ID   SUMO4_PIG               Reviewed;          95 AA.
AC   A7WLI0;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Small ubiquitin-related modifier 4;
DE            Short=SUMO-4;
DE   Flags: Precursor;
GN   Name=SUMO4;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chun T., Lee J.Y.;
RT   "Molecular cloning and expression analysis of porcine SUMO genes.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitin-like protein which can be covalently attached to
CC       target lysines as a monomer. Does not seem to be involved in protein
CC       degradation and may modulate protein subcellular localization,
CC       stability or activity. Upon oxidative stress, conjugates to various
CC       anti-oxidant enzymes, chaperones, and stress defense proteins. May also
CC       conjugate to NFKBIA, TFAP2A and FOS, negatively regulating their
CC       transcriptional activity, and to NR3C1, positively regulating its
CC       transcriptional activity. Covalent attachment to its substrates
CC       requires prior activation by the E1 complex SAE1-SAE2 and linkage to
CC       the E2 enzyme UBE2I (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SAE2. Covalently attached to a number of
CC       proteins (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AM397627; CAL37098.1; -; mRNA.
DR   RefSeq; NP_001106147.1; NM_001112677.1.
DR   AlphaFoldDB; A7WLI0; -.
DR   SMR; A7WLI0; -.
DR   PeptideAtlas; A7WLI0; -.
DR   GeneID; 100127140; -.
DR   KEGG; ssc:100127140; -.
DR   CTD; 387082; -.
DR   InParanoid; A7WLI0; -.
DR   OrthoDB; 1583700at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0016925; P:protein sumoylation; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Isopeptide bond; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..93
FT                   /note="Small ubiquitin-related modifier 4"
FT                   /id="PRO_0000311797"
FT   PROPEP          94..95
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000311798"
FT   DOMAIN          17..95
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        93
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
SQ   SEQUENCE   95 AA;  10775 MW;  EEE3FFF74FA8E092 CRC64;
     MADEKPKEGV KTENNDHINL KVAGQDGSVA QFKIRRHTPL SKLMKAYCER QGLSIRQIRF
     RVDGQPINET HTPAQLELED EDTIDVLQQQ TGGVY