ID   SUMO3_XENLA             Reviewed;          94 AA.
AC   Q7SZ22;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Small ubiquitin-related modifier 3;
DE            Short=SUMO-3;
DE   Flags: Precursor;
GN   Name=sumo3;
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].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitin-like protein which can be covalently attached to
CC       target lysines either as a monomer or as a lysine-linked polymer. Does
CC       not seem to be involved in protein degradation and may function as an
CC       antagonist of ubiquitin in the degradation process. Plays a role in a
CC       number of cellular processes such as nuclear transport, DNA replication
CC       and repair, mitosis and signal transduction. Covalent attachment to its
CC       substrates requires prior activation by the E1 complex sae1-sae2 and
CC       linkage to the E2 enzyme ube2i (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with sae2 and ube2i. Covalently attached to a number
CC       of proteins (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, PML body
CC       {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; BC054172; AAH54172.1; -; mRNA.
DR   RefSeq; NP_001079759.1; NM_001086290.1.
DR   AlphaFoldDB; Q7SZ22; -.
DR   SMR; Q7SZ22; -.
DR   DNASU; 379449; -.
DR   GeneID; 379449; -.
DR   KEGG; xla:379449; -.
DR   CTD; 379449; -.
DR   Xenbase; XB-GENE-1004218; sumo3.L.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016605; C:PML body; 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   Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..92
FT                   /note="Small ubiquitin-related modifier 3"
FT                   /id="PRO_0000267634"
FT   PROPEP          93..94
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000267635"
FT   DOMAIN          15..92
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        92
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   94 AA;  10713 MW;  B315887FB123B46F CRC64;
     MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCDRQ GLSMRQIRFR
     FDGQPINETD TPAQLEMEDE DTIDVFQQQT GGVC