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EIF3C_ANOGA
ID   EIF3C_ANOGA             Reviewed;         955 AA.
AC   Q7PMU8;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 3.
DT   03-AUG-2022, entry version 109.
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=AGAP004725;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
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; AAAB01008968; EAA13192.4; -; Genomic_DNA.
DR   RefSeq; XP_318103.3; XM_318103.4.
DR   AlphaFoldDB; Q7PMU8; -.
DR   SMR; Q7PMU8; -.
DR   STRING; 7165.AGAP004725-PA; -.
DR   PaxDb; Q7PMU8; -.
DR   PRIDE; Q7PMU8; -.
DR   GeneID; 1278503; -.
DR   KEGG; aga:AgaP_AGAP004725; -.
DR   CTD; 1278503; -.
DR   VEuPathDB; VectorBase:AGAP004725; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_0_1; -.
DR   InParanoid; Q7PMU8; -.
DR   OMA; VVMHRSE; -.
DR   OrthoDB; 273138at2759; -.
DR   PhylomeDB; Q7PMU8; -.
DR   Proteomes; UP000007062; Chromosome 2L.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; 1.
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..955
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000365382"
FT   DOMAIN          658..834
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..178
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..955
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   955 AA;  111573 MW;  78925E500E0B2698 CRC64;
     MSRFFAGGSD SDSDSSSDSE PVIRQQVAQF TFSDEEEDVK RVVRSKKEKR YEDLSNIIKS
     IRNHKKIKDM SSVLTSFEEF MRAYTKALPV VMKEENGVTP RIVVRALAEL EDFVNESWDD
     KESRKNLSKN NNKALGTLRQ KFRKYIKDFE SDMKRFRAAP EDFAEEEEDD EREDEKGSDE
     EEEKVVVQVE PKAVSFKKEP EKAKPVKPVA DSDSSDWGSD SDSDSTSSDE DAKYTSIRDR
     FLKKPEKGTE EIASAPSGVS GDDAFKKEKK KKTGEALSKK KKPKQDEMFD ENEEEEEGWK
     VVNGTRSGAS EQPKMFAKDA EIDTKLVVNK LNEVMAARGK KRTDRKMQIE FLRELRTVAE
     TNNLGPAVAV KIRFNIVSAI FDYNPKVSGA MKLEHWSKLL EEIQELLKLL LAHEDVHLSE
     SILDEYEEYD TAPFKIRGCM LTAVERLDDE FTKLLKECDP HSNEYVDRLK DEVPVTNIIE
     QVVTYVERLG NEMEICRIYL RKIDHLYYKF DPDVLKKRKG QLPANTITSV EEMDKLCRYI
     YAKDQTDRLR TRAILSHIFH HALHDNWFQA RDLVLMSHLQ ETIHHSDPAT QILYNRMMAN
     LGLCAFRHGN IKDAHLCLVD LMMTGKPKEL LAQGLVPQRQ HERSLEQEKI EKQRQMPFHM
     HINLELLECV YLVSAMLLEI PYMAAHEFDA RRRMISKTFY QQLRSSERQS LVGPPESMRE
     HVVAAAKAMR HGDWNACANF IVNKKMNVKV WDLFYEANRV REMMIKFIKE ESLRTYLFTY
     SNVFASISVP HLADMFKLPK SKVHSLISKM IINEELMASL DDPTETIVMH RSEPSRLQAL
     SMQLADKVTN LVDANERIFE MKQGNFFQRG GNQGYNRDRQ NYRNQNQNQN WNNNRRQDNR
     NRGNRGNQNR GEGREQREHH RDHHRDQREH REHQNREFRE QREQMRNVEY QNKAE
 
 
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