EIF3C_PICST
ID EIF3C_PICST Reviewed; 839 AA.
AC A3GGB4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 78.
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=PICST_66436;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; AAVQ01000001; EAZ63901.2; -; Genomic_DNA.
DR RefSeq; XP_001387924.2; XM_001387887.1.
DR AlphaFoldDB; A3GGB4; -.
DR SMR; A3GGB4; -.
DR STRING; 4924.XP_001387924.2; -.
DR PRIDE; A3GGB4; -.
DR EnsemblFungi; EAZ63901; EAZ63901; PICST_66436.
DR GeneID; 4851313; -.
DR KEGG; pic:PICST_66436; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_2_1; -.
DR InParanoid; A3GGB4; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
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 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; 2.
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..839
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000366884"
FT DOMAIN 585..759
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 94929 MW; 939008DE60884FB8 CRC64;
MSRFFVAGYN SDSSSEEEDL LSSDEELLSS SSEGEQETSD DDSLDFDDQS DSDSSDSDSD
GRPSGPAYFL KKDFMKGGAG GDSDSDSEDE GRRVVKSAKD KLLDDMNESI EAINVARRSD
TWTTVVSEFD KLGRLLVRAG QQSVSTPNAY IRCLADLEDY ITATSENEKT EKSLNAAEAR
AFNMAKQRVR KQIKEYQAQY DLYRENPELF EREESVDIAA PSRSDVPVED TTGRVLSPVF
TILKQIAETR GKKNIDKYEQ IKTLEDLLND NLAKGSVFEL ISIYQMLLSI RFDASANQNF
MPIEQWKNNE ADLTSLIGLL ESNKDTYQLS ELGSTTDDID IEPVANESGV KAIFGSITSL
IDRLDDEFTR SLQNTDPHSI EYVQRLKDET TIYQLIVRGQ SYIESITPAE VQQSVEQLSR
VVLRRLEHIY YKPDQLIKAN EAEAWKGISH ESVIVSKDST PAELIEGLSS FLTKHKNPVY
AKHALLFSVY YYAVNNNYNR AKELFLDSQI FNKIHHADSS LQVQYNRAIV QLGLSAFRNG
AVEESHKVLN EIVNSQRSKE LLGQGFNSKY PNQATTVEKA KLLPFHQHIN LELLECVYST
CSLLIEIPAL AAATNSKDSR RKATTKSFKS KLEFHDRQFF TGPPESIKDH IVHASIALSK
GDWAKAYQLL SSIKIWKLFP DNDDLLAMMK NQLQVEGLRT YIFSYKSIFS KLSLGKLSQI
FELEADKVES IVQKMIETNE IGGTLDESKA FIQFASTEPQ RSRLQELAIV MNEKVGLLTE
KNEKTSSNGY GKKQPQQQQQ QQQQQQQQQQ QQKDLLQEDN SRFRYANVNT NNDEFQTTA
