LOFG2_ARATH
ID LOFG2_ARATH Reviewed; 388 AA.
AC Q9S752;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable E3 ubiquitin-protein ligase LOG2;
DE EC=2.3.2.27;
DE AltName: Full=Probable RING-type E3 ubiquitin transferase LOG2 {ECO:0000305};
DE AltName: Full=Protein LOSS OF GDU2;
DE AltName: Full=RING finger protein 215;
GN Name=LOG2; Synonyms=RF215, RIG2; OrderedLocusNames=At3g09770;
GN ORFNames=F11F8.36, F8A24.18;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [7]
RP GENE SUBFAMILY, INTERACTION WITH GDU1, FUNCTION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF GLY-2; ILE-321; CYS-354 AND CYS-357, SUBCELLULAR LOCATION,
RP MYRISTOYLATION AT GLY-2, AND DISRUPTION PHENOTYPE.
RX PubMed=22291198; DOI=10.1104/pp.111.191965;
RA Pratelli R., Guerra D.D., Yu S., Wogulis M., Kraft E., Frommer W.B.,
RA Callis J., Pilot G.;
RT "The ubiquitin E3 ligase LOSS OF GDU2 is required for GLUTAMINE DUMPER1-
RT induced amino acid secretion in Arabidopsis.";
RL Plant Physiol. 158:1628-1642(2012).
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates (in vitro). Required for
CC GLUTAMINE DUMPER 1(GDU1)-induced amino acid secretion and for amino
CC acid homeostasis. Ubiquitinates GDU1 (in vitro).
CC {ECO:0000269|PubMed:15644464, ECO:0000269|PubMed:22291198}.
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 GDU1. {ECO:0000269|PubMed:22291198}.
CC -!- INTERACTION:
CC Q9S752; O81775: GDU1; NbExp=15; IntAct=EBI-6290644, EBI-6290661;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22291198}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9S752-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues in both phloem
CC and xylem parenchyma cells. {ECO:0000269|PubMed:22291198}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- PTM: Myristoylated (in vitro). {ECO:0000269|PubMed:22291198}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:22291198}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. LOG2
CC subfamily. {ECO:0000305}.
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DR EMBL; AC015985; AAF23258.1; -; Genomic_DNA.
DR EMBL; AC016661; AAF23312.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74810.1; -; Genomic_DNA.
DR EMBL; AY074275; AAL66972.1; -; mRNA.
DR EMBL; AY087831; AAM65384.1; -; mRNA.
DR RefSeq; NP_566356.1; NM_111812.4. [Q9S752-1]
DR AlphaFoldDB; Q9S752; -.
DR BioGRID; 5469; 17.
DR IntAct; Q9S752; 16.
DR MINT; Q9S752; -.
DR STRING; 3702.AT3G09770.1; -.
DR iPTMnet; Q9S752; -.
DR PaxDb; Q9S752; -.
DR PRIDE; Q9S752; -.
DR ProteomicsDB; 238471; -. [Q9S752-1]
DR EnsemblPlants; AT3G09770.1; AT3G09770.1; AT3G09770. [Q9S752-1]
DR GeneID; 820135; -.
DR Gramene; AT3G09770.1; AT3G09770.1; AT3G09770. [Q9S752-1]
DR KEGG; ath:AT3G09770; -.
DR Araport; AT3G09770; -.
DR TAIR; locus:2075069; AT3G09770.
DR eggNOG; KOG4265; Eukaryota.
DR HOGENOM; CLU_016631_0_0_1; -.
DR InParanoid; Q9S752; -.
DR OMA; RMQNTKC; -.
DR PhylomeDB; Q9S752; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9S752; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S752; baseline and differential.
DR Genevisible; Q9S752; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:1901527; P:abscisic acid-activated signaling pathway involved in stomatal movement; IMP:CACAO.
DR GO; GO:0080144; P:amino acid homeostasis; IGI:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:CACAO.
DR CDD; cd16789; mRING-HC-C3HC5_MGRN1_like---blasttree; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR045195; MGRN1/RNF157_mRING_C3HC5.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; PTHR22996; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:22291198"
FT CHAIN 2..388
FT /note="Probable E3 ubiquitin-protein ligase LOG2"
FT /id="PRO_0000419946"
FT ZN_FING 319..358
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..281
FT /note="DAR2 domain"
FT REGION 368..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:22291198"
FT MUTAGEN 2
FT /note="G->A: Abolishes myristoylation and plasma membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:22291198"
FT MUTAGEN 321
FT /note="I->A: Reduces E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:22291198"
FT MUTAGEN 354
FT /note="C->A: Abolishes E3 ligase activity; in association
FT with Ala-357."
FT /evidence="ECO:0000269|PubMed:22291198"
FT MUTAGEN 357
FT /note="C->A: Abolishes E3 ligase activity; in association
FT with Ala-354."
FT /evidence="ECO:0000269|PubMed:22291198"
SQ SEQUENCE 388 AA; 42848 MW; D0DAAE050FA2D488 CRC64;
MGNISSSGGE GRRRRRRNHT AAPPPPPPPP SSSLPPPPLP TEIQANPIVF AAVTPYPNPN
PNPVYQYPAS YYHHPPPGAM PLPPYDHHLQ HHPPHPYHNH SWAPVAMARY PYAGHMMAQP
TPYVEHQKAV TIRNDVNLKK ESLRLEPDPD NPGRFLVSFT FDATVSGRIS VIFFAKESED
CKLTATKEDI LPPITLDFEK GLGQKFKQSS GSGIDFSVFE DVELFKAAAD TEIYPLAVKA
EAAPSGGENE EEERSGSKNA QITQAVYEKD KGEIKIRVVK QILWVNGTRY ELQEIYGIGN
TVEGDDDSAD DANDPGKECV ICLSEPRDTT VLPCRHMCMC SGCAKVLRFQ TNRCPICRQP
VERLLEIKVH GNNGSGNNTG QGETVEQE
