IKKE1_CAEEL
ID IKKE1_CAEEL Reviewed; 820 AA.
AC P32742; P32741; Q5FC85;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 5.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Inhibitor of nuclear factor kappa-B kinase epsilon subunit homolog 1 {ECO:0000312|WormBase:R107.4b};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=ikke-1 {ECO:0000312|WormBase:R107.4b};
GN ORFNames=R107.4 {ECO:0000312|WormBase:R107.4b};
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
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 [3]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ALLO-1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF LYS-49; 126-LEU--CYS-318 AND 131-VAL--ALA-264.
RX PubMed=29255173; DOI=10.1038/s41556-017-0008-9;
RA Sato M., Sato K., Tomura K., Kosako H., Sato K.;
RT "The autophagy receptor ALLO-1 and the IKKE-1 kinase control clearance of
RT paternal mitochondria in Caenorhabditis elegans.";
RL Nat. Cell Biol. 20:81-91(2018).
CC -!- FUNCTION: Serine/threonine-protein kinase, which plays a role in
CC regulating allophagy, an autophagic process in which paternal
CC organelles, including mitochondria and membranous organelles, are
CC degraded in embryos. Phosphorylates the allophagy receptor allo-1,
CC which is required for allophagy. {ECO:0000269|PubMed:29255173}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Interacts with allo-1 (via N-terminus); the interaction is
CC direct. {ECO:0000269|PubMed:29255173}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29255173}.
CC Note=Localizes to cytoplasmic puncta in oocytes. After fertilization,
CC localizes to paternal organelles during meiosis I and meiosis II. Co-
CC localizes with allo-1 in embryos and oocytes.
CC {ECO:0000269|PubMed:29255173}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b {ECO:0000312|WormBase:R107.4b};
CC IsoId=P32742-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:R107.4a};
CC IsoId=P32742-2; Sequence=VSP_004902, VSP_004904;
CC Name=c {ECO:0000312|WormBase:R107.4c};
CC IsoId=P32742-3; Sequence=VSP_004903;
CC Name=d {ECO:0000312|WormBase:R107.4d};
CC IsoId=P32742-4; Sequence=VSP_004903, VSP_059587;
CC -!- TISSUE SPECIFICITY: Expressed in oocytes.
CC {ECO:0000269|PubMed:29255173}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in defective
CC clearance of paternal mitochondria and impaired accumulation of the
CC autophagosome marker lgg-1 in 1-cell stage embryos.
CC {ECO:0000269|PubMed:29255173}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BX284603; CAA78473.3; -; Genomic_DNA.
DR EMBL; BX284603; CAD45599.1; -; Genomic_DNA.
DR EMBL; BX284603; CAD45600.1; -; Genomic_DNA.
DR EMBL; BX284603; CAI46627.1; -; Genomic_DNA.
DR PIR; C88546; C88546.
DR PIR; S30874; S30874.
DR RefSeq; NP_001022708.1; NM_001027537.3.
DR RefSeq; NP_499002.2; NM_066601.5.
DR RefSeq; NP_871627.1; NM_181898.3. [P32742-1]
DR RefSeq; NP_871628.1; NM_181899.4. [P32742-3]
DR AlphaFoldDB; P32742; -.
DR BioGRID; 41477; 2.
DR IntAct; P32742; 1.
DR STRING; 6239.R107.4b; -.
DR EPD; P32742; -.
DR PaxDb; P32742; -.
DR PeptideAtlas; P32742; -.
DR EnsemblMetazoa; R107.4a.1; R107.4a.1; WBGene00011299. [P32742-2]
DR EnsemblMetazoa; R107.4a.2; R107.4a.2; WBGene00011299. [P32742-2]
DR EnsemblMetazoa; R107.4b.1; R107.4b.1; WBGene00011299. [P32742-1]
DR EnsemblMetazoa; R107.4c.1; R107.4c.1; WBGene00011299. [P32742-3]
DR EnsemblMetazoa; R107.4d.1; R107.4d.1; WBGene00011299. [P32742-4]
DR GeneID; 176278; -.
DR KEGG; cel:CELE_R107.4; -.
DR UCSC; R107.4a; c. elegans.
DR CTD; 176278; -.
