ID   SMO1A_XENLA             Reviewed;         102 AA.
AC   O57686;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Small ubiquitin-related modifier 1-A;
DE            Short=SUMO-1-A;
DE   Flags: Precursor;
GN   Name=sumo1-a;
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 [MRNA], AND FUNCTION.
RX   PubMed=9427648; DOI=10.1016/s0960-9822(98)70044-2;
RA   Saitoh H., Sparrow D.B., Shiomi T., Pu R.T., Nishimoto T., Mohun T.J.,
RA   Dasso M.;
RT   "Ubc9p and the conjugation of SUMO-1 to RanGAP1 and RanBP2.";
RL   Curr. Biol. 8:121-124(1998).
RN   [2]
RP   INTERACTION WITH SOX9 AND SOX10.
RX   PubMed=16256735; DOI=10.1016/j.devcel.2005.09.016;
RA   Taylor K.M., Labonne C.;
RT   "SoxE factors function equivalently during neural crest and inner ear
RT   development and their activity is regulated by SUMOylation.";
RL   Dev. Cell 9:593-603(2005).
CC   -!- FUNCTION: Ubiquitin-like protein that can be covalently attached to
CC       proteins as a monomer or a lysine-linked polymer (PubMed:9427648).
CC       Covalent attachment via an isopeptide bond to its substrates requires
CC       prior activation by the E1 complex sae1-sae2 and linkage to the E2
CC       enzyme ube2i. This post-translational modification on lysine residues
CC       of proteins plays a crucial role in a number of cellular processes such
CC       as nuclear transport, DNA replication and repair, mitosis and signal
CC       transduction. Polymeric sumo1 chains are also susceptible to
CC       polyubiquitination which functions as a signal for proteasomal
CC       degradation of modified proteins (By similarity).
CC       {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:9427648}.
CC   -!- SUBUNIT: Interacts with sae2, ube2i, ranbp2, pias1 and pias2 (By
CC       similarity). Covalently attached to a number of proteins including
CC       rangap1 and ranbp2 (By similarity). Interacts with sox9 and sox10
CC       (PubMed:16256735). {ECO:0000250|UniProtKB:P63165,
CC       ECO:0000269|PubMed:16256735}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P63165}.
CC       Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body
CC       {ECO:0000250|UniProtKB:P63165}. Cell membrane
CC       {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}.
CC   -!- PTM: Cleavage of precursor form by a sentrin-specific protease is
CC       necessary for function. {ECO:0000250|UniProtKB:P63165}.
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; Z97073; CAB09807.1; -; mRNA.
DR   RefSeq; NP_001083717.1; NM_001090248.1.
DR   AlphaFoldDB; O57686; -.
DR   SMR; O57686; -.
DR   GeneID; 399078; -.
DR   KEGG; xla:399078; -.
DR   CTD; 399078; -.
DR   Xenbase; XB-GENE-6254630; sumo1.L.
DR   OrthoDB; 1583700at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 399078; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
DR   GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR   GO; GO:0016925; P:protein sumoylation; ISS:AgBase.
DR   CDD; cd16114; Ubl_SUMO1; 1.
DR   InterPro; IPR022617; Rad60/SUMO-like_dom.
DR   InterPro; IPR046332; SUMO1_Ubl.
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   Cell membrane; Cytoplasm; Isopeptide bond; Membrane; Nucleus;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..98
FT                   /note="Small ubiquitin-related modifier 1-A"
FT                   /id="PRO_0000267618"
FT   PROPEP          99..102
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000267619"
FT   DOMAIN          21..98
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        98
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   102 AA;  11703 MW;  621F0289FA306E26 CRC64;
     MSDQEAKPSS EDLGDKKDGG DYIKLKVIGQ DSSEIHFKVK MTTHLKKLKE SYRQRQGVPM
     NSLRFLFEGQ RISDHQTPKE LGMEEEDVIE VYQEQTGGHS TF