ID SUMO3_CHICK Reviewed; 94 AA.
AC Q5ZHQ1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Small ubiquitin-related modifier 3 {ECO:0000305};
DE Short=SUMO-3 {ECO:0000305};
DE Flags: Precursor;
GN Name=SUMO3 {ECO:0000305};
GN ORFNames=RCJMB04_34j10 {ECO:0000312|EMBL:CAG32742.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ721083; CAG32742.1; -; mRNA.
DR RefSeq; NP_001072966.1; NM_001079498.1.
DR AlphaFoldDB; Q5ZHQ1; -.
DR BMRB; Q5ZHQ1; -.
DR SMR; Q5ZHQ1; -.
DR STRING; 9031.ENSGALP00000047262; -.
DR PaxDb; 9031-ENSGALP00000033053; -.
DR Ensembl; ENSGALT00000080195; ENSGALP00000047262; ENSGALG00000032783.
DR Ensembl; ENSGALT00010062275.1; ENSGALP00010038495.1; ENSGALG00010025522.1.
DR Ensembl; ENSGALT00015051426; ENSGALP00015029735; ENSGALG00015021099.
DR GeneID; 770553; -.
DR KEGG; gga:770553; -.
DR CTD; 6612; -.
DR VEuPathDB; HostDB:geneid_770553; -.
DR eggNOG; KOG1769; Eukaryota.
DR GeneTree; ENSGT00950000182895; -.
DR HOGENOM; CLU_148322_2_1_1; -.
DR InParanoid; Q5ZHQ1; -.
DR OMA; QFRIKRH; -.
DR OrthoDB; 5132985at2759; -.
DR PhylomeDB; Q5ZHQ1; -.
DR TreeFam; TF315116; -.
DR Reactome; R-GGA-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-GGA-3065679; SUMO is proteolytically processed.
DR Reactome; R-GGA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-GGA-3232118; SUMOylation of transcription factors.
DR Reactome; R-GGA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-GGA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-GGA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-GGA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-GGA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-GGA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-GGA-5696395; Formation of Incision Complex in GG-NER.
DR PRO; PR:Q5ZHQ1; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000032783; Expressed in ovary and 13 other cell types or tissues.
DR ExpressionAtlas; Q5ZHQ1; baseline and differential.
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 activity; IBA:GO_Central.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IEA:Ensembl.
DR CDD; cd16115; Ubl_SUMO2_3_4; 1.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10562; SMALL UBIQUITIN-RELATED MODIFIER; 1.
DR PANTHER; PTHR10562:SF135; SMALL UBIQUITIN-RELATED MODIFIER 3; 1.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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_0000267628"
FT PROPEP 93..94
FT /evidence="ECO:0000250"
FT /id="PRO_0000267629"
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; 10711 MW; D878493AB123B53E CRC64;
MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR
FDGQPINEAD TPAQLEMEDE DTIDVFQQQT GGLC
//
