SUD1_ARATH
ID SUD1_ARATH Reviewed; 1108 AA.
AC F4JKK0; F4JKK1; O49494; Q0WLP2;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Probable E3 ubiquitin ligase SUD1;
DE EC=2.3.2.27;
DE AltName: Full=Protein ECERIFERUM 9;
DE AltName: Full=Protein SUPPRESSOR OF DRY2 DEFFECTS 1;
DE Short=AtSUD1;
DE AltName: Full=RING-type E3 ubiquitin transferase SUD1 {ECO:0000305};
DE AltName: Full=RING/U-box domain-containing protein;
GN Name=SUD1; Synonyms=CER9; OrderedLocusNames=At4g34100; ORFNames=F28A23.140;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] OF 327-1108 (ISOFORM 1).
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 [4]
RP FUNCTION, MUTAGENESIS OF CYS-114, DISRUPTION PHENOTYPE, DEVELOPMENTAL
RP STAGE, AND TISSUE SPECIFICITY.
RX PubMed=22635115; DOI=10.1104/pp.112.198697;
RA Lue S., Zhao H., Des Marais D.L., Parsons E.P., Wen X., Xu X.,
RA Bangarusamy D.K., Wang G., Rowland O., Juenger T., Bressan R.A.,
RA Jenks M.A.;
RT "Arabidopsis ECERIFERUM9 involvement in cuticle formation and maintenance
RT of plant water status.";
RL Plant Physiol. 159:930-944(2012).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-218; ARG-244 AND GLY-360.
RX PubMed=23404890; DOI=10.1105/tpc.112.108696;
RA Doblas V.G., Amorim-Silva V., Pose D., Rosado A., Esteban A., Arro M.,
RA Azevedo H., Bombarely A., Borsani O., Valpuesta V., Ferrer A.,
RA Tavares R.M., Botella M.A.;
RT "The SUD1 gene encodes a putative E3 ubiquitin ligase and is a positive
RT regulator of 3-hydroxy-3-methylglutaryl coenzyme a reductase activity in
RT Arabidopsis.";
RL Plant Cell 25:728-743(2013).
CC -!- FUNCTION: Probable E3 ubiquitin ligase acting as a positive post-
CC transcriptional regulator of 3-hydroxy-3-methylglutaryl-coenzyme A
CC reductase activity. Might be involved in the quality control that
CC degrades misfolded proteins (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:22635115, ECO:0000269|PubMed:23404890}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JKK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JKK0-2; Sequence=VSP_046615;
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves, roots, stems,
CC inflorescences and siliques. Expression higher at the top than at the
CC base of the stem. {ECO:0000269|PubMed:22635115}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed throughout development.
CC {ECO:0000269|PubMed:22635115}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
CC -!- DISRUPTION PHENOTYPE: Semiglossy stem. Elevated drought tolerance and
CC reduced transpiration rate. Elevated amounts of 18-carbon-length cutin
CC monomers and shift in the cuticular wax profile toward the very-long-
CC chain free fatty acids tetracosanoic acid (C24) and hexacosanoic acid
CC (C26). {ECO:0000269|PubMed:22635115}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17562.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80127.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021961; CAA17562.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80127.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86323.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86324.1; -; Genomic_DNA.
DR EMBL; AK230154; BAF01965.1; -; mRNA.
DR PIR; T05426; T05426.
DR RefSeq; NP_001119113.1; NM_001125641.1. [F4JKK0-2]
DR RefSeq; NP_195136.3; NM_119571.5. [F4JKK0-1]
DR AlphaFoldDB; F4JKK0; -.
DR SMR; F4JKK0; -.
DR BioGRID; 14838; 1.
DR IntAct; F4JKK0; 1.
DR STRING; 3702.AT4G34100.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR SwissPalm; F4JKK0; -.
DR PaxDb; F4JKK0; -.
DR PRIDE; F4JKK0; -.
DR ProteomicsDB; 228398; -. [F4JKK0-1]
DR EnsemblPlants; AT4G34100.1; AT4G34100.1; AT4G34100. [F4JKK0-1]
DR EnsemblPlants; AT4G34100.2; AT4G34100.2; AT4G34100. [F4JKK0-2]
DR GeneID; 829556; -.
DR Gramene; AT4G34100.1; AT4G34100.1; AT4G34100. [F4JKK0-1]
DR Gramene; AT4G34100.2; AT4G34100.2; AT4G34100. [F4JKK0-2]
DR KEGG; ath:AT4G34100; -.
DR Araport; AT4G34100; -.
DR TAIR; locus:2124251; AT4G34100.
DR eggNOG; KOG1609; Eukaryota.
