EIF3A_SCHPO
ID EIF3A_SCHPO Reviewed; 932 AA.
AC O74760; P78924;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 110 kDa subunit;
DE Short=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Translation initiation factor eIF3, p110 subunit;
GN Name=tif32; Synonyms=eif3a; ORFNames=SPBC17D11.05;
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 447-746.
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-374; SER-501; SER-874;
RP SER-875 AND SER-877, 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: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S 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_03000}.
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_03000,
CC ECO:0000269|PubMed:11134033, ECO:0000269|PubMed:15904532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAA21076.1; -; Genomic_DNA.
DR EMBL; D89275; BAA13936.1; -; mRNA.
DR PIR; T39716; T39716.
DR PIR; T43205; T43205.
DR RefSeq; NP_596379.1; NM_001022300.2.
DR AlphaFoldDB; O74760; -.
DR SMR; O74760; -.
DR BioGRID; 276482; 19.
DR IntAct; O74760; 1.
DR MINT; O74760; -.
DR STRING; 4896.SPBC17D11.05.1; -.
DR iPTMnet; O74760; -.
DR MaxQB; O74760; -.
DR PaxDb; O74760; -.
DR PRIDE; O74760; -.
DR EnsemblFungi; SPBC17D11.05.1; SPBC17D11.05.1:pep; SPBC17D11.05.
DR GeneID; 2539938; -.
DR KEGG; spo:SPBC17D11.05; -.
DR PomBase; SPBC17D11.05; tif32.
DR VEuPathDB; FungiDB:SPBC17D11.05; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; O74760; -.
DR OMA; VMYQTTA; -.
DR PhylomeDB; O74760; -.
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:O74760; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA: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; IDA:PomBase.
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:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..932
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000123543"
FT DOMAIN 309..492
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 793..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 537..862
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 793..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:18257517"
FT CONFLICT 569
FT /note="L -> I (in Ref. 2; BAA13936)"
FT /evidence="ECO:0000305"
FT CONFLICT 609..610
FT /note="NK -> DE (in Ref. 2; BAA13936)"
FT /evidence="ECO:0000305"
FT CONFLICT 726..746
FT /note="KHEQAIKDKKAFAQFASYIHA -> TSVLLPLMLRCLNDNYVKLLF (in
FT Ref. 2; BAA13936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 932 AA; 107071 MW; 120EEDBC5C43DBC9 CRC64;
MAPPQGKPEN VLRLADELIA LDQHSSALQS LHETIVLKRS RNAQGFSLEP IMMRFIELCV
HLRKGKIAKE GLYTYKNAVQ NTSVTAIENV VKHFIELANK RVQEAQEKAD KISVEYVDDL
EATETPESIM MSLVSGDLSK SRTDRALVTP WLKFLWDAYR TVLDILRNNA RLEVMYQLIA
NSAFQFCLKY QRKTEFRRLC ELLRSHLGNA SKFSNAPHSI NLNDAETMQR HLDMRFSQLN
VAVELELWQE AFRSIEDIHS LLTFSKRAPA AVMLGNYYRK LIKIFLVCDN YLLHAAAWNR
YFTFTNVQKP ATANFVILSA LSIPIIDANK LSGPSIEAED AKSKNARLAL LLNLSKTPTR
ETLIKDAISR GVLSFCDQAI RDLYQILEVE FHPLSICKKL QPIIKRLAES NDTAQYIRPL
QQVILTRLFQ QLSQVYDSIS LKYVMDLATF EEPYDFNPGQ IEKFIMNGNK KGAFSIRLNH
IENSISFSSD LFSNPIKSSD SVSLQSTPSE LITSQLTRIA KSLSSVLMRF DTDFCLLRKQ
QAEAAYERAQ AGVEQERKAV IAQRSLLELR RGQADTLATQ REAELAAQRA LKQKQESEAE
SLRVQEEINK RNAERIRREK EAIRINEAKK LAEELKAKGG LEVNAEDLEH LDADKLRAMQ
IEQVEKQNKS MNERLRVIGK RIDHLERAYR REAIPLWEED AKQQAEHDRE IFYEREKQRK
EVQERKHEQA IKDKKAFAQF ASYIHAYKQN IDDERDKAYQ EAYAKAKNVI DAERERQRKE
IFEQKLAEAI REAEEEAARA AEEEANRELH EQEEAQKRAI EERTRAAREA KEREQREMAE
KLERQRRIQQ ERDEEISRKL AEKAAARRAN IGASSPSPGA WRRGGASAGG VSRDSPRYSR
GGYSRGSVPP RETLAPSKGA YVPPSRRNQQ QQ
