ID   SUMO3_BOVIN             Reviewed;         104 AA.
AC   Q17QV3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Small ubiquitin-related modifier 3;
DE            Short=SUMO-3;
DE   Flags: Precursor;
GN   Name=SUMO3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) 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, and can be promoted by an E3 ligase
CC       such as PIAS1-4, RANBP2 or CBX4. Plays a role in the regulation of
CC       sumoylation status of SETX (By similarity).
CC       {ECO:0000250|UniProtKB:P55854}.
CC   -!- SUBUNIT: Interacts with SAE2 and UBE2I. Covalently attached to a number
CC       of proteins. Interacts with USP25 (via ts SIM domain); the interaction
CC       sumoylates USP25 and inhibits its ubiquitin hydrolyzing activity.
CC       Interacts with ARNTL/BMAL1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Nucleus, PML body {ECO:0000250}.
CC   -!- PTM: Polymeric chains can be formed through Lys-11 cross-linking.
CC       {ECO:0000250}.
CC   -!- PTM: Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary
CC       for function. {ECO:0000250}.
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; BC118163; AAI18164.1; -; mRNA.
DR   RefSeq; NP_001069917.1; NM_001076449.1.
DR   AlphaFoldDB; Q17QV3; -.
DR   BMRB; Q17QV3; -.
DR   SMR; Q17QV3; -.
DR   STRING; 9913.ENSBTAP00000023029; -.
DR   PaxDb; Q17QV3; -.
DR   PRIDE; Q17QV3; -.
DR   Ensembl; ENSBTAT00000023029; ENSBTAP00000023029; ENSBTAG00000017321.
DR   GeneID; 617236; -.
DR   KEGG; bta:617236; -.
DR   CTD; 6612; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017321; -.
DR   VGNC; VGNC:56237; SUMO3.
DR   eggNOG; KOG1769; Eukaryota.
DR   GeneTree; ENSGT00950000182895; -.
DR   HOGENOM; CLU_148322_2_1_1; -.
DR   InParanoid; Q17QV3; -.
DR   OMA; MICKEDG; -.
DR   OrthoDB; 1583700at2759; -.
DR   TreeFam; TF315116; -.
DR   Reactome; R-BTA-3065679; SUMO is proteolytically processed.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000017321; Expressed in retina and 104 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR   GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR   GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR   GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR   GO; GO:1900180; P:regulation of protein localization to nucleus; IEA:Ensembl.
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_0000267624"
FT   PROPEP          93..104
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000267625"
FT   DOMAIN          15..92
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        5
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P55854"
FT   CROSSLNK        7
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P55854"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P55854"
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   104 AA;  11669 MW;  AD7F1A6482EF4A21 CRC64;
     MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR
     FDGQPINETD TPAQLEMEDE DTIDVFQQQT GGSRVASCLL GSGL