EIF3D_SCHPO
ID EIF3D_SCHPO Reviewed; 567 AA.
AC O94236;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003};
DE Short=eIF3d {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=Microtubule-destabilizing protein moe1;
GN Name=moe1; Synonyms=eif3d; ORFNames=SPAC637.07;
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 [GENOMIC DNA], INTERACTION WITH SCD1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9892665; DOI=10.1073/pnas.96.2.517;
RA Chen C.-R., Li Y.-C., Chen J., Hou M.-C., Papadaki P., Chang E.C.;
RT "Moe1, a conserved protein in Schizosaccharomyces pombe, interacts with a
RT Ras effector, Scd1, to affect proper spindle formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:517-522(1999).
RN [2]
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 [3]
RP FUNCTION, INTERACTION WITH SUM1, ASSOCIATION WITH THE 40S RIBOSOMAL
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=11705997; DOI=10.1074/jbc.m107790200;
RA Bandyopadhyay A., Lakshmanan V., Matsumoto T., Chang E.C., Maitra U.;
RT "Moe1 and spInt6, the fission yeast homologues of mammalian translation
RT initiation factor 3 subunits p66 (eIF3d) and p48 (eIF3e), respectively, are
RT required for stable association of eIF3 subunits.";
RL J. Biol. Chem. 277:2360-2367(2002).
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).
CC -!- FUNCTION: mRNA cap-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. In the
CC eIF-3 complex, eif3d specifically recognizes and binds the 7-
CC methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_03003, ECO:0000269|PubMed:11705997}.
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_03003,
CC ECO:0000269|PubMed:15904532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003,
CC ECO:0000269|PubMed:9892665}.
CC -!- DOMAIN: The RNA gate region regulates mRNA cap recognition to prevent
CC promiscuous mRNA-binding before assembly of eif3d into the full
CC eukaryotic translation initiation factor 3 (eIF-3) complex.
CC {ECO:0000255|HAMAP-Rule:MF_03003}.
CC -!- DISRUPTION PHENOTYPE: Reduced rate of protein synthesis, although the
CC polyribosome content is not affected. Enhanced sensitivity to caffeine
CC and defective spore formation. {ECO:0000269|PubMed:11705997}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit D family. {ECO:0000255|HAMAP-
CC Rule:MF_03003}.
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DR EMBL; AF038568; AAD08893.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA22586.1; -; Genomic_DNA.
DR PIR; T43555; T43555.
DR RefSeq; NP_594625.1; NM_001020053.2.
DR AlphaFoldDB; O94236; -.
DR SMR; O94236; -.
DR IntAct; O94236; 1.
DR MINT; O94236; -.
DR STRING; 4896.SPAC637.07.1; -.
DR iPTMnet; O94236; -.
DR MaxQB; O94236; -.
DR PaxDb; O94236; -.
DR PRIDE; O94236; -.
DR GeneID; 2543412; -.
DR KEGG; spo:SPAC637.07; -.
DR PomBase; SPAC637.07; moe1.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR InParanoid; O94236; -.
DR PhylomeDB; O94236; -.
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:O94236; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; 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; 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:0098808; F:mRNA cap binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0002191; P:cap-dependent translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:PomBase.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR HAMAP; MF_03003; eIF3d; 1.
DR InterPro; IPR007783; eIF3d.
DR PANTHER; PTHR12399; PTHR12399; 1.
DR Pfam; PF05091; eIF-3_zeta; 1.
DR PIRSF; PIRSF016281; EIF-3_zeta; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT CHAIN 1..567
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D"
FT /id="PRO_0000123524"
FT REGION 12..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..314
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT CONFLICT 367
FT /note="Q -> E (in Ref. 2; CAA22586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 62636 MW; 5C382CA754A747D1 CRC64;
MATGFKLPEL APVKSAWGPP ETEQIGGDIP YAPFSKGDRL GKIADWSVDQ PKDGREQRGR
QGAFAGRFRD QYQTYGYGAS SIFGYQHSED ESSFSVIDRG SVNRTRTSAR NGGTLLKVRG
RGQNVQRGGR GGRYGSSGGR GAGDTVVSRS SGAGGARGRR FGWKDYDKHQ RLRNASVTVG
DDWQLLDEVE FSHLSKLNLA AAAPVTVDSY GYIYPYDKSF DKIHVKSEKP LQALDRVHYN
PTTTEDPVIQ KLALNSDANI FITDSILSLL MCSTRSVYPW DIVITHQSGK LFFDKREGGP
FDYLTVNENA YDSPMDADNR EGVNSPGALS VEATYINQNF CVQALRETEE EKYKLPHPNP
FYNSKEQSEP LAAHGYIYRD VDLSLETDEK PVKLMVRTEV DGYVKNPAND VQYISIKALN
EYDPKFTNVT GSVDWRSKLE SQRGAVFATE MKNNSCKLAR WTVEALLAGV DSMKVGFVSR
SNARDAQHHG ILGVVAYKPA DLASQMNLSL SNGWGIVRTI ADVCLKMPDG KYVLVKDPNR
PILRLYSVPP NTFEEAAGPS LEASSTA
