EIF3C_NEUCR
ID EIF3C_NEUCR Reviewed; 872 AA.
AC Q7SBD4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 93 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03002};
DE Short=eIF3 p93 {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=Translation initiation factor eIF3, p93 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03002};
GN Name=nip-1; ORFNames=NCU07831;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002238; EAA33716.1; -; Genomic_DNA.
DR RefSeq; XP_962952.1; XM_957859.3.
DR AlphaFoldDB; Q7SBD4; -.
DR SMR; Q7SBD4; -.
DR STRING; 5141.EFNCRP00000007471; -.
DR PRIDE; Q7SBD4; -.
DR EnsemblFungi; EAA33716; EAA33716; NCU07831.
DR GeneID; 3879100; -.
DR KEGG; ncr:NCU07831; -.
DR VEuPathDB; FungiDB:NCU07831; -.
DR HOGENOM; CLU_004304_0_2_1; -.
DR InParanoid; Q7SBD4; -.
DR OMA; VVMHRSE; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
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; -; 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; 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 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..872
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000364287"
FT DOMAIN 613..787
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 872 AA; 98399 MW; 38611B9B0CC93EA1 CRC64;
MSRFFRGGDD SSTDSSSEEE EVYTSEEEEE KVQAEDESSS EEESDEEESD EESSSDEEEG
TKKKGASRFL QSDDESEEEE EEQSDDEATT KVKSAKDKRF DELESTISQI QNGQKINDWS
LIANEFDKLN RQVVKLQDGS KAPKSYIKAI ADLEDFMNET LAKQKVTPKK MNATNARGLN
AVKQRIRKNN KEYQTQIDAY RKDADAFMES DDEVAAPKVV SKVRFEAPVV SAEQQEEDDK
GFSTVDSRGK VVQYTPESIL KHLRAIIESR GKKNTDRLEQ IKVMETLNKV VPITPYQKIR
VLQTLISARF DLGAGGAAQM PLDQWKAAER DLASLLEILE KEKDHVVVEG AEEWDDDDKL
PTIPEGEKYL KVPGSVVSLI ERLDDELTRS LQAIDPHTSE YIDRLTDEGS LYNTIFRGLL
YYEHLRKDAS LEVPQESLNR IIQRRLDHVY YKPAQVVKIL EENAWKQVSA EADSEITPRS
QSGDAGKLIN ILSNYLFENS EGIIRARAML CQIYFLALHD EYYKSRDLML TSHLQETIAN
FDIATQILYN RTLVQVGLCA FRKGLVYDAQ NTLQEICGSG RQKELLAQGV MIQRYSQVTP
EQERLEKQRQ LPFHMHINLE LLECVYLTCS MLLEIPLLAQ TGSSPDVKKR IISKTYRRML
EYHERQIFTG PPENTRDHVM QASKALAAGE WKKATDFIHS IKIWDLMPNT EGIKTMLAKQ
IQEEGLRTYL FTYAPFYDTL AIATLSSMFE LDSRKVSAVV SKMISHEELA AALDQVTETV
IFRKGVELSR LQSLALTLSD KASSLIETNE RTLEQKTQGS ANAFSRKDNR GGGQRGGGQR
GGRGGARTGG NPQRQAGGTQ FTGGALGNAV RG