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EIF3C_CULQU
ID   EIF3C_CULQU             Reviewed;         904 AA.
AC   B0W0S3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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 subunit 8 {ECO:0000255|HAMAP-Rule:MF_03002};
GN   Name=eIF3-S8 {ECO:0000255|HAMAP-Rule:MF_03002}; ORFNames=CPIJ000742;
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB;
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA   Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_03002}.
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; DS231818; EDS41375.1; -; Genomic_DNA.
DR   RefSeq; XP_001842307.1; XM_001842255.1.
DR   AlphaFoldDB; B0W0S3; -.
DR   SMR; B0W0S3; -.
DR   STRING; 7176.CPIJ000742-PA; -.
DR   GeneID; 6031517; -.
DR   KEGG; cqu:CpipJ_CPIJ000742; -.
DR   VEuPathDB; VectorBase:CPIJ000742; -.
DR   VEuPathDB; VectorBase:CQUJHB010886; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_0_1; -.
DR   InParanoid; B0W0S3; -.
DR   OMA; VVMHRSE; -.
DR   OrthoDB; 273138at2759; -.
DR   PhylomeDB; B0W0S3; -.
DR   Proteomes; UP000002320; Partially assembled WGS sequence.
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:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13937; PTHR13937; 1.
DR   Pfam; PF05470; eIF-3c_N; 2.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..904
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000365384"
FT   DOMAIN          636..812
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..182
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..229
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..870
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  105521 MW;  C9D18A195709DB1A CRC64;
     MSRFFAGGSE SDSDSSSDSE PIQRQTAPQF TFSDEEEDVK RVVRSTKEKR YEDLSNIIKS
     IRNYKKIKDM SSLLSSFEDL TRAYAKALPV ITKEENGVCP RFIIRALAEL EDFINEVWDD
     REGRKNLSKN NSKSLGALRQ KFRKYIKDFD SDLKKFRESP DAADDEDEEE EKKEEEESDD
     EEAAVVPAAK AVSFKKDTVE KVKVEKDDDD SDDSIDWGQD SDSDESSSEE EAYGANIRER
     FLKRPEKEDG DDGEKKKEKK KTKETKDSRK KKRVEDDDDE GWESSATSEK PKMFAKDAEI
     DVALVVNKLN EVMAARGKKR TDRKLQIEFL RELRAISEEK KLGAAVAAKI RFNIVSAIFD
     YNPKVSEPMK LEHWSKLLEE IQALIKLLLA NEDIVLSENI LDENEEYDTA PYKIRGCMLT
     AVERLDDEFT KLLKECDPHS NEYVDRLKDE VTVTNVIEQV VQYVERLGNE METCRIYLRK
     IDHLYYKFDP NVLKKRKAQL PASSLTSVDE MERLCRFIYA KDQTDRLRTR AILSHIFHHA
     LHDNWFQARD LVLMSHLQET IHHSDPPTQI LYNRTMANLG LCAFRHGNIK DAHQCLVDLM
     MTGKPKELLA QGLVPQRQNE RSLEQEKVEK QRQMPFHMHI NLELLECVYL VSAMLLEIPY
     MAAHEFDARR RMISKTFYQQ LRSSERQSLV GPPESMREHV VAAAKAMRHG DWQACSNFIV
     NKKMNVKVWD LFYEADRVRE MLAKFIKEEA LRTYLFTYSN VYASISVPYL AEMFDLPKSK
     VHSLISKMII NEELMASLDD PTETVVLHRS EPSRLQALSM QLADKVTNLV DSNERVFEMK
     QGNFFQRGGN QGYNRDRQNY RNQNQNRENW NNNRRQDRGN RNRNQNRDRE QREQHRVEFE
     EKAE
 
 
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