ID A0A1D6DXC1_MAIZE Unreviewed; 915 AA.
AC A0A1D6DXC1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000256|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000256|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000256|HAMAP-Rule:MF_03002};
DE AltName: Full=eIF3 p110 {ECO:0000256|HAMAP-Rule:MF_03002};
GN ORFNames=ZEAMMB73_Zm00001d002166 {ECO:0000313|EMBL:ONM13303.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM13303.1};
RN [1] {ECO:0000313|EMBL:ONM13303.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM13303.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC Rule:MF_03002}.
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DR EMBL; CM007648; ONM13303.1; -; Genomic_DNA.
DR EMBL; CM007648; ONM13313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6DXC1; -.
DR OMA; NIDSRYL; -.
DR ExpressionAtlas; A0A1D6DXC1; baseline and differential.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13937; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03002};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}.
FT DOMAIN 625..796
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 104618 MW; B3323F29181C5EBE CRC64;
MASRFWGQGD SESEEEEVEE VESEQGSDSD DDGGRGGAGR GAQNRYLKNQ EDDSDESDTG
HRVIRSLRDK RNEEMRSIVD QMRNAMKIND WVSLQESFEK LNKHLEKVVR VNESTEVPKM
YIKALVLLED FLAEALANKE ARKKMSSSNS KALNAMRQKL KKNNKQYEEQ IQKCREHPES
FEDEAADDKD VDDDDADESD AEIEDPDKIA MSESEEEQDE EDDDKDGWEQ KRSKKDKLMD
KQFLKDPSEI TWDIVDKKLK EIIASRGKKG TGRIERVEQL TFLTRVAKTP AQKLEILFHV
ISAQFDVNPS LLGHMPVNVW KKCVNNMLLV LDILQQYPNI VVDTSFEPDE NETQKGADYN
GTIHVVGDLV AFLERLDSEF LKTLQCTDPY TKDYVQRLRE EPLFLVVAQN VQDYLERVGN
FKAAAKVALR RVELVYYKPQ EVYDAMRKLA EQPEDCVDDD DAEAGDEHKA VDDNRGPSPF
VVIPEAVHRK PTFPESGRTL MDGLMFLIYK YGDERTKARA MLCDIYHHAI SDEFSVARDL
LLMSHLQDGI QLMDISSQIL FNRVMAQLGL CAFRAGLINE AHGCLTELYS TGRVKELLAQ
GVQQSRYHEK TPEQERLERR RQMPYHMHIN LELLEATHLI CAMLIEVPNM AASTYDKRRP
MSKTFRRLLE VSERQTFVGP PENVRDHVMA ATRALNKGDH QKAFSVINSL EIWKLLRNRE
HVLEMLELKI KEEALRTYLF SYSSSYESLS LNQLTTMFDL SEQHAHSIVS KMMMHEELHA
SWDQPTKCIV FHSVDQTRLQ GLLFQMADKL SVLVEINERA YEARTGGTLE GVPPRRRGEG
QDNMGKWQDN FVSSQGRQGG GNRFGYSGRG AISGQSGGGH QRDRGNQGYR GGYGGVSRFQ
DASARMVNLN RMGRV
//
