EIF3C_PICGU
ID EIF3C_PICGU Reviewed; 836 AA.
AC A5DPQ5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
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=NIP1 {ECO:0000255|HAMAP-Rule:MF_03002}; ORFNames=PGUG_05256;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408161; EDK41158.2; -; Genomic_DNA.
DR RefSeq; XP_001482236.1; XM_001482186.1.
DR AlphaFoldDB; A5DPQ5; -.
DR SMR; A5DPQ5; -.
DR STRING; 4929.XP_001482236.1; -.
DR EnsemblFungi; EDK41158; EDK41158; PGUG_05256.
DR GeneID; 5124234; -.
DR KEGG; pgu:PGUG_05256; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_2_1; -.
DR InParanoid; A5DPQ5; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR Proteomes; UP000001997; 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:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:UniProt.
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; 2.
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..836
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000366883"
FT DOMAIN 586..761
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 95072 MW; ABA4DBB5EEAFAE5F CRC64;
MSRFFVSGYD SESSSEEEDL LTSSEEELMS SEQESDSEFD DEFANDDDSD SSDSDSDGRP
SGPAYFLKSS FRKGAGGDSD SDSEDEGRRV VKSAKEKLTD DMKDAVEAVN SAKRQENWIS
ALTEFERLGR LLVRAGQQGF GTPNFYIKCL VDLEAYLIET TANEKESTRK MNANLARAFT
SLKQRVKKQV KEFSHLVELY KSEPELFDKE EPVETIEKDA EIQATPLASS TGRALSPVFA
TLKSVAETRG KKNIDKFEQV QILEDLLEEV SPKGSPFEII SIYQMLLSIR FDASSHHAFM
PLDQWQKNKD TLNDLLDFLE KHSNEYQVSE LGTASDDIDL EPPANADGIR ILPGSVTSHI
ERLDDEFIRY LQNTDPHSLE YIDRLKDEKD TYNLVVRGQL YVEKTTPDHV RGTYQGEQLA
RIVMRRMNHI YYKPDQLIKA NESEAWRHLS GDSQIVAKNS EPKDVINGLA EFLSKQDGAI
YPKGALLFSV YYHAVNNDYS VARDMFLSSQ VHQGINNADS SIQVLYNRAM VQLGLSAFRY
GNIEESHQAL NEIANSQRLK ELLGQGFNSK YPSQATVAEK QRLLPFHMHI NLELLECVFM
TCSLLIEIPQ LAAASNSTKE SRRKTNIKSF KSKLEFHDRQ YFTGPPESIK DHIVHASISL
QKGDWHNAYK LLSTIKIWKL LPNNDQLLEM MRGKLQVEGL RTYIFTYKSI YTKLSVVKLA
KIFDINEEEV LSIVDKMISS GEVSASLSDD KKSINFVSSE HLQRTRLQEL AIVMNEKIGL
LTDKNEKTAS NGHGRKTTQQ QQQQQQKEQR EQTHDENIKF RYANVNTNND EFQTIA
