ID A0A251TMZ1_HELAN Unreviewed; 924 AA.
AC A0A251TMZ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 Name=EIF3C {ECO:0000313|EMBL:OTG12460.1};
GN ORFNames=HannXRQ_Chr10g0309871 {ECO:0000313|EMBL:OTG12460.1},
GN HanXRQr2_Chr10g0456201 {ECO:0000313|EMBL:KAF5787734.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG12460.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|EMBL:KAF5787734.1, ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5787734.1};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
RN [2] {ECO:0000313|EMBL:OTG12460.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaves {ECO:0000313|EMBL:OTG12460.1};
RA Langlade N., Munos S.;
RT "Sunflower complete genome.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF5787734.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5787734.1};
RA Gouzy J., Langlade N., Munos S.;
RT "Helianthus annuus Genome sequencing and assembly Release 2.";
RL Submitted (JUN-2020) 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; MNCJ02000325; KAF5787734.1; -; Genomic_DNA.
DR EMBL; CM007899; OTG12460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251TMZ1; -.
DR STRING; 4232.A0A251TMZ1; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr10g0456201; mRNA:HanXRQr2_Chr10g0456201; HanXRQr2_Chr10g0456201.
DR Gramene; mRNA:HanXRQr2_Chr10g0456201; mRNA:HanXRQr2_Chr10g0456201; HanXRQr2_Chr10g0456201.
DR InParanoid; A0A251TMZ1; -.
DR OMA; FRCGLIK; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000215914; Chromosome 10.
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; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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}; Proteasome {ECO:0000313|EMBL:KAF5787734.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000215914}.
FT DOMAIN 618..790
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 104774 MW; 4F2F29BDB3B2672B CRC64;
MASKFWSNQA DSETESEVSD TEQDDVSEQE DATNAPDRNK YLDTGDSDSD DSDSHKRVIK
SAKDKRFEEL STTIDQMKNA MKINDWVSLQ ESFDKINRQL EKVMRVTESD RAPNNYIKAL
VMLEDFLNQA MANKEAKKKM SSSNAKALNA MRQKLKKNNK QYEDLINKCR ENPESFEDQE
EAEEPSEDED DDDEDESGSE IDDITKAEPE SDDTDDEDDE DKDVNQPGWE RKLSKKDKLM
EKQFKDPNQV TWDTVNKKFK EVVAARGRKG TGRLELVEQL TFLTKVAKTP AQKLEILFSV
VSAQFDVNPG LSGHMPINVW KKCVQNMLVI LDILEQYPNI LVDDTVEPDE NETQKGTDYT
DTIRIWGNLA AFLEKIDVEF FKSLQCIDPH TREYVERLQD EPLFFVLAQN VQAYLERVGD
HKAAAKVALK LVELVYYKPQ EVYGAMRNLA DQSEVDDGEE SGTESKGGPL APFVNVPEIV
PRKPSFPTSS RELMDNLVSL IYKHGDERTK ARAMLCDIYH HAILDEFSMA RDLLLMSHLQ
DSVQHMDIST QILFNRSMAQ LGLSAFRAGL ITEGHGCLSE LYSGGRVKEL LAQGVSQSRY
HEKTPEQERL ERRRQMPYHM HINLELLESV HLICAMLLEV PNMAANSHDA RRKVISKTLR
RLLEISDRQT FTGPPENVRD HVMAATRALS KGDFQTSFDV INSLDVWKLL KNRETVLAMI
KNKINEEALR TYLFTYSASY ETLKLEQLAK MFDLSESQTH SVVSKMMINE ELHASWDQPT
QCIVFHEVEH SRLQALAFQL TEKLSVLAES NERAIEARLG GGGLESLSSR RREGQDYAAV
AGGNKWQDNQ SYTQGRQQSG YGGGRPYGPG QNYQNRTSQS RGGYQSTRYQ DSAGAGRNYG
GSAARGGQMD GSNRMVSLNR GARA
//
