位置:首页 > 蛋白库 > RF4_ARATH
RF4_ARATH
ID   RF4_ARATH               Reviewed;         823 AA.
AC   Q9ZVT8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Putative E3 ubiquitin-protein ligase RF4;
DE            EC=2.3.2.27;
DE   AltName: Full=RING finger protein 4;
DE   AltName: Full=RING-type E3 ubiquitin transferase RF4 {ECO:0000305};
GN   Name=RF4; OrderedLocusNames=At1g03365; ORFNames=F15K9.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA   Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT   "Evaluation and classification of RING-finger domains encoded by the
RT   Arabidopsis genome.";
RL   Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RING-type zinc finger family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC005278; AAC72106.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27564.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM58631.1; -; Genomic_DNA.
DR   PIR; D86165; D86165.
DR   RefSeq; NP_001184899.1; NM_001197970.2.
DR   RefSeq; NP_001321053.1; NM_001331406.1.
DR   AlphaFoldDB; Q9ZVT8; -.
DR   SMR; Q9ZVT8; -.
DR   STRING; 3702.AT1G03365.1; -.
DR   PaxDb; Q9ZVT8; -.
DR   PRIDE; Q9ZVT8; -.
DR   ProteomicsDB; 236992; -.
DR   EnsemblPlants; AT1G03365.1; AT1G03365.1; AT1G03365.
DR   EnsemblPlants; AT1G03365.2; AT1G03365.2; AT1G03365.
DR   GeneID; 10723112; -.
DR   Gramene; AT1G03365.1; AT1G03365.1; AT1G03365.
DR   Gramene; AT1G03365.2; AT1G03365.2; AT1G03365.
DR   KEGG; ath:AT1G03365; -.
DR   Araport; AT1G03365; -.
DR   TAIR; locus:6530298128; AT1G03365.
DR   eggNOG; ENOG502SB0J; Eukaryota.
DR   HOGENOM; CLU_012143_0_1_1; -.
DR   InParanoid; Q9ZVT8; -.
DR   OMA; KPHAIAR; -.
DR   OrthoDB; 259830at2759; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9ZVT8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9ZVT8; baseline and differential.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Metal-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..823
FT                   /note="Putative E3 ubiquitin-protein ligase RF4"
FT                   /id="PRO_0000395977"
FT   ZN_FING         768..808
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          24..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          536..738
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        25..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   823 AA;  91537 MW;  64D007A4E87D0E53 CRC64;
     MSIVQKQEEM NGCGLNVDKV EAFTVSPQEK GRKNKRKLAD PSQPNASSLT EFPPYELPSL
     KPQNHLSGNG SVGEVSNQLQ VEVSESVEWD DPFACHLEEL LSSNLLTLFL DTMKQLIDLG
     YTDDEVLKAV SRCRLYCGGN NLLSNIVNNT LSALKTGDEG AGSGDYVFED LQQLVSYTLV
     EMISLIKEVR PSLSTVEAMW RLLMCDLNVL QAFEAEGDGL VSSSKLSDSE SLGAESNPPK
     SSDPDNPKPP QSDPQSNRNE PLKFGNFPNT PNSKKTQSSG TTPGKEVCSG STVSCQGMRS
     TSFTLVSDEK LVSCRKGRTK KEIAMLRQKS CVEKIRTYSK GSGYKAAKFA SVGSFLLEKR
     VKSSSEFVPR NSSSKITAEI GVKVSLAEDS GCFVRKNSKL DSPVVVVDAK GYITALPARS
     VKSASKKKTG SESVTLIPSA SEKKSDSSIP STSEKKSGSE SEEKASVSAK LAPDYYAGIP
     YDAALGIYVP RDKKDELILK LVPRVNDLQN ELQVWTDWAN QKVKEATGRL LKDQPELKAL
     RKEREEAEQY KKEKQLLEEN TRKRLSEMDF ALKNATSQLE KAFNTAHRLE LEQSILKKEM
     EAAKIKAVES AESFREAKER GERSLKDIHS WEGQKIMLQE ELKGQREKVT VLQKEVTKAK
     NRQNQIEAAL KQERTAKGKL SAQASLIRKE TKELEALGKV EEERIKGKAE TDVKYYIDNI
     KRLEREISEL KLKSDYSRII ALKKGSSESK ATKRESLGMP KVKRERECVM CLSEEMSVIF
     LPCAHQVLCF KCNQLHEKEG MMDCPSCRGT IHRRIQARFA RSG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024