ASG2_ARATH
ID ASG2_ARATH Reviewed; 757 AA.
AC Q94BQ3; Q9LEU6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Protein ALTERED SEED GERMINATION 2 {ECO:0000303|PubMed:26147561};
GN Name=ASG2 {ECO:0000303|PubMed:26147561};
GN OrderedLocusNames=At5g10940 {ECO:0000312|Araport:AT5G10940};
GN ORFNames=T30N20.210 {ECO:0000312|EMBL:CAB96849.1};
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] (ISOFORM 1).
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 GENE FAMILY.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [5]
RP GENE FAMILY.
RX PubMed=18552200; DOI=10.1105/tpc.108.058891;
RA Zhang Y., Feng S., Chen F., Chen H., Wang J., McCall C., Xiong Y.,
RA Deng X.W.;
RT "Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 forms a nuclear E3 ubiquitin
RT ligase with DDB1 and CUL4 that is involved in multiple plant developmental
RT processes.";
RL Plant Cell 20:1437-1455(2008).
RN [6]
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 [7]
RP FUNCTION, MUTAGENESIS OF 245-ARG--ARG-257 AND CYS-754, DISRUPTION
RP PHENOTYPE, ISOPRENYLATION AT CYS-754, SUBCELLULAR LOCATION, INTERACTION
RP WITH DDB1A, AND NUCLEAR LOCALIZATION SIGNAL.
RC STRAIN=cv. Columbia;
RX PubMed=26147561; DOI=10.1111/pce.12605;
RA Dutilleul C., Ribeiro I., Blanc N., Nezames C.D., Deng X.W., Zglobicki P.,
RA Palacio Barrera A.M., Atehortua L., Courtois M., Labas V.,
RA Giglioli-Guivarc'h N., Ducos E.;
RT "ASG2 is a farnesylated DWD protein that acts as ABA negative regulator in
RT Arabidopsis.";
RL Plant Cell Environ. 39:185-198(2016).
RN [8]
RP FUNCTION, MUTAGENESIS OF CYS-754, DISRUPTION PHENOTYPE, INTERACTION WITH
RP HDA9, ISOPRENYLATION, SUBCELLULAR LOCATION, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=28663238; DOI=10.1534/genetics.116.198382;
RA Ducos E., Verges V., Duge de Bernonville T., Blanc N.,
RA Giglioli-Guivarc'h N., Dutilleul C.;
RT "Remarkable evolutionary conservation of antiobesity ADIPOSE/WDTC1 homologs
RT in animals and plants.";
RL Genetics 207:153-162(2017).
CC -!- FUNCTION: May function as a substrate adapter for CUL4-DDB1 E3
CC ubiquitin-protein ligase complex (Probable). Negative regulator of
CC fatty acid biosynthetic process and accumulation (PubMed:28663238).
CC Acts as an abscisic acid (ABA) negative regulator (PubMed:26147561).
CC Involved in responses to salt (NaCl) and osmotic (e.g. in response to
CC mannitol and PEG) stresses (PubMed:26147561).
CC {ECO:0000269|PubMed:26147561, ECO:0000269|PubMed:28663238,
CC ECO:0000305|PubMed:26147561}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8N5D0}.
CC -!- SUBUNIT: Interacts with DDB1; the subcellular localization of this
CC complex depends on farnesylation status (PubMed:26147561). Binds to
CC HDA9 in the cytosol when farnesylated (PubMed:28663238).
CC {ECO:0000269|PubMed:26147561, ECO:0000269|PubMed:28663238}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:26147561}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:26147561, ECO:0000269|PubMed:28663238}.
CC Note=Excluded from the nucleus when farnesylated at Cys-754.
CC {ECO:0000269|PubMed:26147561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94BQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94BQ3-2; Sequence=VSP_060594;
CC -!- PTM: Farnesylated at Cys-754 by FTB/ERA1; this modification triggers an
CC exclusion from the nucleus. {ECO:0000269|PubMed:26147561,
CC ECO:0000269|PubMed:28663238}.
CC -!- DISRUPTION PHENOTYPE: Production of 'obese' seeds characterized by
CC increased weight, oil body density and higher fatty acid contents
CC (PubMed:28663238). Increased sensitivity to abscisic acid (ABA) as well
CC as salt (NaCl) and osmotic (e.g. in response to mannitol and PEG)
CC stresses in term of seed germination and roots elongation
CC (PubMed:26147561). {ECO:0000269|PubMed:26147561,
CC ECO:0000269|PubMed:28663238}.
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DR EMBL; AL365234; CAB96849.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91611.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91612.1; -; Genomic_DNA.
DR EMBL; AY039964; AAK64141.1; -; mRNA.
DR EMBL; AY150424; AAN12885.1; -; mRNA.
DR PIR; T50803; T50803.
