SCE1_ARATH
ID SCE1_ARATH Reviewed; 160 AA.
AC Q42551; Q0WMG8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=SUMO-conjugating enzyme SCE1;
DE EC=2.3.2.-;
DE AltName: Full=Protein EMBRYO DEFECTIVE 1637;
DE AltName: Full=Protein hus5 homolog;
DE AltName: Full=SUMO-conjugating enzyme 1;
DE Short=AtSCE1;
GN Name=SCE1; Synonyms=AHUS5, EMB1637; OrderedLocusNames=At3g57870;
GN ORFNames=T10K17.80;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RA Winge P., Kristensen R., Bones A.M.;
RT "Arabidopsis thaliana ubiquitin-conjugating like enzyme.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-160.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17644626; DOI=10.1104/pp.107.102285;
RA Saracco S.A., Miller M.J., Kurepa J., Vierstra R.D.;
RT "Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and
RT SUMO2 to nuclear proteins is essential.";
RL Plant Physiol. 145:119-134(2007).
RN [7]
RP FUNCTION, INTERACTION WITH SIZ1, AND MUTAGENESIS OF CYS-94.
RX PubMed=18502747; DOI=10.1074/jbc.m708176200;
RA Garcia-Dominguez M., March-Diaz R., Reyes J.C.;
RT "The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain
RT GTE proteins.";
RL J. Biol. Chem. 283:21469-21477(2008).
RN [8]
RP FUNCTION, AND INTERACTION WITH MMS21.
RX PubMed=19682286; DOI=10.1111/j.1365-313x.2009.03992.x;
RA Huang L., Yang S., Zhang S., Liu M., Lai J., Qi Y., Shi S., Wang J.,
RA Wang Y., Xie Q., Yang C.;
RT "The Arabidopsis SUMO E3 ligase AtMMS21, a homologue of NSE2/MMS21,
RT regulates cell proliferation in the root.";
RL Plant J. 60:666-678(2009).
RN [9]
RP INTERACTION WITH KIN10.
RX PubMed=20855607; DOI=10.1073/pnas.1005452107;
RA Elrouby N., Coupland G.;
RT "Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates
RT identify Arabidopsis proteins implicated in diverse biological processes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17415-17420(2010).
RN [10]
RP INTERACTION WITH KIN10.
RX PubMed=26662259; DOI=10.1111/tpj.13096;
RA Crozet P., Margalha L., Butowt R., Fernandes N., Elias C.A., Orosa B.,
RA Tomanov K., Teige M., Bachmair A., Sadanandom A., Baena-Gonzalez E.;
RT "SUMOylation represses SnRK1 signaling in Arabidopsis.";
RL Plant J. 85:120-133(2016).
RN [11]
RP INTERACTION WITH TCP14 AND TCP15.
RX PubMed=29250092; DOI=10.3389/fpls.2017.02043;
RA Mazur M.J., Spears B.J., Djajasaputra A., van der Gragt M., Vlachakis G.,
RA Beerens B., Gassmann W., van den Burg H.A.;
RT "Arabidopsis TCP transcription factors interact with the SUMO conjugating
RT machinery in nuclear foci.";
RL Front. Plant Sci. 8:2043-2043(2017).
CC -!- FUNCTION: SUMO-conjugating enzyme that accepts the SUMO proteins from
CC the E1 SUMO-activating heterodimer SAE1/SAE2 and catalyzes its covalent
CC attachment to other proteins with the E3 SUMO ligases SIZ1 and MMS21.
CC Associates with SIZ1 for sumoylation of the transcription factor GTE3.
CC {ECO:0000269|PubMed:17644626, ECO:0000269|PubMed:18502747,
CC ECO:0000269|PubMed:19682286}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with SIZ1 (via PHD domain) and MMS21
CC (PubMed:18502747, PubMed:19682286). Interacts with TCP14 and TCP15
CC (PubMed:29250092). Interacts with KIN10 (PubMed:20855607,
CC PubMed:26662259). {ECO:0000269|PubMed:18502747,
CC ECO:0000269|PubMed:19682286, ECO:0000269|PubMed:20855607,
CC ECO:0000269|PubMed:26662259, ECO:0000269|PubMed:29250092}.
CC -!- INTERACTION:
CC Q42551; O80837: DBP; NbExp=3; IntAct=EBI-4442034, EBI-1788073;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:17644626}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U44976; AAA86642.1; -; mRNA.
DR EMBL; AF091106; AAC64116.1; -; Genomic_DNA.
DR EMBL; AL132977; CAB67615.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79711.1; -; Genomic_DNA.
DR EMBL; AY042838; AAK68778.1; -; mRNA.
DR EMBL; BT003377; AAO30040.1; -; mRNA.
DR EMBL; AK229859; BAF01688.1; -; mRNA.
DR PIR; T46009; T46009.
DR RefSeq; NP_191346.1; NM_115649.3.
DR PDB; 6GUM; X-ray; 1.79 A; A=1-160.
DR PDB; 6GV3; X-ray; 1.20 A; A=1-160.
DR PDBsum; 6GUM; -.
DR PDBsum; 6GV3; -.
DR AlphaFoldDB; Q42551; -.
DR SMR; Q42551; -.
DR BioGRID; 10271; 166.
DR IntAct; Q42551; 6.
DR STRING; 3702.AT3G57870.1; -.
DR PaxDb; Q42551; -.
DR PRIDE; Q42551; -.
DR ProteomicsDB; 226589; -.
DR EnsemblPlants; AT3G57870.1; AT3G57870.1; AT3G57870.
DR GeneID; 824956; -.
DR Gramene; AT3G57870.1; AT3G57870.1; AT3G57870.
DR KEGG; ath:AT3G57870; -.
DR Araport; AT3G57870; -.
DR TAIR; locus:2095838; AT3G57870.
DR eggNOG; KOG0424; Eukaryota.
DR HOGENOM; CLU_030988_12_1_1; -.
DR InParanoid; Q42551; -.
DR OMA; QEPAWRA; -.
DR OrthoDB; 1522509at2759; -.
DR PhylomeDB; Q42551; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:Q42551; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42551; baseline and differential.
DR Genevisible; Q42551; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0032183; F:SUMO binding; IPI:TAIR.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0016925; P:protein sumoylation; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P42747"
FT CHAIN 2..160
FT /note="SUMO-conjugating enzyme SCE1"
FT /id="PRO_0000396013"
FT DOMAIN 5..158
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 94
FT /note="Glycyl thioester intermediate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P42747"
FT MUTAGEN 94
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18502747"
FT CONFLICT 157
FT /note="P -> A (in Ref. 5; BAF01688)"
FT /evidence="ECO:0000305"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:6GV3"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:6GV3"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:6GV3"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:6GV3"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:6GV3"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:6GV3"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6GV3"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6GV3"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6GV3"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:6GV3"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:6GV3"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:6GV3"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:6GV3"
SQ SEQUENCE 160 AA; 17986 MW; 6D9E5C538B09D345 CRC64;
MASGIARGRL AEERKSWRKN HPHGFVAKPE TGQDGTVNLM VWHCTIPGKA GTDWEGGFFP
LTMHFSEDYP SKPPKCKFPQ GFFHPNVYPS GTVCLSILNE DYGWRPAITV KQILVGIQDL
LDTPNPADPA QTDGYHLFCQ DPVEYKKRVK LQSKQYPALV