DR InParanoid; F4JKK0; -.
DR OMA; WLPIRIL; -.
DR OrthoDB; 170933at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:F4JKK0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JKK0; baseline and differential.
DR Genevisible; F4JKK0; AT.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042335; P:cuticle development; IMP:CACAO.
DR GO; GO:0010143; P:cutin biosynthetic process; IMP:TAIR.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IMP:TAIR.
DR GO; GO:1900486; P:positive regulation of isopentenyl diphosphate biosynthetic process, mevalonate pathway; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IGI:TAIR.
DR GO; GO:0010345; P:suberin biosynthetic process; IMP:TAIR.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR GO; GO:0010025; P:wax biosynthetic process; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1108
FT /note="Probable E3 ubiquitin ligase SUD1"
FT /id="PRO_0000422766"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 894..914
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 982..1002
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1017..1036
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 60..121
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 286..308
FT /evidence="ECO:0000255"
FT COMPBIAS 10..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT VAR_SEQ 788..789
FT /note="DR -> E (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046615"
FT MUTAGEN 114
FT /note="C->Y: In cer9-1; Semiglossy shoots."
FT /evidence="ECO:0000269|PubMed:22635115"
FT MUTAGEN 218
FT /note="G->R: In sud1-1; No visible phenotype except glossy
FT shoots, but is able to suppress the dry2 phenotype."
FT /evidence="ECO:0000269|PubMed:23404890"
FT MUTAGEN 244
FT /note="R->K: In sud1-3; Able to suppress the dry2
FT phenotype."
FT /evidence="ECO:0000269|PubMed:23404890"
FT MUTAGEN 360
FT /note="G->E: In sud1-2; Able to suppress the dry2
FT phenotype."
FT /evidence="ECO:0000269|PubMed:23404890"
FT CONFLICT 816
FT /note="V -> D (in Ref. 3; BAF01965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1108 AA; 123004 MW; 70273F274F89DAEE CRC64;
MEISPADSLS ISGAAASEVV SEPSVSSSSS SSSPNQASPN PFSNMDPAVS TATGSRYVDD
DEDEEDVCRI CRNPGDADNP LRYPCACSGS IKFVHQDCLL QWLNHSNARQ CEVCKHPFSF
SPVYADNAPS RLPFQEFVVG IAMKACHVLQ FFLRLSFVLS VWLLTIPFIT FWIWRLAFVR
TFGEAQRLFL SHISTTVILT DCLHGFLLSA SIVFIFLGAT SLRDYFRHLR ELGGQEERDD
DVDRNGARAA RRPAGQANRN LAGEGNGEDA GDQGAAVGQI ARRNPENVLA RLDIQAARLE
AQVEQMFDGL DDADGAEDVP FDELVGMQGP VFHLVENAFT VLASNMIFLG VVIFVPFTLG
RIILYHVSWL FAAARGPAVA ASLHLTDTGL SLENITLKSA LTAVSNLTSE GQGNGLLGQL
TEMMKVNGSE LNGANNTLSV ATDLLKGSTV GASKLSDITT LAVGYMFIVF LVFLYLGIIA
LIRYAKGEPL TVGRFYGIAS IVEAVPSLLR QFLAAMRHLM TMIKVAFLLV IELGVFPLMC
GWWLDVCTVR MFGKTMSHRV QFLSISPLAS SLVHWVVGIM YMLQISIFVS LLRGVLRPGV
LYFLRDPADP NYNPFRDLID DPVHKHARRV LLSVAVYGSL IVMLVFLPVK LAIRMAPSIF
PLDISVSDPF TEIPADMLLF QICIPFIIEH FRLRTTIKSL LRCWFTGVGW ALGLTDFLLP
RPEDNIGQDN GNGEPGRQNR AQVLQVGGPD RAMAALPVAD DPNRSRLRAG NVNTGEEYED
DDEQSDSDRY NFVVRIILLL LVAWVTLLLF NSALIVVPVS LGRALFSAIP ILPITHGIKC
NDLYAFVIGT YAFWTTISGA RYAIEHVKSK RTSVLLNQIW KWCGIVFKSS VLLAIWVFII
PVLIGLLFEL LVIVPMRVPV DESPVFLLYQ DWALGLIFLK IWTRLVMLDH MLPIVDDSWR
AKFERVREDG FSRLQGLWVL REIVFPIVMK LLTALCVPYV LARGVFPMLG YPLVVNSAVY
RFAWIGCLSV SLFCFCAKRC HVWFRNLHNS IRDDRYLIGR RLHNFGEAAL ANQNQNQSSE
DAGDGVLIGR EGDVDNGLRL RRAIQQEA
