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Database: UniProt
Entry: G5EFS1_CAEEL
LinkDB: G5EFS1_CAEEL
Original site: G5EFS1_CAEEL 
ID   G5EFS1_CAEEL            Unreviewed;       597 AA.
AC   G5EFS1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Death domain-containing protein {ECO:0000313|EMBL:CAB62796.1};
DE   SubName: Full=IKB-1 {ECO:0000313|EMBL:AAK37547.1};
GN   Name=ikb-1 {ECO:0000313|EMBL:CAB62796.1,
GN   ECO:0000313|WormBase:C04F12.3};
GN   ORFNames=C04F12.3 {ECO:0000313|WormBase:C04F12.3}, CELE_C04F12.3
GN   {ECO:0000313|EMBL:CAB62796.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB62796.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAB62796.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB62796.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000313|EMBL:AAK37547.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11516642; DOI=10.1016/S0960-9822(01)00241-X;
RA   Pujol N., Link E.M., Liu L.X., Kurz C.L., Alloing G., Tan M., Ray K.P.,
RA   Solari R., Johnson C.D., Ewbank J.J.;
RT   "A reverse genetic analysis of components of the Toll signaling pathway in
RT   Caenorhabditis elegans.";
RL   Curr. Biol. 11:809-821(2001).
RN   [3] {ECO:0000313|EMBL:CAB62796.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB62796.1};
RA   Sulson J.E., Waterston R.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:CAB62796.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB62796.1};
RG   WormBase Consortium;
RA   WormBase;
RL   Submitted (AUG-2023) to the EMBL/GenBank/DDBJ databases.
CC   -!- INTERACTION:
CC       G5EFS1; Q9TZK8: meg-4; NbExp=3; IntAct=EBI-314119, EBI-314126;
CC       G5EFS1; Q03601: nhl-1; NbExp=5; IntAct=EBI-314119, EBI-314158;
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DR   EMBL; AF348169; AAK37547.1; -; mRNA.
DR   EMBL; BX284601; CAB62796.1; -; Genomic_DNA.
DR   RefSeq; NP_492575.1; NM_060174.5.
DR   SMR; G5EFS1; -.
DR   IntAct; G5EFS1; 9.
DR   MINT; G5EFS1; -.
DR   STRING; 6239.C04F12.3.1; -.
DR   PaxDb; 6239-C04F12-3; -.
DR   EnsemblMetazoa; C04F12.3.1; C04F12.3.1; WBGene00002069.
DR   GeneID; 172817; -.
DR   KEGG; cel:CELE_C04F12.3; -.
DR   AGR; WB:WBGene00002069; -.
DR   WormBase; C04F12.3; CE19676; WBGene00002069; ikb-1.
DR   eggNOG; KOG0504; Eukaryota.
DR   HOGENOM; CLU_457284_0_0_1; -.
DR   OMA; CLADSED; -.
DR   OrthoDB; 5406967at2759; -.
DR   Reactome; R-CEL-8951664; Neddylation.
DR   Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00002069; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; HDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051059; F:NF-kappaB binding; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd08310; Death_NFkB-like; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   PANTHER; PTHR24178:SF9; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00531; Death; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00005; DEATH; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Proteomics identification {ECO:0007829|EPD:G5EFS1,
KW   ECO:0007829|PeptideAtlas:G5EFS1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT   REPEAT          212..244
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          282..314
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          316..348
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          349..381
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          502..595
FT                   /note="Death"
FT                   /evidence="ECO:0000259|SMART:SM00005"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  66422 MW;  CD271E6B4CF25A35 CRC64;
     MSKADENDAN LTENGVHKSR SDSEINSHTS SIHKSSSQHR RLFIDDISTI EASAGDRVWA
     TCSGAGDATE LITIHFLGDQ FEESAIDVVR KHSLVMFTVP SLKVDSELEV ELRFSTSNDN
     VTTISFKYLP RKIQRSHTQE ISLFDNLLEF ATNGDTISLL QPFVAQISKQ DIEGNTVFHV
     AAKNGQSFSL KLLLSVIPPD IKNEVINVQN THGLTALHVA IRTGDPDAVH YLMNHGAKID
     ISDNHGSTAL HYLGDAYNES IFKEILEPSR GQRFDVNQLN SEGFAPIHVA VRRLKLSLIE
     MLIEAGALID FLDTEKKRNA LMHAIEMNDF ETIQLLVERG SGTNIEDESG ETALSLAVKN
     VNYPVIGLLL DNGADPNRQN SKGICLADSE DSVIQNIING DRPELPKKEA FGVPNDLAIS
     RSPLFGRSHP DQAPGEESGR HRVVKRSREE ILNDAQTLLA ETDSMAPRVS RISTSESEDE
     QQPGPSTSSG TRRRRSEWDR NPKLSDSVCN LDYLTRIRVA KIFDDQCKWQ RLAQQLNCDH
     MVELISICSS GDDSSPTMIL LDQFEQLEDS SISRLRDAMN QMAEDDAVKL IDSRYVY
//
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