EIF3C_MEDTR
ID EIF3C_MEDTR Reviewed; 935 AA.
AC Q9XHM1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03002};
GN Name=TIF3C1; Synonyms=AM3-1;
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=10065555; DOI=10.1094/mpmi.1999.12.3.171;
RA van Buuren M.L., Maldonado-Mendoza I.E., Trieu A.T., Blaylock L.A.,
RA Harrison M.J.;
RT "Novel genes induced during an arbuscular mycorrhizal (AM) symbiosis formed
RT between Medicago truncatula and Glomus versiforme.";
RL Mol. Plant Microbe Interact. 12:171-181(1999).
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:0000255|HAMAP-Rule:MF_03002}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000255|HAMAP-
CC Rule:MF_03002}.
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DR EMBL; AF106930; AAD39891.1; -; mRNA.
DR PIR; T50774; T50774.
DR RefSeq; XP_003589347.2; XM_003589299.2.
DR AlphaFoldDB; Q9XHM1; -.
DR SMR; Q9XHM1; -.
DR STRING; 3880.AES59598; -.
DR iPTMnet; Q9XHM1; -.
DR GeneID; 11419223; -.
DR eggNOG; KOG1075; Eukaryota.
DR eggNOG; KOG1076; Eukaryota.
DR ExpressionAtlas; Q9XHM1; 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 HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13937; PTHR13937; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Initiation factor; Protein biosynthesis.
FT CHAIN 1..935
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000123528"
FT DOMAIN 624..796
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 105069 MW; 199F5FFF898EB11F CRC64;
MTSRFFYQGG DQSDTDDEPT DIDDEPSDTE PAPTDPNGKS KYLAGGNADD SDDDDGQKRV
VKSAKDKRFD EMASTVDQIK NAIKINDWVS LQESFDKINK QLEKVMRVIE SQKIPNLYIK
ALVMLEDFLA QASANKDAKK KMSPSNAKAF NSMKQKLKKN NKQYEDLIIK CRESPESEGE
KDEDDEDSDE YESDDEMIEP DQLRKPEPVS DSETSELGND RPGDDGDAPW DQKLSKKDRL
LEKMFMKKPS EITWDTVNKK FKEILEARGR KGTGRFEQVE QLTFLTKVAK TPAQKLQILF
SVVSAQFDVN PGLSGHMPIS VWKKCVQNML VILDILVQHP NIKVDDSVEL DENETKKGDD
YNGPINVWGN LVAFLEKIDA EFFKSLQCID PHTREYVERL RDEPQFVVLA QNVQEYLESI
GDFKASSKVA LKRVELIYYK PHEVYEATRK LAEMTVEGDN GEMSEEPKGF EDTRIPAPFV
VTLELVARKP TFPENSRTLM DVLVSLIYKY GDERTKARAM LCDIYHHALL DEFAVARDLL
LMSHLQENVH HMDISTQILF NRAMSQLGLC AFRAGLVSEA HGCLSELYSG GRVKELLAQG
VSQSRYHEKT PEQERLERRR QMPYHMHINL ELLESVHLTS AMLLEVPNMA ANVHDAKRKI
ISKNFRRLLE VSEKQTFTGP PETVRDHVMA ATRVLINGDF QKAFDIIASL DVWKFVKNRD
AVLEMLKDKI KEEALRTYLF TFSSSYDSLS VVQLTNFFDL SLPRVHSIVS RMMVNEELHA
SWDQPTGCII FRNVEHSRVQ ALAFQLTEKL SILAESNERA TEARLGGGGL DLPPRRRDGQ
DYAAAAAGGG SGTSSGGRWQ DLSYSQTRQG SGRTGYGGGR ALSFSQAGGS GGYSRGRGTG
GGGYQNSGRT QGGSALRGPH GDTSTRMVSL RGVRA
