GEI17_CAEEL
ID GEI17_CAEEL Reviewed; 780 AA.
AC Q94361; Q564X2; Q7Z0X3; Q7Z0X4; Q94363; Q9U326;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=E3 SUMO-protein ligase gei-17;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase gei-17 {ECO:0000305};
DE AltName: Full=Gex-3-interacting protein 17;
GN Name=gei-17 {ECO:0000312|WormBase:W10D5.3c};
GN ORFNames=W10D5.3 {ECO:0000312|WormBase:W10D5.3c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP POSSIBLE INTERACTION WITH GEX-3.
RX PubMed=11922622; DOI=10.1006/bbrc.2002.6717;
RA Tsuboi D., Qadota H., Kasuya K., Amano M., Kaibuchi K.;
RT "Isolation of the interacting molecules with GEX-3 by a novel functional
RT screening.";
RL Biochem. Biophys. Res. Commun. 292:697-701(2002).
RN [3]
RP FUNCTION.
RX PubMed=15654100; DOI=10.1534/genetics.104.036137;
RA Holway A.H., Hung C., Michael W.M.;
RT "Systematic, RNA-interference-mediated identification of mus-101 modifier
RT genes in Caenorhabditis elegans.";
RL Genetics 169:1451-1460(2005).
RN [4]
RP FUNCTION.
RX PubMed=16701625; DOI=10.1016/j.ydbio.2006.04.001;
RA Roy Chowdhuri S., Crum T., Woollard A., Aslam S., Okkema P.G.;
RT "The T-box factor TBX-2 and the SUMO conjugating enzyme UBC-9 are required
RT for ABa-derived pharyngeal muscle in C. elegans.";
RL Dev. Biol. 295:664-677(2006).
RN [5]
RP FUNCTION.
RX PubMed=16549501; DOI=10.1083/jcb.200512136;
RA Holway A.H., Kim S.-H., La Volpe A., Michael W.M.;
RT "Checkpoint silencing during the DNA damage response in Caenorhabditis
RT elegans embryos.";
RL J. Cell Biol. 172:999-1008(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24297748; DOI=10.1083/jcb.201307181;
RA Ferreira H.C., Towbin B.D., Jegou T., Gasser S.M.;
RT "The shelterin protein POT-1 anchors Caenorhabditis elegans telomeres
RT through SUN-1 at the nuclear periphery.";
RL J. Cell Biol. 203:727-735(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-417.
RX PubMed=25475837; DOI=10.1038/ncomms6485;
RA Pelisch F., Sonneville R., Pourkarimi E., Agostinho A., Blow J.J.,
RA Gartner A., Hay R.T.;
RT "Dynamic SUMO modification regulates mitotic chromosome assembly and cell
RT cycle progression in Caenorhabditis elegans.";
RL Nat. Commun. 5:5485-5485(2014).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=25873636; DOI=10.1534/g3.115.018101;
RA Milton A.C., Okkema P.G.;
RT "Caenorhabditis elegans TBX-2 Directly Regulates Its Own Expression in a
RT Negative Autoregulatory Loop.";
RL G3 (Bethesda) 5:1177-1186(2015).
