MXT_CAEEL
ID MXT_CAEEL Reviewed; 507 AA.
AC Q9XW13;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Eukaryotic translation initiation factor 4E-binding protein Mextli homolog {ECO:0000305};
GN Name=mxt-1 {ECO:0000312|WormBase:Y18D10A.8};
GN Synonyms=mxt {ECO:0000303|PubMed:26294658};
GN ORFNames=Y18D10A.8 {ECO:0000312|WormBase:Y18D10A.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0007744|PDB:5ABX, ECO:0007744|PDB:5ABY}
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 471-507 IN COMPLEX WITH IFE-3,
RP INTERACTION WITH IFE-3, DOMAIN, AND MUTAGENESIS OF MET-493; ILE-497 AND
RP ILE-504.
RX PubMed=26294658; DOI=10.1101/gad.269068.115;
RA Peter D., Weber R., Kone C., Chung M.Y., Ebertsch L., Truffault V.,
RA Weichenrieder O., Igreja C., Izaurralde E.;
RT "Mextli proteins use both canonical bipartite and novel tripartite binding
RT modes to form eIF4E complexes that display differential sensitivity to 4E-
RT BP regulation.";
RL Genes Dev. 29:1835-1849(2015).
CC -!- FUNCTION: Plays a role in promoting translation.
CC {ECO:0000250|UniProtKB:Q9VR35}.
CC -!- SUBUNIT: Interacts with eukaryotic translation initiation factor ife-3.
CC {ECO:0000269|PubMed:26294658}.
CC -!- INTERACTION:
CC Q9XW13; Q8MQ52: CELE_F44A2.5; NbExp=4; IntAct=EBI-330111, EBI-330140;
CC Q9XW13; Q21693: ife-2; NbExp=5; IntAct=EBI-330111, EBI-330154;
CC Q9XW13; O61955: ife-3; NbExp=5; IntAct=EBI-330111, EBI-330119;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9VR35}.
CC -!- DOMAIN: Binds to ife-3 using a bipartite interface in the C-terminal
CC domain which comprises a canonical helix which engages the ife-3 dorsal
CC surface and a non-canonical helix which engages the ife-3 lateral
CC surface. {ECO:0000269|PubMed:26294658}.
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DR EMBL; BX284601; CAA22321.1; -; Genomic_DNA.
DR PIR; T26530; T26530.
DR RefSeq; NP_493246.1; NM_060845.5.
DR PDB; 5ABX; X-ray; 1.66 A; B=471-507.
DR PDB; 5ABY; X-ray; 1.95 A; B/D/F=471-507.
DR PDBsum; 5ABX; -.
DR PDBsum; 5ABY; -.
DR AlphaFoldDB; Q9XW13; -.
DR SMR; Q9XW13; -.
DR ComplexPortal; CPX-3482; Eukaryotic translation initiation factor 4E-Mxt complex.
DR DIP; DIP-27212N; -.
DR IntAct; Q9XW13; 10.
DR STRING; 6239.Y18D10A.8; -.
DR EPD; Q9XW13; -.
DR PaxDb; Q9XW13; -.
DR PeptideAtlas; Q9XW13; -.
DR EnsemblMetazoa; Y18D10A.8.1; Y18D10A.8.1; WBGene00012478.
DR GeneID; 173151; -.
DR KEGG; cel:CELE_Y18D10A.8; -.
DR UCSC; Y18D10A.8; c. elegans.
DR CTD; 173151; -.
DR WormBase; Y18D10A.8; CE21404; WBGene00012478; mxt-1.
DR eggNOG; ENOG502QRYP; Eukaryota.
DR GeneTree; ENSGT00520000058221; -.
DR HOGENOM; CLU_596168_0_0_1; -.
DR InParanoid; Q9XW13; -.
DR OMA; LRHEMII; -.
DR OrthoDB; 915513at2759; -.
DR PhylomeDB; Q9XW13; -.
DR PRO; PR:Q9XW13; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00012478; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034518; C:RNA cap binding complex; IBA:GO_Central.
DR GO; GO:0070992; C:translation initiation complex; IC:ComplexPortal.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:1901190; P:regulation of formation of translation initiation ternary complex; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IC:ComplexPortal.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR040160; Mxt.
DR PANTHER; PTHR20849; PTHR20849; 1.
DR Pfam; PF00013; KH_1; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..507
FT /note="Eukaryotic translation initiation factor 4E-binding
FT protein Mextli homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436264"
FT DOMAIN 242..307
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 126..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 493
FT /note="M->D: Reduced binding to ife-3."
FT /evidence="ECO:0000269|PubMed:26294658"
FT MUTAGEN 497
FT /note="I->D: Reduced binding to ife-3; when associated with
FT D-504."
FT /evidence="ECO:0000269|PubMed:26294658"
FT MUTAGEN 504
FT /note="I->D: Reduced binding to ife-3; when associated with
FT D-497."
FT /evidence="ECO:0000269|PubMed:26294658"
FT HELIX 475..481
FT /evidence="ECO:0007829|PDB:5ABX"
FT HELIX 491..500
FT /evidence="ECO:0007829|PDB:5ABX"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:5ABX"
SQ SEQUENCE 507 AA; 56571 MW; 3D9DDE0D40F088F6 CRC64;
MLHNYDDFGG GKMQGAPQVP RNTLLSVDQQ LQLMNTINNM VRASQFTSQL ANTIFTLCAQ
LKTSGSMLEQ SHKNELNKVF TSLRQACCRD NGQLGTPCRL KIMELVELRA MNWRTNLAHS
QYYVNRPEGQ HDPAPTVGIP PSATSPPTQV TSSVTSPVPS SPQPPMQFVP QNPMMFQDPM
AANHNAGGIF FIPAASTWMN PLMPMPPNPF LPHSMIPPDH QMFLRQRSLN KKPNNLMNKT
LQLRHEMIIR NSDSGKIMGV KGRRVAAVEQ LTNTVISFQK VDSKSKERTL TITASTMEDI
ERAKDMIIDT IRRNMSPMRT DMSIPPPNQY SGMSSENQSI PSQQNTANID EDDDDDDEDI
KLEQTSDGKL TFHCDDPELL AAAQEALSAY LRVRARPSAE EREKKKERRK SMPLQQTARD
QQEPVMLKPA KTFHGSTPNL ADGLAATTTV VVASIPQPMV PNVHASGDNP IRYNRDTLMT
ARDTKRAPIP DEMLQEINRV APDILIA
