SUMO2_ARATH
ID SUMO2_ARATH Reviewed; 103 AA.
AC Q9FLP6; Q67ZL9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Small ubiquitin-related modifier 2;
DE Short=AtSUMO2;
GN Name=SUMO2; Synonyms=SUM2; OrderedLocusNames=At5g55160; ORFNames=MCO15.11;
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 [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=12482876; DOI=10.1074/jbc.m209694200;
RA Kurepa J., Walker J.M., Smalle J., Gosink M.M., Davis S.J., Durham T.L.,
RA Sung D.Y., Vierstra R.D.;
RT "The small ubiquitin-like modifier (SUMO) protein modification system in
RT Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by
RT stress.";
RL J. Biol. Chem. 278:6862-6872(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-103.
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=17041025; DOI=10.1104/pp.106.088831;
RA Yoo C.Y., Miura K., Jin J.B., Lee J., Park H.C., Salt D.E., Yun D.J.,
RA Bressan R.A., Hasegawa P.M.;
RT "SIZ1 small ubiquitin-like modifier E3 ligase facilitates basal
RT thermotolerance in Arabidopsis independent of salicylic acid.";
RL Plant Physiol. 142:1548-1558(2006).
RN [8]
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).
CC -!- FUNCTION: Ubiquitin-like protein which can be covalently attached to
CC target lysines as a monomer. Does not seem to be involved in protein
CC degradation and may function as an antagonist of ubiquitin in the
CC degradation process. Required for the massive protein sumoylation in
CC the nucleus induced by heat shock and controlled by SIZ1.
CC {ECO:0000269|PubMed:17041025, ECO:0000269|PubMed:17644626}.
CC -!- SUBUNIT: Interacts with SAE2, SCE1, SIZ1 and MMS21 (By similarity).
CC Interacts with HSFA2. Covalently attached to ABI5, FLD, GTE3, HSFA2 and
CC ICE1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12482876}. Cytoplasm
CC {ECO:0000269|PubMed:12482876}.
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=Q9FLP6-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17644626}.
CC -!- MISCELLANEOUS: Stress conditions rapidly and substantially elevates the
CC amount of SUMO1 and SUMO2 conjugates with a concomitant reduction in
CC the amount of free SUMO proteins. The SUMO conjugation system plays an
CC important function in stress protection and/or repair.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
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DR EMBL; AF510520; AAN03846.1; -; mRNA.
DR EMBL; AB010071; BAB08585.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96593.1; -; Genomic_DNA.
DR EMBL; AY075614; AAL91628.1; -; mRNA.
DR EMBL; AY113019; AAM47327.1; -; mRNA.
DR EMBL; AY085191; AAM61742.1; -; mRNA.
DR EMBL; AK176098; BAD43861.1; -; mRNA.
DR RefSeq; NP_200327.1; NM_124898.4. [Q9FLP6-1]
DR AlphaFoldDB; Q9FLP6; -.
DR SMR; Q9FLP6; -.
DR BioGRID; 20853; 16.
DR PRIDE; Q9FLP6; -.
DR ProteomicsDB; 228288; -. [Q9FLP6-1]
DR EnsemblPlants; AT5G55160.1; AT5G55160.1; AT5G55160. [Q9FLP6-1]
DR GeneID; 835609; -.
DR Gramene; AT5G55160.1; AT5G55160.1; AT5G55160. [Q9FLP6-1]
DR KEGG; ath:AT5G55160; -.
DR Araport; AT5G55160; -.
DR HOGENOM; CLU_148322_4_0_1; -.
DR InParanoid; Q9FLP6; -.
DR OMA; AYCDRVG; -.
DR PhylomeDB; Q9FLP6; -.
DR PRO; PR:Q9FLP6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLP6; baseline and differential.
DR Genevisible; Q9FLP6; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..103
FT /note="Small ubiquitin-related modifier 2"
FT /id="PRO_0000397033"
FT DOMAIN 15..92
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
SQ SEQUENCE 103 AA; 11654 MW; E8F9C486588FF342 CRC64;
MSATPEEDKK PDQGAHINLK VKGQDGNEVF FRIKRSTQLK KLMNAYCDRQ SVDFNSIAFL
FDGRRLRAEQ TPDELEMEDG DEIDAMLHQT GGGAKNGLKL FCF