CC -!- FUNCTION: Functions as an E3-type smo-1 ligase (PubMed:15654100,
CC PubMed:16701625, PubMed:16549501, PubMed:25475837). Mediates smo-1
CC conjugation to air-2 in vitro and is required for proper chromosome
CC alignment (PubMed:25475837). In the early embryo, specifically
CC suppresses checkpoint activation in response to DNA damage, maybe by
CC promoting mus-101 sumoylation (PubMed:15654100). In embryos, plays a
CC role in determining telomere localization in the nucleus
CC (PubMed:24297748). {ECO:0000269|PubMed:15654100,
CC ECO:0000269|PubMed:16549501, ECO:0000269|PubMed:16701625,
CC ECO:0000269|PubMed:24297748, ECO:0000269|PubMed:25475837}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: May interact with gex-3. {ECO:0000269|PubMed:11922622}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=c;
CC IsoId=Q94361-1; Sequence=Displayed;
CC Name=2; Synonyms=f;
CC IsoId=Q94361-2; Sequence=VSP_022187, VSP_022191;
CC Name=3; Synonyms=g;
CC IsoId=Q94361-3; Sequence=VSP_022185, VSP_022190, VSP_022191;
CC Name=4; Synonyms=e;
CC IsoId=Q94361-4; Sequence=VSP_022187, VSP_022188, VSP_022189;
CC Name=5; Synonyms=a;
CC IsoId=Q94361-5; Sequence=VSP_022187, VSP_022189;
CC Name=6; Synonyms=d;
CC IsoId=Q94361-6; Sequence=VSP_022186, VSP_022187, VSP_022189;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown abolishes metaphase and
CC spindle midzone-specific smo-1 conjugation during the first embryonic
CC mitotic division. RNAi-mediated knockdown disrupts the anchoring of
CC telomeres to the nuclear envelope in embryos, but not in muscle nuclei
CC (PubMed:24297748). RNAi-mediated knockdown results in ectopic tbx-2
CC expression in seam cells, the gut and in the syncytial hypodermis
CC (PubMed:25873636). {ECO:0000269|PubMed:24297748,
CC ECO:0000269|PubMed:25475837, ECO:0000269|PubMed:25873636}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
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DR EMBL; BX284601; CAB02133.4; -; Genomic_DNA.
DR EMBL; BX284601; CAB02134.3; -; Genomic_DNA.
DR EMBL; BX284601; CAB54321.3; -; Genomic_DNA.
DR EMBL; BX284601; CAD98729.3; -; Genomic_DNA.
DR EMBL; BX284601; CAD98730.3; -; Genomic_DNA.
DR EMBL; BX284601; CAI79179.3; -; Genomic_DNA.
DR PIR; T26330; T26330.
DR PIR; T26331; T26331.
DR PIR; T26332; T26332.
DR RefSeq; NP_001021677.3; NM_001026506.3. [Q94361-4]
DR RefSeq; NP_001021678.3; NM_001026507.3. [Q94361-2]
DR RefSeq; NP_001021679.3; NM_001026508.3. [Q94361-3]
DR RefSeq; NP_492442.3; NM_060041.3. [Q94361-5]
DR RefSeq; NP_492443.3; NM_060042.3. [Q94361-6]
DR RefSeq; NP_492444.4; NM_060043.4. [Q94361-1]
DR AlphaFoldDB; Q94361; -.
DR SMR; Q94361; -.
DR BioGRID; 38164; 21.
DR DIP; DIP-24916N; -.
DR IntAct; Q94361; 9.
DR STRING; 6239.W10D5.3c.1; -.
DR EPD; Q94361; -.
DR PaxDb; Q94361; -.
DR PeptideAtlas; Q94361; -.
DR EnsemblMetazoa; W10D5.3a.1; W10D5.3a.1; WBGene00001574. [Q94361-5]
DR EnsemblMetazoa; W10D5.3a.2; W10D5.3a.2; WBGene00001574. [Q94361-5]
DR EnsemblMetazoa; W10D5.3c.1; W10D5.3c.1; WBGene00001574. [Q94361-1]
DR EnsemblMetazoa; W10D5.3c.2; W10D5.3c.2; WBGene00001574. [Q94361-1]
DR EnsemblMetazoa; W10D5.3c.3; W10D5.3c.3; WBGene00001574. [Q94361-1]
DR EnsemblMetazoa; W10D5.3d.1; W10D5.3d.1; WBGene00001574. [Q94361-6]
DR EnsemblMetazoa; W10D5.3e.1; W10D5.3e.1; WBGene00001574. [Q94361-4]
DR EnsemblMetazoa; W10D5.3f.1; W10D5.3f.1; WBGene00001574. [Q94361-2]
DR EnsemblMetazoa; W10D5.3g.1; W10D5.3g.1; WBGene00001574. [Q94361-3]
DR GeneID; 172733; -.
DR KEGG; cel:CELE_W10D5.3; -.
DR UCSC; W10D5.3f; c. elegans. [Q94361-1]
DR CTD; 172733; -.
