EIF3C_SCHPO
ID EIF3C_SCHPO Reviewed; 918 AA.
AC O14164; O13885; P78791; Q9P6P4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 146.
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; Synonyms=eif3c, tif33;
GN ORFNames=SPAC1E11.01c, SPAC4A8.16c, SPAC823.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 571-918.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11134033; DOI=10.1074/jbc.m010188200;
RA Akiyoshi Y., Clayton J., Phan L., Yamamoto M., Hinnebusch A.G.,
RA Watanabe Y., Asano K.;
RT "Fission yeast homolog of murine Int-6 protein, encoded by mouse mammary
RT tumor virus integration site, is associated with the conserved core
RT subunits of eukaryotic translation initiation factor 3.";
RL J. Biol. Chem. 276:10056-10062(2001).
RN [4]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15904532; DOI=10.1186/1741-7007-3-14;
RA Zhou C., Arslan F., Wee S., Krishnan S., Ivanov A.R., Oliva A.,
RA Leatherwood J., Wolf D.A.;
RT "PCI proteins eIF3e and eIF3m define distinct translation initiation factor
RT 3 complexes.";
RL BMC Biol. 3:14-14(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12; SER-16; SER-19;
RP SER-20 AND THR-667, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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. The eIF-3 complex appears to include tif32/eif3a,
CC SPAC25G10.08/eif3b, tif33/eif3c, SPBC4C3.07/eif3f, tif35/eif3g and
CC sum1/eif3i. This set of common subunits may also associate exclusively
CC with either moe1/eif3d and int6/eif3e, or with SPAC821.05/eif3h and
CC SPAC1751.03/eif3m. The eIF-3 complex may also include
CC SPAC3A12.13c/eif3j. {ECO:0000255|HAMAP-Rule:MF_03002,
CC ECO:0000269|PubMed:11134033, ECO:0000269|PubMed:15904532}.
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; CU329670; CAB11485.1; -; Genomic_DNA.
DR EMBL; Z98599; CAB11250.2; -; Genomic_DNA.
DR EMBL; D89140; BAA13802.1; -; mRNA.
DR PIR; T38786; T38786.
DR PIR; T42417; T42417.
DR RefSeq; NP_593828.2; NM_001019257.2.
DR AlphaFoldDB; O14164; -.
DR SMR; O14164; -.
DR BioGRID; 280035; 8.
DR STRING; 4896.SPAC4A8.16c.1; -.
DR iPTMnet; O14164; -.
DR MaxQB; O14164; -.
DR PaxDb; O14164; -.
DR PRIDE; O14164; -.
DR EnsemblFungi; SPAC4A8.16c.1; SPAC4A8.16c.1:pep; SPAC4A8.16c.
DR GeneID; 2543621; -.
DR KEGG; spo:SPAC4A8.16c; -.
DR PomBase; SPAC4A8.16c; -.
DR VEuPathDB; FungiDB:SPAC4A8.16c; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_2_1; -.
DR InParanoid; O14164; -.
DR OMA; VVMHRSE; -.
DR PhylomeDB; O14164; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
DR Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SPO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:O14164; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IC:PomBase.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:PomBase.
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 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..918
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000123529"
FT DOMAIN 681..856
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..64
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..128
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 667
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT ECO:0000269|PubMed:18257517"
FT CONFLICT 683
FT /note="M -> I (in Ref. 2; BAA13802)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 918 AA; 104367 MW; 43B70599409688EF CRC64;
MSRFFKGGSS DSDAESVDSS EENRLTSSRL KKQDDSSSEE ESSEEESASS SESESSEEES
ESEESEVEVP KKKAVAASED SESDSESSEE EEETESEEDS EVSDESESES ESESESEEES
ESEEESDESE RSGPSSFLKK PEKEEAKPAG LKFLRGESSE ESSDEEEGRR VVKSAKDKRY
EEFISCMETI KNAMSSNNWI VVSNEFDHLN KVSQKCKEAG RNPPPYIEFL SALDQKLESA
DKAFIKSLDA ANGRAFNALK QRVRKNNRQF QSDIDRYRKD PEGFMKPAEL NEIPKPAGKA
GQDEVIVDGV ATRGIVAPTE GLGKPEEITP ADIFKYLRAI FEARGKKSTD RSEQIRLLEK
LSTIAVTDYQ RLRVKVALLA VRFDINTGSG QYMPIDQWNA ALTELHSILD IFDANPKIVI
VEQVEDENEE EEEAIAAAEN NNGVIQVQGS VVSFLERLDD EFTRSLQMID PHTPEYIDRL
KDETSLYTLL VRSQGYLERI GVVENTARLI MRRLDRVYYK PEQVIRANEE VAWRSFPPTF
DLTITPRATT TTPDILIHSL CVYLYNNGVS LLRTRAMLCH IYHEALQNRF YKARDMLLMS
HLQDSVHAAD IATQILHNRT MVQIGLCAFR NGMVQETQYA LQDISTTGRV KELLGQGIQA
PKFGQFTPDQ DRLDKQLVLP FHMHINLELL ECVYLTCSML MEIPAMAAAS STASDSRKRV
ISRPFRRMLE YIDRQLFVGP PENTREYIMQ ASKALADGEW RRCEEFIHAI KIWSLMPDAD
KIKQMLSEKI REEGLRTYLL AYAAFYDSVS LEFLATTFDL PVQRVTVIVS RLLSKREIHA
ALDQVHGAII FERVEINKLE SLTVSLSEKT AQLNEANEKL YEQKTQHTNP QENRRRDKGG
SVKRRNERTE NRNRSDMN
