ID   SUMO1_ONCMY             Reviewed;         101 AA.
AC   Q9PT08;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Small ubiquitin-related modifier 1;
DE            Short=SUMO-1;
DE   Flags: Precursor;
GN   Name=sumo1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Inaba K.;
RT   "Molecular cloning of trout testis small ubiquitin-related modifier-1
RT   (SUMO-1).";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitin-like protein that can be covalently attached to
CC       proteins as a monomer or a lysine-linked polymer. Covalent attachment
CC       via an isopeptide bond to its substrates requires prior activation by
CC       the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. 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 sumo1 chains are also susceptible to polyubiquitination which
CC       functions as a signal for proteasomal degradation of modified proteins.
CC       {ECO:0000250|UniProtKB:P63165}.
CC   -!- SUBUNIT: Interacts with sae2, ube2i, ranbp2, pias1 and pias2 (By
CC       similarity). Covalently attached to a number of proteins (By
CC       similarity). {ECO:0000250|UniProtKB:P63165}.
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}.
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DR   EMBL; AB036430; BAA89293.1; -; mRNA.
DR   RefSeq; NP_001118056.1; NM_001124584.1.
DR   AlphaFoldDB; Q9PT08; -.
DR   SMR; Q9PT08; -.
DR   Ensembl; ENSOMYT00000162347; ENSOMYP00000121727; ENSOMYG00000025363.
DR   GeneID; 100136592; -.
DR   KEGG; omy:100136592; -.
DR   CTD; 100136592; -.
DR   OrthoDB; 1583700at2759; -.
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: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: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   3: Inferred from homology;
KW   Cell membrane; Cytoplasm; Isopeptide bond; Membrane; Nucleus;
KW   Ubl conjugation pathway.
FT   CHAIN           1..97
FT                   /note="Small ubiquitin-related modifier 1"
FT                   /id="PRO_0000267616"
FT   PROPEP          98..101
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000267617"
FT   DOMAIN          20..97
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        97
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   101 AA;  11544 MW;  E9C5709DD7B7FB12 CRC64;
     MSDTDTKPSG QDGGDQKDGE YIKLKVIGQD NSEIHFKVKM TTHLKKLKES YSQRQGVHMS
     TLRFLFEGQR ISDNHTPKEL GMEDEDVIEV YQEQTGGLRN N