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EIF3D_DANRE
ID   EIF3D_DANRE             Reviewed;         552 AA.
AC   Q6TH15; A2BHH8; Q7T353;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=Eukaryotic translation initiation factor 3 subunit 7 {ECO:0000255|HAMAP-Rule:MF_03003};
GN   Name=eif3d; Synonyms=eif3s7; ORFNames=si:dkey-165I8.6;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA   Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA   Hopkins N.;
RT   "Identification of 315 genes essential for early zebrafish development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney marrow;
RX   PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA   Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA   Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA   Look A.T., Chen Z.;
RT   "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is composed of 13 subunits: eif3a, eif3b, eif3c,
CC       eif3d, eif3e, eif3f, eif3g, eif3h, eif3i, eif3j, eif3k, eif3l and
CC       eif3m. {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
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   -!- SIMILARITY: Belongs to the eIF-3 subunit D family. {ECO:0000255|HAMAP-
CC       Rule:MF_03003}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM15128.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY648769; AAT68087.1; -; mRNA.
DR   EMBL; AY398341; AAQ97774.1; -; mRNA.
DR   EMBL; BX571960; CAM15128.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC053250; AAH53250.1; -; mRNA.
DR   RefSeq; NP_956310.1; NM_200016.1.
DR   AlphaFoldDB; Q6TH15; -.
DR   SMR; Q6TH15; -.
DR   STRING; 7955.ENSDARP00000011011; -.
DR   PaxDb; Q6TH15; -.
DR   PRIDE; Q6TH15; -.
DR   Ensembl; ENSDART00000011052; ENSDARP00000011011; ENSDARG00000021257.
DR   GeneID; 336498; -.
DR   KEGG; dre:336498; -.
DR   CTD; 8664; -.
DR   ZFIN; ZDB-GENE-030131-8442; eif3d.
DR   eggNOG; KOG2479; Eukaryota.
DR   GeneTree; ENSGT00390000002667; -.
DR   InParanoid; Q6TH15; -.
DR   OrthoDB; 1030308at2759; -.
DR   PhylomeDB; Q6TH15; -.
DR   TreeFam; TF101519; -.
DR   Reactome; R-DRE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-DRE-72649; Translation initiation complex formation.
DR   Reactome; R-DRE-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-DRE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-DRE-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-DRE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   PRO; PR:Q6TH15; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 3.
DR   Bgee; ENSDARG00000021257; Expressed in somite and 29 other tissues.
DR   ExpressionAtlas; Q6TH15; baseline and differential.
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; ISS:UniProtKB.
DR   GO; GO:0098808; F:mRNA cap binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0002191; P:cap-dependent translational initiation; ISS:UniProtKB.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..552
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D"
FT                   /id="PRO_0000364134"
FT   REGION          288..302
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   REGION          525..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..552
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        155..156
FT                   /note="Missing (in Ref. 3; CAM15128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        505
FT                   /note="E -> D (in Ref. 4; AAH53250)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   552 AA;  64090 MW;  C22F811A41D56177 CRC64;
     MAKFHAPVIQ DNPSGWGPCA VPEKFKDMPY QPFSKGDRLG KVADWTGATY QDKRYTNKYS
     SQFGGGSQYA YFHEEDEASF QLVDTAKTQK TAYQRNRMRF AQRNLRRDKD RRTLTQFNMQ
     TLPKSAKQKE RDRMRLQKKF QKQFGVRQKW DQKSQAQLKP RDSSVEVRSD WEVKEEMDFP
     RLMKMRYMDV ADPLDIECCG ALEHYDKAFD RITTRNEKPL KSIKRIFHTV TTTDDPVIRK
     LAKTQGNVFA TDAILATLMC CTRSVNSWDI IVQRVGNKLF FDKRDNSDFD LLTVSETANE
     PPQDEGSSLN SPRNLAMEAT YINHNFSQQC LRMGGERYKF PNPNPFVEED TEKSEVASVA
     YRYRRWKLGE DIDLIVRCEH DGVMTGANGE VSFINVKTLN EWDSRYCNGV DWRQKLDSQR
     GAVLATELKN NSYKLARWTC CAILAGSEYL KLGYVSRYHV KDSSRHVVLG TQQFKPNEFA
     SQINLSMENA WGILRCVIDI CRKLEEGKYL ILKDPNKQVI RVYSLPDGTF SSDEDEEEDD
     EDEEDEEEDE DN
 
 
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