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Probable E3 ubiquitin-protein ligase LOG2 (EC 2.3.2.27) (Probable RING-type E3 ubiquitin transferase LOG2) (Protein LOSS OF GDU2) (RING finger protein 215)

 LOFG2_ARATH             Reviewed;         388 AA.
Q9S752;
31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 123.
RecName: Full=Probable E3 ubiquitin-protein ligase LOG2;
EC=2.3.2.27;
AltName: Full=Probable RING-type E3 ubiquitin transferase LOG2 {ECO:0000305};
AltName: Full=Protein LOSS OF GDU2;
AltName: Full=RING finger protein 215;
Name=LOG2; Synonyms=RF215, RIG2; OrderedLocusNames=At3g09770;
ORFNames=F11F8.36, F8A24.18;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
GENE FAMILY ORGANIZATION.
PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
Kosarev P., Mayer K.F.X., Hardtke C.S.;
"Evaluation and classification of RING-finger domains encoded by the
Arabidopsis genome.";
Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
[6]
FUNCTION, AND DOMAIN.
PubMed=15644464; DOI=10.1104/pp.104.052423;
Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E.,
Callis J.;
"Functional analysis of the RING-type ubiquitin ligase family of
Arabidopsis.";
Plant Physiol. 137:13-30(2005).
[7]
GENE SUBFAMILY, INTERACTION WITH GDU1, FUNCTION, TISSUE SPECIFICITY,
MUTAGENESIS OF GLY-2; ILE-321; CYS-354 AND CYS-357, SUBCELLULAR
LOCATION, MYRISTOYLATION AT GLY-2, AND DISRUPTION PHENOTYPE.
PubMed=22291198; DOI=10.1104/pp.111.191965;
Pratelli R., Guerra D.D., Yu S., Wogulis M., Kraft E., Frommer W.B.,
Callis J., Pilot G.;
"The ubiquitin E3 ligase LOSS OF GDU2 is required for GLUTAMINE
DUMPER1-induced amino acid secretion in Arabidopsis.";
Plant Physiol. 158:1628-1642(2012).
-!- FUNCTION: Acts as an E3 ubiquitin-protein ligase, or as part of E3
complex, which accepts ubiquitin from specific E2 ubiquitin-
conjugating enzymes and then transfers it to substrates (in
vitro). Required for GLUTAMINE DUMPER 1(GDU1)-induced amino acid
secretion and for amino acid homeostasis. Ubiquitinates GDU1 (in
vitro). {ECO:0000269|PubMed:15644464,
ECO:0000269|PubMed:22291198}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with GDU1. {ECO:0000269|PubMed:22291198}.
-!- INTERACTION:
O81775:GDU1; NbExp=15; IntAct=EBI-6290644, EBI-6290661;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22291198}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9S752-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in the vascular tissues in both
phloem and xylem parenchyma cells. {ECO:0000269|PubMed:22291198}.
-!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
ubiquitin-conjugating enzyme. {ECO:0000250}.
-!- PTM: Myristoylated (in vitro). {ECO:0000269|PubMed:22291198}.
-!- DISRUPTION PHENOTYPE: No visible phenotype.
{ECO:0000269|PubMed:22291198}.
-!- SIMILARITY: Belongs to the RING-type zinc finger family. LOG2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC015985; AAF23258.1; -; Genomic_DNA.
EMBL; AC016661; AAF23312.1; -; Genomic_DNA.
EMBL; CP002686; AEE74810.1; -; Genomic_DNA.
EMBL; AY074275; AAL66972.1; -; mRNA.
EMBL; AY087831; AAM65384.1; -; mRNA.
RefSeq; NP_566356.1; NM_111812.4. [Q9S752-1]
UniGene; At.22524; -.
ProteinModelPortal; Q9S752; -.
SMR; Q9S752; -.
BioGrid; 5469; 17.
IntAct; Q9S752; 7.
STRING; 3702.AT3G09770.1; -.
iPTMnet; Q9S752; -.
PaxDb; Q9S752; -.
EnsemblPlants; AT3G09770.1; AT3G09770.1; AT3G09770. [Q9S752-1]
GeneID; 820135; -.
Gramene; AT3G09770.1; AT3G09770.1; AT3G09770.
KEGG; ath:AT3G09770; -.
Araport; AT3G09770; -.
TAIR; locus:2075069; AT3G09770.
eggNOG; KOG4265; Eukaryota.
eggNOG; ENOG410XRAE; LUCA.
HOGENOM; HOG000239918; -.
InParanoid; Q9S752; -.
OMA; CANIMRM; -.
OrthoDB; EOG09360IAT; -.
PhylomeDB; Q9S752; -.
UniPathway; UPA00143; -.
PRO; PR:Q9S752; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9S752; baseline and differential.
Genevisible; Q9S752; AT.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
GO; GO:1901527; P:abscisic acid-activated signaling pathway involved in stomatal movement; IMP:CACAO.
GO; GO:0080144; P:amino acid homeostasis; IGI:UniProtKB.
GO; GO:0009737; P:response to abscisic acid; IMP:CACAO.
InterPro; IPR001841; Znf_RING.
SMART; SM00184; RING; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Lipoprotein;
Membrane; Metal-binding; Myristate; Reference proteome; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:22291198}.
CHAIN 2 388 Probable E3 ubiquitin-protein ligase
LOG2.
/FTId=PRO_0000419946.
ZN_FING 319 358 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
REGION 159 281 DAR2 domain.
COMPBIAS 12 17 Poly-Arg.
COMPBIAS 23 96 Pro-rich.
COMPBIAS 248 253 Poly-Glu.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:22291198}.
MUTAGEN 2 2 G->A: Abolishes myristoylation and plasma
membrane localization.
{ECO:0000269|PubMed:22291198}.
MUTAGEN 321 321 I->A: Reduces E3 ligase activity.
{ECO:0000269|PubMed:22291198}.
MUTAGEN 354 354 C->A: Abolishes E3 ligase activity; in
association with Ala-357.
{ECO:0000269|PubMed:22291198}.
MUTAGEN 357 357 C->A: Abolishes E3 ligase activity; in
association with Ala-354.
{ECO:0000269|PubMed:22291198}.
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


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