DR RefSeq; NP_001190286.1; NM_001203357.2. [Q94BQ3-2]
DR RefSeq; NP_568242.1; NM_121132.4. [Q94BQ3-1]
DR AlphaFoldDB; Q94BQ3; -.
DR SMR; Q94BQ3; -.
DR IntAct; Q94BQ3; 1.
DR STRING; 3702.AT5G10940.1; -.
DR PaxDb; Q94BQ3; -.
DR PRIDE; Q94BQ3; -.
DR EnsemblPlants; AT5G10940.1; AT5G10940.1; AT5G10940. [Q94BQ3-1]
DR EnsemblPlants; AT5G10940.2; AT5G10940.2; AT5G10940. [Q94BQ3-2]
DR GeneID; 830961; -.
DR Gramene; AT5G10940.1; AT5G10940.1; AT5G10940. [Q94BQ3-1]
DR Gramene; AT5G10940.2; AT5G10940.2; AT5G10940. [Q94BQ3-2]
DR KEGG; ath:AT5G10940; -.
DR Araport; AT5G10940; -.
DR TAIR; locus:2183735; AT5G10940.
DR eggNOG; KOG1310; Eukaryota.
DR HOGENOM; CLU_012381_3_0_1; -.
DR InParanoid; Q94BQ3; -.
DR OMA; HWQRQQY; -.
DR OrthoDB; 1270484at2759; -.
DR PhylomeDB; Q94BQ3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94BQ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BQ3; baseline and differential.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:UniProtKB.
DR GO; GO:1901000; P:regulation of response to salt stress; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR045151; DCAF8.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15574; PTHR15574; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Coiled coil;
KW Cytoplasm; Lipoprotein; Nucleus; Prenylation; Reference proteome; Repeat;
KW TPR repeat; WD repeat.
FT CHAIN 1..757
FT /note="Protein ALTERED SEED GERMINATION 2"
FT /id="PRO_0000450280"
FT REPEAT 6..43
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 48..87
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 91..132
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 145..185
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 213..253
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 277..316
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 442..475
FT /note="TPR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 618..658
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 661..700
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REGION 519..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 245..257
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768,
FT ECO:0000269|PubMed:26147561"
FT COMPBIAS 581..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 754
FT /note="S-12-hydroxyfarnesyl cysteine; by FTB/ERA1"
FT /evidence="ECO:0000269|PubMed:26147561"
FT VAR_SEQ 312..314
FT /note="Missing (in isoform 2)"
FT /id="VSP_060594"
FT MUTAGEN 245..257
FT /note="Missing: Impaired nuclear localization."
FT /evidence="ECO:0000269|PubMed:26147561"
FT MUTAGEN 754
FT /note="C->S: Impaired farnesylation leading to a
FT constitutive localizes in both cytosol and nucleus, as well
FT as reduced interaction with HDA9."
FT /evidence="ECO:0000269|PubMed:26147561,
FT ECO:0000269|PubMed:28663238"
SQ SEQUENCE 757 AA; 83830 MW; 12BE45AAC114056D CRC64;
MDNLSFHDGN IFNLLHTRSQ DPSHEVDQRM QFHSSLVRRL SQEQELEGHQ GCVNALAWNS
NGSLLISGSD DLRINIWNYS SRKLLHSIDT GHTANIFCTK FVPETSDELV VSGAGDAEVR
LFNTSRLSGR AEDDNAIIPS ALYQCHTRRV KKLAVEPGNP NVVWSASEDG TLRQHDFRES
TSCPPAGTAH QECRSVLLDL RSGAKRALAD PPKQTLSLKS CDISATRPHL LLVGGSDAFA
RLYDRRMLPP LASSRKRMPP PPCVNYFCPM HLSERGRTNL HLTHVTFSPN GEEVLLSYSG
EHVYLMNVNN GICSTGIMQY TPGDVDNLFS FSNNLHDVES PPQVSTTPQN GFHRSSNAAT
VKKCTELVEI AKWSLEEGTD VFYAIEAANE VLDAHSNDIE SALRHECLCT RAALLLKRKW
KNDAHMAVRD CHNARRIDAS SFKAHYYMSE ALQQLGKCKE ALDFATAAQH MNPSDADIVA
KVESIKRDLQ AAGAEKNEET GAGTTRVLSL SDILYRSEAN SDSSHDMSRS EREDSDYDEE
LELDIQTSLS DDEGRDTDSN SMRGSLNLRI HRVGDDKPME NTVDNASSGT ASSSQNDRTS
YQPEGAIDMK RRYVGHCNVG TDIKQASFLG QRGEYIASGS DDGRWFIWEK QTGRLMKVLV
GDESVLNCIQ CHPFDSVVAT SGIDNTIKIW SPTASVPSIV AGGSAGPATA NVVEVMESNQ
QKLSRNRENP LSVELMQRFR MQEFAEGNFH PFECTQS
