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EIF3A_KLULA
ID   EIF3A_KLULA             Reviewed;         925 AA.
AC   Q6CT90;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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 homolog {ECO:0000255|HAMAP-Rule:MF_03000};
DE            Short=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03000};
DE   AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
GN   Name=TIF32 {ECO:0000255|HAMAP-Rule:MF_03000};
GN   OrderedLocusNames=KLLA0C14498g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC       Rule:MF_03000}.
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DR   EMBL; CR382123; CAH01700.1; -; Genomic_DNA.
DR   RefSeq; XP_452849.1; XM_452849.1.
DR   AlphaFoldDB; Q6CT90; -.
DR   SMR; Q6CT90; -.
DR   STRING; 28985.XP_452849.1; -.
DR   PRIDE; Q6CT90; -.
DR   EnsemblFungi; CAH01700; CAH01700; KLLA0_C14498g.
DR   GeneID; 2892152; -.
DR   KEGG; kla:KLLA0_C14498g; -.
DR   eggNOG; KOG2072; Eukaryota.
DR   HOGENOM; CLU_002096_2_1_1; -.
DR   InParanoid; Q6CT90; -.
DR   OMA; VMYQTTA; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0002188; P:translation reinitiation; IEA:EnsemblFungi.
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   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..925
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   A"
FT                   /id="PRO_0000366363"
FT   DOMAIN          324..498
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          108..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          534..666
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          785..885
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COMPBIAS        514..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..880
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   925 AA;  107109 MW;  5B99CBD1FEE769D0 CRC64;
     MAPPALRPEN AIRRADELVS VGEPMAALQS LFDLLSSRRS RFADAATLEP IIFKFLELGV
     ELRKGKMIKE GLYQYKKHMQ HTPEGLISVG AVARKFIDLI ETKMTNIQAQ TDAKEESNKD
     QAEEDLEGGV TPENLLVSVY EQEQTVGGFN NDDVSAWLRF TWESYRTTLD FLRNNSQLEI
     TYAGVVNRTM QFCYKYNRKN EFKRLAEMLR QHLDAANYQQ QRYGHHTVDL SDPDTLQRYS
     DQRFQQVNVS VKLELWHEAF RSIEDVHHLM RLSKRAPKPS VLANYYENLA KIFFVSGNYL
     LHAAAWEKFY NLYLKNPNAS EEDFKFYSSQ FVLSALAIQL DDLPIAGFDP QIRLCDLLDL
     ESKPKRKDLI TAAGEQQVVE KADADILKFF NILETNFDVK SAKSQLSALL PNLVEKPYFA
     QYVAPLRNLF IRRSIIEVSK AQTSIHLVEL HEMLSLPAPF ELSVFELEKY LIQAAMDDYV
     SISIDHETDT VSFAQDPFDA WQASLVEVPE SSTSDEAKNS ESEEETSQET HADEEQNEQV
     FTRNSEVRSK LTDLSKILKA NEEYENGSYY YRVKLVREEL IRRKEEVIKL EKEAAEIRAK
     SNAERKKRSE EENKILAKKA LEERQRRMAE EKAAVESSME KEAERRAEEM MEREREAIHE
     QEMKKLIAET NANGVIHIDP KEAKNLTSDK INQMVIEQVA KNKKDLTERM TYAFKKLDHL
     ERAYRQMELP LLEKDAEEQK KRDRENYDNF KKKLIETSKA DYEKKLALHQ RLNKIYSTFN
     QYKSSVIAEK KEELEKQRAL KEAQLEEAKK QRIEQVRKER YEAKVAEIQA AIEAEAAEKE
     ALAKEEELAK RRAERERINK ERDEIARKQR EIEELLEKKN GSSRSSPVPS TPTPAPAPAQ
     TAPVSNKPMS MAEKLRLKRM NAGRG
 
 
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