ID A0A3Q0CT57_MESAU Unreviewed; 418 AA.
AC A0A3Q0CT57;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=E3 SUMO-protein ligase EGR2 {ECO:0000256|ARBA:ARBA00040715};
DE AltName: Full=E3 SUMO-protein transferase ERG2 {ECO:0000256|ARBA:ARBA00042877};
DE AltName: Full=Early growth response protein 2 {ECO:0000256|ARBA:ARBA00042200};
GN Name=Egr2 {ECO:0000313|RefSeq:XP_021083259.1,
GN ECO:0000313|RefSeq:XP_021083260.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021083259.1};
RN [1] {ECO:0000313|RefSeq:XP_021083259.1, ECO:0000313|RefSeq:XP_021083260.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its
CC coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2
CC transcriptional activity. {ECO:0000256|ARBA:ARBA00037627}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU363046}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000256|ARBA:ARBA00005682, ECO:0000256|RuleBase:RU363046}.
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DR RefSeq; XP_021083259.1; XM_021227600.1.
DR RefSeq; XP_021083260.1; XM_021227601.1.
DR KEGG; maua:101834268; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR InterPro; IPR021849; EGR_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF54; E3 SUMO-PROTEIN LIGASE EGR2; 1.
DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1.
DR Pfam; PF11928; DUF3446; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU363046};
KW Ligase {ECO:0000313|RefSeq:XP_021083259.1,
KW ECO:0000313|RefSeq:XP_021083260.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363046};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363046};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363046};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU363046};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU363046};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 286..315
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 316..343
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 344..371
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 76..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 44527 MW; 9C5EDDDC5B0FBAA6 CRC64;
MNGVAGDGMI NIDMTGEKRP LDLPYPSSFA PISAPRNQTF TYMGKFSIDP QYPGASCYPE
GIINIVSAGI LQGVTPPAST TASSSVTSAS PNPLATGPLG VCTMSQTQPE LDHLYSPPPP
PPPYSGCTGD LYQDPSAFLS PPTTSTSSLA YQPPPSYPSP KPAMDPGLIP MIPDYPGFFP
PPCQRDPHGA AGPDRKPFPC PLDSLRVPPP LTPLSTIRNF TLGGPSAGVT GPGASGGSEG
PRLPGSGSAA VTPTPYNPHH LPLRPILRPR KYPNRPSKTP VHERPYPCPA EGCDRRFSRS
DELTRHIRIH TGHKPFQCRI CMRNFSRSDH LTTHIRTHTG EKPFACDYCG RKFARSDERK
RHTKIHLRQK ERKSSAPSSS APAQPSASGP GGSQAGGSLC TTTTIGGPLT CTSRTRTP
//