HAKAI_ARATH
ID HAKAI_ARATH Reviewed; 360 AA.
AC Q9LFC0; A0A178UJ32;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=E3 ubiquitin-protein ligase HAKAI homolog {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase HAKAI {ECO:0000305};
GN Name=HAKAI {ECO:0000303|PubMed:28503769};
GN OrderedLocusNames=At5g01160 {ECO:0000312|Araport:AT5G01160};
GN ORFNames=F7J8_140 {ECO:0000312|EMBL:CAB69844.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MTB AND
RP VIR, AND SUBCELLULAR LOCATION.
RX PubMed=28503769; DOI=10.1111/nph.14586;
RA Ruzicka K., Zhang M., Campilho A., Bodi Z., Kashif M., Saleh M.,
RA Eeckhout D., El-Showk S., Li H., Zhong S., De Jaeger G., Mongan N.P.,
RA Hejatko J., Helariutta Y., Fray R.G.;
RT "A mRNA methylation in Arabidopsis reveals a role for the conserved E3
RT ubiquitin ligase HAKAI.";
RL New Phytol. 215:157-172(2017).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase which is a subunit of
CC the N6-methyltransferase complex, a multiprotein complex that mediates
CC N6-methyladenosine (m6A) methylation at the 5'-[AG]GAC-3' consensus
CC sites of some mRNAs (PubMed:28503769). Associates with MTA, MTB, FIP37
CC and VIR to form the m6A writer complex which is essential for adenosine
CC methylation at specific mRNA sequences (PubMed:28503769). N6-
CC methyladenosine (m6A) plays a role in mRNA stability, processing,
CC translation efficiency and editing (PubMed:28503769).
CC {ECO:0000269|PubMed:28503769}.
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:0000305};
CC -!- SUBUNIT: Interacts with MTB and VIR (PubMed:28503769). Associates with
CC MTA, MTB, FIP37 and VIR to form the m6A writer complex which is
CC essential for adenosine methylation at specific mRNA sequences
CC (PubMed:28503769). {ECO:0000269|PubMed:28503769}.
CC -!- INTERACTION:
CC Q9LFC0; Q5PP65: At2g35430; NbExp=3; IntAct=EBI-15192365, EBI-15192363;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:28503769}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:28503769}.
CC -!- SIMILARITY: Belongs to the Hakai family. {ECO:0000305}.
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DR EMBL; AL137189; CAB69844.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90305.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69516.1; -; Genomic_DNA.
DR EMBL; BT024744; ABD59082.1; -; mRNA.
DR EMBL; AK227241; BAE99278.1; -; mRNA.
DR PIR; T45956; T45956.
DR RefSeq; NP_001331186.1; NM_001342575.1.
DR RefSeq; NP_195736.1; NM_120194.5.
DR AlphaFoldDB; Q9LFC0; -.
DR SMR; Q9LFC0; -.
DR IntAct; Q9LFC0; 15.
DR STRING; 3702.AT5G01160.1; -.
DR iPTMnet; Q9LFC0; -.
DR PaxDb; Q9LFC0; -.
DR PRIDE; Q9LFC0; -.
DR ProteomicsDB; 247350; -.
DR EnsemblPlants; AT5G01160.1; AT5G01160.1; AT5G01160.
DR EnsemblPlants; AT5G01160.2; AT5G01160.2; AT5G01160.
DR GeneID; 831742; -.
DR Gramene; AT5G01160.1; AT5G01160.1; AT5G01160.
DR Gramene; AT5G01160.2; AT5G01160.2; AT5G01160.
DR KEGG; ath:AT5G01160; -.
DR Araport; AT5G01160; -.
DR TAIR; locus:2150094; AT5G01160.
DR eggNOG; KOG2932; Eukaryota.
DR HOGENOM; CLU_041733_0_0_1; -.
DR InParanoid; Q9LFC0; -.
DR OMA; INHPPPG; -.
DR OrthoDB; 1161986at2759; -.
DR PhylomeDB; Q9LFC0; -.
DR PRO; PR:Q9LFC0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFC0; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0080009; P:mRNA methylation; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; IBA:GO_Central.
DR CDD; cd16508; RING-HC_HAKAI_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR040380; HAKAI-like_RING-HC.
DR InterPro; IPR040383; HAKAI/CBLL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13480; PTHR13480; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..360
FT /note="E3 ubiquitin-protein ligase HAKAI homolog"
FT /id="PRO_0000445519"
FT ZN_FING 72..107
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 123..148
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 39772 MW; B53DA47C1F1F2D3C CRC64;
MLQIRLRRDS PTETGNGARP SPTETVTVAC PDHLVLADLP VAKGIGSVTP TTVIKPVGRR
SRRQLGERVH FCVRCDFPIA IYGRLIPCDH AFCLECARSD SICYLCDERI QKIQTIKMME
GIFICAAPHC LRSFLKKLDF EAHVHDLHGS LLQADAEKED GNQSDVQSTM QQSSASESTL
RAPLRSQLQQ SRELNRSASF AKSQSGFSQV QNYPPDSDNS RPPGFETASP KPGIRFPDYP
QPMNLMQPPS LPVPMNQNPG LPQQFGFPSY PTTESGSSQQ FFNGAQYEMT RTESGGSEQS
SLLGYPPPSP MTNLNFQGSY PPPSWNPGMA PPHTTQQVNR GRDGQSFGWP QENRDGFGQE