DR WormBase; W10D5.3a; CE46915; WBGene00001574; gei-17. [Q94361-5]
DR WormBase; W10D5.3c; CE46906; WBGene00001574; gei-17. [Q94361-1]
DR WormBase; W10D5.3d; CE46859; WBGene00001574; gei-17. [Q94361-6]
DR WormBase; W10D5.3e; CE47019; WBGene00001574; gei-17. [Q94361-4]
DR WormBase; W10D5.3f; CE46965; WBGene00001574; gei-17. [Q94361-2]
DR WormBase; W10D5.3g; CE46934; WBGene00001574; gei-17. [Q94361-3]
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR InParanoid; Q94361; -.
DR OMA; SYLMMNE; -.
DR OrthoDB; 1131748at2759; -.
DR SignaLink; Q94361; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:Q94361; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001574; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0070090; C:metaphase plate; IDA:WormBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0061665; F:SUMO ligase activity; IDA:WormBase.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:WormBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0043060; P:meiotic metaphase I plate congression; IMP:WormBase.
DR GO; GO:1904290; P:negative regulation of mitotic DNA damage checkpoint; IMP:WormBase.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:WormBase.
DR GO; GO:1904333; P:positive regulation of error-prone translesion synthesis; IMP:WormBase.
DR GO; GO:1990466; P:protein autosumoylation; IDA:WormBase.
DR GO; GO:0016925; P:protein sumoylation; IDA:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.60.120.780; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA repair; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..780
FT /note="E3 SUMO-protein ligase gei-17"
FT /id="PRO_0000270191"
FT DOMAIN 203..367
FT /note="PINIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00799"
FT ZN_FING 400..485
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 181..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT VAR_SEQ 85..206
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_022185"
FT VAR_SEQ 85..86
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_022186"
FT VAR_SEQ 152..206
FT /note="Missing (in isoform 2, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_022187"
FT VAR_SEQ 559..574
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_022188"
FT VAR_SEQ 661..706
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_022189"
FT VAR_SEQ 661
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_022190"
FT VAR_SEQ 763..780
FT /note="GAFAYYPPQYPQQQYRQN -> DTNNIQPPRILSMAEIQANASRLLVNGHLM
FT IDHSGVTMRNPRGSRN (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_022191"
FT MUTAGEN 417
FT /note="L->A: Greatly reduces E3 ligase activity and
FT decreases smo-1 chain formation."
FT /evidence="ECO:0000269|PubMed:25475837"
SQ SEQUENCE 780 AA; 88139 MW; 49D86A064355139D CRC64;
MLPNNQWQIP INNGLTHQEN MAAHAAVMKL RVHDLQSIIS QLSLRKPRPQ KSEHQKVVVE
SLRDPHHARQ IYQMASNFPN GNYEMQKRPA TTSQVRSHPY VLPSRSGASN HLVNHHYQQQ
QQQQPQPHNL LHQQMMASHH SHLQQQHHPS TVRWLTPELL EEQLRGSMRY GAPAAAAATN
APLHSSFPNH GRSSQQSLQK SEKSNRPKKM YADNFEPLPL PFYDVISVLL KPVELHSSDS
PTLKQTKQLQ FPFLLTAEHI SKISYRADVT PLPRYELQLR FFNLTEPVQG PQKDDFPLNC
YARVDDSVVQ LPNVIPTNKT NAEPKRPSRP VNITSNMNRY KKEHTVAVEW LADKRVWAAG
VYFVHRVNSD ILFKRLNQNV SRHRSLEVTK QEVIKKLSGG EDDIAMDRLN ISLLDPLCKT
RMTTPSRCQD CTHLQCFDLL SYLMMNEKKP TWQCPVCSSN CPYDRLIVDD YFLDMLAKVD
KNTTEVELKE DGSYDVIKEE AFCISDDDDD DVVPATVNGT ASCSSTNGNG LANEAAKKKP
ADDDIITLSD DDDEELNRGI MNSLNDSFSP GRHTASAELA AQKTPPQQKK KTKDDDIEII
TLDDTPPRPV AASANLPMRQ MSQQNQMPVG SSPSGMASTQ MGMNEGASKT IRDALNKIGE
QSANSSTQSS PLVQLHHTTH PLNFAQSSYM NPSSGSQTPT SQYGYSPMIN QAPHFQMQNG
LIGRNNQMVH MQQHHLQQQQ QQQQSPQIMS PSFYAQQQMS NGGAFAYYPP QYPQQQYRQN
