHEFHLDC IGSAFNAKGV MQCPNCRQIE RGNWLYANGS RPSQDVSNDD
     WGHDEDFYDA NQPETSRSVF LPFRFQWCPI GRLAQLPSVF DEGESAPPVT FHDFMGQNFT
     SEHLPVSAPG ATPPGPYIAY FQPLQSSASS SSSHVTERTM DGTTYHDHWN PLPGPSDGRP
     LATVHPIDFH HNHWTHLPNS YSQPNSNNGV AEQMAIPVVP MRVGGLDSDS QQRGSLPSVY
     GNGSGSRSRI PSVPPMAPQF MRPHGNINEQ YQQNSSSLYA APQRRTAVQA VQDSMNFTLF
     PQAPTGPNSM ETEDAGGNQF YAWERDRFAP YPLMPVDSEA NWWGSTPQSH GVTDHSAAPG
     RRLFGQWIGA GRSPPPPPPP PADNSSYRQM HIPRM
 
 
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