ID   SMO2A_XENLA             Reviewed;          95 AA.
AC   Q7ZTK7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Small ubiquitin-related modifier 2-A;
DE            Short=SUMO-2-A;
DE   Flags: Precursor;
GN   Name=sumo2-a; Synonyms=smt3h2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=14597774; DOI=10.1083/jcb.200304088;
RA   Azuma Y., Arnaoutov A., Dasso M.;
RT   "SUMO-2/3 regulates topoisomerase II in mitosis.";
RL   J. Cell Biol. 163:477-487(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=15933717; DOI=10.1038/sj.emboj.7600700;
RA   Azuma Y., Arnaoutov A., Anan T., Dasso M.;
RT   "PIASy mediates SUMO-2 conjugation of Topoisomerase-II on mitotic
RT   chromosomes.";
RL   EMBO J. 24:2172-2182(2005).
CC   -!- FUNCTION: Ubiquitin-like protein that can be covalently attached to
CC       proteins as a monomer or as a lysine-linked polymer. Covalent
CC       attachment via an isopeptide bond to its substrates requires prior
CC       activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme
CC       ube2i, and can be promoted by an E3 ligase such as pias1-4. This post-
CC       translational modification on lysine residues of proteins plays a
CC       crucial role in a number of cellular processes such as nuclear
CC       transport, DNA replication and repair, mitosis and signal transduction.
CC       Polymeric sumo2 chains are also susceptible to polyubiquitination which
CC       functions as a signal for proteasomal degradation of modified proteins.
CC       {ECO:0000269|PubMed:14597774, ECO:0000269|PubMed:15933717}.
CC   -!- SUBUNIT: Interacts with sae2 and ube2i. Covalently attached to a number
CC       of proteins, including top2.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Polymeric chains can be formed through Lys-11 cross-linking.
CC       {ECO:0000250}.
CC   -!- PTM: Cleavage of precursor form by a sentrin-specific protease is
CC       necessary for function. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC045271; AAH45271.1; -; mRNA.
DR   EMBL; BC106623; AAI06624.1; -; mRNA.
DR   RefSeq; NP_001080085.1; NM_001086616.1.
DR   AlphaFoldDB; Q7ZTK7; -.
DR   SMR; Q7ZTK7; -.
DR   DNASU; 379777; -.
DR   GeneID; 379777; -.
DR   KEGG; xla:379777; -.
DR   CTD; 379777; -.
DR   Xenbase; XB-GENE-6254945; sumo2.L.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 379777; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..93
FT                   /note="Small ubiquitin-related modifier 2-A"
FT                   /id="PRO_0000269471"
FT   PROPEP          94..95
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000269472"
FT   DOMAIN          16..95
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        93
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   95 AA;  10820 MW;  EBCD9B7058A6F99A CRC64;
     MADDKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRQTPL SKLMKAYCER QGLSMRQIRF
     RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGSF