HOS1_ARATH
ID HOS1_ARATH Reviewed; 927 AA.
AC Q84JU6; O22289;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=E3 ubiquitin-protein ligase HOS1;
DE EC=2.3.2.27;
DE AltName: Full=Protein HIGH EXPRESSION OF OSMOTICALLY RESPONSIVE GENE 1;
DE AltName: Full=RING finger protein HOS1;
DE AltName: Full=RING-type E3 ubiquitin transferase HOS1 {ECO:0000305};
GN Name=HOS1; OrderedLocusNames=At2g39810; ORFNames=T5I7.11;
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 [GENOMIC DNA / MRNA], INDUCTION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=11297514; DOI=10.1101/gad.866801;
RA Lee H., Xiong L., Gong Z., Ishitani M., Stevenson B., Zhu J.-K.;
RT "The Arabidopsis HOS1 gene negatively regulates cold signal transduction
RT and encodes a RING finger protein that displays cold-regulated nucleo-
RT cytoplasmic partitioning.";
RL Genes Dev. 15:912-924(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, MUTAGENESIS OF HIS-75 AND CYS-89, AND INTERACTION WITH ICE1.
RX PubMed=16702557; DOI=10.1073/pnas.0602874103;
RA Dong C.H., Agarwal M., Zhang Y., Xie Q., Zhu J.K.;
RT "The negative regulator of plant cold responses, HOS1, is a RING E3 ligase
RT that mediates the ubiquitination and degradation of ICE1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8281-8286(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX BY MASS SPECTROMETRY, AND
RP FUNCTION.
RX PubMed=21189294; DOI=10.1105/tpc.110.079947;
RA Tamura K., Fukao Y., Iwamoto M., Haraguchi T., Hara-Nishimura I.;
RT "Identification and characterization of nuclear pore complex components in
RT Arabidopsis thaliana.";
RL Plant Cell 22:4084-4097(2010).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH FLK; MSI4/FVE AND
RP SCRM/ICE1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP INTERMITTENT COLD.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=22960247; DOI=10.1093/pcp/pcs123;
RA Lee J.H., Kim J.J., Kim S.H., Cho H.J., Kim J., Ahn J.H.;
RT "The E3 ubiquitin ligase HOS1 regulates low ambient temperature-responsive
RT flowering in Arabidopsis thaliana.";
RL Plant Cell Physiol. 53:1802-1814(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of the transcription factor ICE1.
CC Acts as a negative regulator of cold signaling pathways
CC (PubMed:16702557). Probably involved in recruiting the NUP107-160
CC subcomplex of the nuclear pore complex to chromatin (Probable).
CC Controls flowering time in response to ambient temperatures (16 and 23
CC degrees Celsius) and intermittent cold, probably via the regulation of
CC FT and TSF levels (PubMed:22960247). {ECO:0000269|PubMed:16702557,
CC ECO:0000269|PubMed:22960247, ECO:0000305|PubMed:21189294}.
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 -!- SUBUNIT: Interacts with SCRM/ICE1, FLK and MSI4/FVE.
CC {ECO:0000269|PubMed:16702557, ECO:0000269|PubMed:22960247}.
CC -!- INTERACTION:
CC Q84JU6; Q9LSE2: SCRM; NbExp=3; IntAct=EBI-15583242, EBI-15583266;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11297514,
CC ECO:0000269|PubMed:22960247}. Cytoplasm {ECO:0000269|PubMed:11297514,
CC ECO:0000269|PubMed:22960247}. Note=Nuclear after cold treatment.
CC Cytoplasmic when plant are grown or returned to normal growth
CC temperatures. {ECO:0000269|PubMed:11297514,
CC ECO:0000269|PubMed:22960247}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in leaf
CC vasculature, roots and root tips. {ECO:0000269|PubMed:11297514,
CC ECO:0000269|PubMed:22960247}.
CC -!- INDUCTION: Rapid and transient reduction of expression in response to
CC brief cold treatment. After recovery, the level is maintained until 2
CC days after cold treatment, before declining again.
CC {ECO:0000269|PubMed:11297514, ECO:0000269|PubMed:22960247}.
CC -!- DOMAIN: The RING domain is required for E3 ubiquitin ligase activity.
CC -!- DOMAIN: The C-terminal part of HOS1 is involved in the interaction with
CC ICE1.
CC -!- DISRUPTION PHENOTYPE: Early flowering, and insensitivity to ambient
CC temperature and to intermittent cold, but normal responses to
CC vernalization and gibberellic acid. {ECO:0000269|PubMed:22960247}.
