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EIF3C_DICDI
ID   EIF3C_DICDI             Reviewed;         936 AA.
AC   Q54X97;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=eif3C; Synonyms=eif3s8; ORFNames=DDB_G0279109;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000027; EAL67893.1; -; Genomic_DNA.
DR   RefSeq; XP_641870.1; XM_636778.1.
DR   AlphaFoldDB; Q54X97; -.
DR   SMR; Q54X97; -.
DR   STRING; 44689.DDB0233926; -.
DR   PaxDb; Q54X97; -.
DR   EnsemblProtists; EAL67893; EAL67893; DDB_G0279109.
DR   GeneID; 8621876; -.
DR   KEGG; ddi:DDB_G0279109; -.
DR   dictyBase; DDB_G0279109; eif3C.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; Q54X97; -.
DR   OMA; VVMHRSE; -.
DR   PhylomeDB; Q54X97; -.
DR   Reactome; R-DDI-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-DDI-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-DDI-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-DDI-72702; Ribosomal scanning and start codon recognition.
DR   PRO; PR:Q54X97; -.
DR   Proteomes; UP000002195; Chromosome 3.
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:dictyBase.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:dictyBase.
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..936
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000330330"
FT   DOMAIN          643..814
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..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..936
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        169..187
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..258
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..860
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..882
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   936 AA;  106690 MW;  9E15FC9BFC89F9BC CRC64;
     MSRFYRQGSS SESSSESSSD SDVQVKKPTR YVSSSEDEIE EKRIVLSAKD KIWQQFDESL
     KKVRNALKTN DWVSTTSEFD NMTKLITNGK TTRIIEKEGF PPSFIKALFI IQTSHRDLTT
     EQKKKLHANN NKSYNSIKQK LKKTCDLYAK ELKPYHDNPA LVNEQENKAN SDDDDDDLSE
     SESEESESSD DDKGKGKGKA AFGKKPATKA VVAKKPLTKK GDDDSESESE ESESESEELI
     SESWSSDSDD DSDSDSDDDS GDNKWMIKDD KKVVAKASVT TVRKTDKDKL DRRNAVVSPL
     SGSGSAVPTA GEGEGEKLTQ DQIMKKVKEV ISNRGKLKTD PMKQIQQLEY FYSLIQGDKE
     TFIVLYELIA AQFDTASVKV ALSIPVWQKV ADGIKKLLEI LETNTNFVLV LEHQEPTISK
     GQVAVTGNLL ALFEMLDDEF SKSLQSINYP TKEYLDRLQD EQIILDLGES LQKYYESAGN
     NGAAAKIAIR RIEHIYYKSS NLKNNIIPST MPLSEQITLM SKLSSFVYKF GDERLNARTI
     LCNIYFNAIN NKFHEARDMM LMSHLQDNPT LMDVSTQILF NRAMVQLGLC AFRCGYIQEA
     QNCVVEFSGL RKDLLAQGLS VQSKTAEKDT VREVEETTRI LPAHMWIPID LIETVNLISG
     MLIAVPQNAY RPFDNKFKTC KFYQRHMDSV DRQIFIAPSE TSKDIIYQAS KALSAGDWQQ
     CLEHVNTLRF WSLIPDIDSV REKLTRIVQE VSLKTFLFTY STSYDSILLS ELADRFHLPK
     SQVHSIVAKM MNNHEISASM EHSTESITFR AEQTKLQYLA LHYSESLVDF VEQNERIYDV
     KFGTSYRKKG DNDHLPIAGG QHHGHQHHGH QHHGHHHHNQ QQQQHHQQQQ QTTQHHHHHH
     QNQNQGNQQY QNKKHHNSNQ QKSHKKRQNN SLVVNN
 
 
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