ID   SUMO5_ARATH             Reviewed;         108 AA.
AC   Q8VZI7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Small ubiquitin-related modifier 5;
DE            Short=AtSUMO5;
GN   Name=SUMO5; Synonyms=SUM5; OrderedLocusNames=At2g32765; ORFNames=F24L7.10;
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].
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SAE2, SCE1, SIZ1 and MMS21 Covalently attached
CC       to a number of proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
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}.
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; AF510522; AAN03848.1; -; mRNA.
DR   EMBL; AC003974; AAM14900.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08735.1; -; Genomic_DNA.
DR   EMBL; AY064140; AAL36047.1; -; mRNA.
DR   EMBL; AY097408; AAM19924.1; -; mRNA.
DR   EMBL; AY087010; AAM64571.1; -; mRNA.
DR   RefSeq; NP_565752.1; NM_128836.4.
DR   AlphaFoldDB; Q8VZI7; -.
DR   SMR; Q8VZI7; -.
DR   STRING; 3702.AT2G32765.1; -.
DR   iPTMnet; Q8VZI7; -.
DR   PaxDb; Q8VZI7; -.
DR   PRIDE; Q8VZI7; -.
DR   ProteomicsDB; 228284; -.
DR   EnsemblPlants; AT2G32765.1; AT2G32765.1; AT2G32765.
DR   GeneID; 817837; -.
DR   Gramene; AT2G32765.1; AT2G32765.1; AT2G32765.
DR   KEGG; ath:AT2G32765; -.
DR   Araport; AT2G32765; -.
DR   TAIR; locus:505006284; AT2G32765.
DR   eggNOG; KOG1769; Eukaryota.
DR   HOGENOM; CLU_148322_4_1_1; -.
DR   InParanoid; Q8VZI7; -.
DR   OMA; VFICESG; -.
DR   OrthoDB; 1583700at2759; -.
DR   PhylomeDB; Q8VZI7; -.
DR   PRO; PR:Q8VZI7; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8VZI7; baseline and differential.
DR   Genevisible; Q8VZI7; 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; IDA:TAIR.
DR   GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR   GO; GO:0016925; P:protein sumoylation; IDA:TAIR.
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   Cytoplasm; Isopeptide bond; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..108
FT                   /note="Small ubiquitin-related modifier 5"
FT                   /id="PRO_0000397036"
FT   DOMAIN          26..103
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        103
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
SQ   SEQUENCE   108 AA;  12098 MW;  2D557A7DD9C5CE96 CRC64;
     MVSSTDTISA SFVSKKSRSP ETSPHMKVTL KVKNQQGAED LYKIGTHAHL KKLMSAYCTK
     RNLDYSSVRF VYNGREIKAR QTPAQLHMEE EDEICMVMEL GGGGPYTP