CC -!- MISCELLANEOUS: Loss-of-function mutation (hos1) in the gene shows an
CC early flowering phenotype due to a constitutive vernalization and a
CC reduced freezing tolerance without cold acclimation.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB87130.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003000; AAB87130.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09734.1; -; Genomic_DNA.
DR EMBL; BT004255; AAO42259.1; -; mRNA.
DR EMBL; BT005517; AAO63937.1; -; mRNA.
DR PIR; T01011; T01011.
DR RefSeq; NP_181511.3; NM_129540.5.
DR AlphaFoldDB; Q84JU6; -.
DR SMR; Q84JU6; -.
DR BioGRID; 3906; 18.
DR DIP; DIP-61174N; -.
DR IntAct; Q84JU6; 1.
DR STRING; 3702.AT2G39810.1; -.
DR iPTMnet; Q84JU6; -.
DR PaxDb; Q84JU6; -.
DR PRIDE; Q84JU6; -.
DR ProteomicsDB; 230248; -.
DR EnsemblPlants; AT2G39810.1; AT2G39810.1; AT2G39810.
DR GeneID; 818568; -.
DR Gramene; AT2G39810.1; AT2G39810.1; AT2G39810.
DR KEGG; ath:AT2G39810; -.
DR Araport; AT2G39810; -.
DR TAIR; locus:2063917; AT2G39810.
DR eggNOG; ENOG502QUFI; Eukaryota.
DR HOGENOM; CLU_013617_0_0_1; -.
DR InParanoid; Q84JU6; -.
DR OrthoDB; 400460at2759; -.
DR PhylomeDB; Q84JU6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q84JU6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84JU6; baseline and differential.
DR Genevisible; Q84JU6; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025151; ELYS_dom.
DR InterPro; IPR044718; HOS1.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47358; PTHR47358; 1.
DR Pfam; PF13934; ELYS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Sensory transduction; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..927
FT /note="E3 ubiquitin-protein ligase HOS1"
FT /id="PRO_0000248162"
FT ZN_FING 53..93
FT /note="RING-type; degenerate"
FT REGION 678..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 75
FT /note="H->Y: Loss of E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:16702557"
FT MUTAGEN 89
FT /note="C->S: Loss of E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:16702557"
SQ SEQUENCE 927 AA; 105229 MW; 65932F2A2BE0E12D CRC64;
MDTREINGFA SAARSISLPT QPNYSSKPVQ EALKHLASIN LRELCNEAKV ERCRATRDLA
SCGRFVNYVL NPCGHASLCT ECCQRCDVCP ICRSTLPKFG DRLRLRLYYE CVEAGLISRT
HEEASQDSDE DEHQLAADVH RLYSLFDVAM NNNLISVVCH YITNVCMDET AVSSDPVIAF
LLDEVVVKDW VKRTFRSTLA ELQEIYNLET KEMQAWLDKL LRCSKQVAGI CSVLEVMESA
FKGSVSPQLQ DVQTLRENIG KTKQHLDIMV WCIRHGFLDD VRSRYSNFTS WNALVGERKS
NAVKRAWPDA VDQSSDCSVQ SASLFIEDAL ENLEREPEYS QEIGADLEVG RLQKDKRSFL
RSKIEGTSGS YPFENLRTAA DMLFLHGGSD LVVAKQAIFL YYLFDRHWTT PEKYWKHTID
DFAATFGITR HSLLESFVFY LLDDHSEEAL QEACRILPEI CGPETYPKVA QVLLERDNPE
TALMVLRWSG RDGVSELVSI GEAVTALRVR VECGLLSEAF TYQRTLCLKV KENNLKNGAV
KHASDDLDIW SWTEWMEILV NEFCCLSIRR NLVDRIIELP WNPDEEKYLH RCLLDSATDD
PSSAVGSLLV VFYLQRYRYI QAYQVDLRLQ KIEEAFVSDN QIGEEVMFRM RSQSHWRKEL
VDRAIDILPV IQQQQVRSGQ FSEMEDASEG AKKSDLPDAP DMITSSVPFA TTNSVFLQSA
NNARAREPVA NNGSPFQPGH MIGNASHDLS HGRLFTNANR GQKSEVRSVT KNLKFGEMST
PFKDLNRARG NSQLQGKRTE ESSPEVNVDR YIENNMSSPY LRRITANNPV TVKSSSNHLN
GSSQKPESTF FGTRMQPDKD NFVDLDDPMD MSSSLKDNNN NVLATESRNN SGGLRWRSDE
TSDDEDELTS FGSMPVKGRR RRRFAAR