DR WormBase; R107.4a; CE31817; WBGene00011299; ikke-1. [P32742-2]
DR WormBase; R107.4b; CE31818; WBGene00011299; ikke-1. [P32742-1]
DR WormBase; R107.4c; CE31819; WBGene00011299; ikke-1. [P32742-3]
DR WormBase; R107.4d; CE37846; WBGene00011299; ikke-1. [P32742-4]
DR eggNOG; KOG4250; Eukaryota.
DR GeneTree; ENSGT00970000196625; -.
DR InParanoid; P32742; -.
DR OMA; YFCATGK; -.
DR OrthoDB; 1661979at2759; -.
DR PhylomeDB; P32742; -.
DR PRO; PR:P32742; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00011299; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Autophagy; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..820
FT /note="Inhibitor of nuclear factor kappa-B kinase epsilon
FT subunit homolog 1"
FT /id="PRO_0000086831"
FT DOMAIN 21..299
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 758..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 751..754
FT /note="FFCQ -> RVIN (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_004902"
FT VAR_SEQ 751..754
FT /note="Missing (in isoform c and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_004903"
FT VAR_SEQ 755..820
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_004904"
FT VAR_SEQ 774..820
FT /note="ESSIDEGSTSFESTPPSSPPDVGSNNYFQAVFQYFAKPTSSPSSSAK -> T
FT KKMERIFKKKRRENGNEGGDNDVCRICCENERQEKREKKRKSSGRRH (in isoform
FT d)"
FT /evidence="ECO:0000305"
FT /id="VSP_059587"
FT MUTAGEN 49
FT /note="K->M: Localizes to paternal organelles and interacts
FT with allo-1 in embryos, but does not rescue the paternal
FT mitochondrial clearance defect in the ikke-1 gk1264
FT mutant."
FT /evidence="ECO:0000269|PubMed:29255173"
FT MUTAGEN 126..318
FT /note="Missing: In gk1246; results in defective clearance
FT of paternal mitochondria in 1-cell stage embryos, and
FT impaired accumulation of the autophagosome marker lgg-1 in
FT 1-cell stage embryos and oocytes."
FT /evidence="ECO:0000269|PubMed:29255173"
FT MUTAGEN 131..264
FT /note="Missing: In tm4102; results in defective clearance
FT of paternal mitochondria and impaired accumulation of the
FT autophagosome marker lgg-1 in 1-cell stage embryos."
FT /evidence="ECO:0000269|PubMed:29255173"
SQ SEQUENCE 820 AA; 93169 MW; BCBAFB88D6796DB9 CRC64;
MAVSPHKTYP IVITHGEKYT LFNDESIGKG AYSEVYRGRT ESGRLVAVKT ACKKLEVAAI
GIEIEILKKL KGASNIVQYF GSNHTKMAPG SVTSETISFA MEYASSSLEA EMRRPKNHRG
LSSNALIDLV VDCSMALSAL REHNIAHRDI KHMNILLFPG TPTRGRRSTH LFKLCDMGCS
KSLSENSSHE MRTLVGTPNL LHPFLAHEMV DPLMAQNRHN WKTKSAYTSE QCDLWALGCT
LYFCATGKFP FEHERNNKSL YHKAVVALTQ NPDAIAMVLV QKGRDPGRRT DIFEFQPVTE
LPAKFTRYPK WLVSTMTCLL RSFFHEPSIE YYAKVADAMR NSKRRTFSSV DQMSIVEHTD
MSNVPHLGFS IPSISKCLGY PEGTDILLLS NTSTHYLDSK QKSVDGLPDD LYLVVPQTSH
VDMRKILARN IEFHEFDDMT DRKLSEIRIK KCYEGLSMLT EIDEYLALFD RVSTILSTQF
SLLVQELSQF ERVQTASRFA VYVDMASVPL MLFDEANPET KMISDQCIQQ AKRAREELER
HAKVSMDIEA CAKQLSKDAE DLRLEDMDLP GICEEIESYV FYDKQAILST QKYSQELVEL
CLKRRNNIME QIFNSPDRIN KSKLNKAMNL AASLSQLRSN YRKLQDMISE CVDLLEKPFQ
EMKDTVNRYL QAQGCSRNTM QKSMHLLRPE FHESQIRIKK TTKSCRKLID QLNIELDQLG
FVRLGDILIK AESEQTLTRS EEIQETQVVS FFCQAESSPN KEQFPKPEQD SILESSIDEG
STSFESTPPS SPPDVGSNNY FQAVFQYFAK PTSSPSSSAK
