ID A0A4W5N5Y4_9TELE Unreviewed; 998 AA.
AC A0A4W5N5Y4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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};
GN Name=EIF3C {ECO:0000256|HAMAP-Rule:MF_03002};
GN Synonyms=EIF3S8 {ECO:0000256|HAMAP-Rule:MF_03002};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000046112.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000046112.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. {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 AlphaFoldDB; A0A4W5N5Y4; -.
DR Ensembl; ENSHHUT00000047812.1; ENSHHUP00000046112.1; ENSHHUG00000028075.1.
DR GeneTree; ENSGT00390000017900; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000314982}.
FT DOMAIN 675..851
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 113806 MW; 149E2B8FD978074A CRC64;
MSRFFATGSD SESESSSSAD EITPKAPGTT FTKQSLLLSD DEEDTKRVVR SAKDKRFEEL
TNLIKTIRNA MKIRDMSKCL EEFEQLCRAF LKSKTIVDKE GVPPFYIRLL ADLEDYLNQL
WEDKEGKKKM NKNNAKALST LRQKIRKYNR DYETEIASYK ENPMASADEE EEEEEKDEVD
SGSSSDSDEV PGVAKSFLKK KPVAEVAAPP PDPSKFLKAA ADKDASSSSD EDDEEWDSDT
AESGSGSEDE EGKNASMAQI FLKKPGSEAE RHTSEKKKED RKKRHKRKER LEEEAEEEAQ
DEGEGEWEKV KGGVPLVKMF AKGTEINTTV VVKKLNEILQ ARGKKGTDRA AQIELLHALA
NISNENNLGE GILVKIKFNI IASLYDYNPN LAAFMKADMW KTCLDCIDEL LDILFNNNNI
FIGENIAEDS ENLAIADSQP FRVRGCILTL VERMDEEFTK IMQNTDPHSQ EYVDNLKDEG
RVCGIIDRLL GYLETKGSTE EVCRVYLRRI MHTYYKFDYK AHRRALGLQG ETKSEQDAEE
SEGEDSAFIM DRLCKFIYAK DRTDRIRTCA ILCHIYHHAL HSRWYQARDL MLMSHLQDNI
QHADPPVQIL YNRTMVQLGI CAFRQGMIKD AHNALLDIQS SGRAKELLGQ GLLMRNMQER
NAEQEKIEKR RQVPFHMHIN LELLECVYLV SAMLLEIPYM AAHEFDARRR MISKQFHHQL
RVGERQPLLG PPESMREHVV AASKSMKMGD WRTCHSFIIN EKMNSKVWDL FPETQCVREM
LVRKIQEESL RTYLFTYSSV YDSISMETLN EMFELELPTV HSIISKMIIN EELMASLDQP
TQTVVMHRTE PTSLQNMALQ LAEKLGGLVE NNERIFDLKQ GVYGGYFNRD QKGGYQQKQG
GYNRDQRGSY QQKQGGYNRD GQRGSYQPKQ GGYNRDGGSY QQRGGYNRDG NRGGGGGYQG
QNRGGYQGGG GYQGGGGYQG GYRGGYKGGY QNQDRRDY
//
