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EIF3C_XENTR
ID   EIF3C_XENTR             Reviewed;         922 AA.
AC   Q6P1V4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
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=eif3c; Synonyms=eif3s8; ORFNames=TGas102o09.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2004) 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, 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_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; CR942354; CAJ83565.1; -; mRNA.
DR   EMBL; BC064857; AAH64857.1; -; mRNA.
DR   RefSeq; NP_989413.1; NM_204082.2.
DR   AlphaFoldDB; Q6P1V4; -.
DR   SMR; Q6P1V4; -.
DR   PaxDb; Q6P1V4; -.
DR   Ensembl; ENSXETT00000006431; ENSXETP00000006431; ENSXETG00000002941.
DR   GeneID; 395052; -.
DR   KEGG; xtr:395052; -.
DR   CTD; 8663; -.
DR   Xenbase; XB-GENE-5720067; eif3c.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_0_1; -.
DR   InParanoid; Q6P1V4; -.
DR   OMA; VVMHRSE; -.
DR   OrthoDB; 273138at2759; -.
DR   PhylomeDB; Q6P1V4; -.
DR   TreeFam; TF101520; -.
DR   Reactome; R-XTR-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-XTR-72649; Translation initiation complex formation.
DR   Reactome; R-XTR-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-XTR-72702; Ribosomal scanning and start codon recognition.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000002941; Expressed in neurula embryo and 22 other tissues.
DR   ExpressionAtlas; Q6P1V4; baseline.
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: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; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..922
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000365379"
FT   DOMAIN          674..850
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..922
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..185
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..242
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..911
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  106480 MW;  3F0970B2A6F2B002 CRC64;
     MSRFFATGSD SESESSLSGD EILPKPVGGT FGKQPIILSD DEEDTKRVVR SAKDKRFEEL
     TNLIKTIRNA MKIRDMTKCL EEFEQLGKAF IKAKNIVDKE GVPRFYIRLL SDLEDYLNEL
     WEDKEGKKKM NKNNAKALST LRQKLRKYNR DFEAPIAAYK QNPEESADED QEKDEDSEAS
     SSSDDDSDEG MSASKFLKKA DSAPPESRSK FLKKEEAEDE ESSSDDEDWG SDSDESDSDE
     SDDENKYTSM ASRFLKKTVN EGDRQAAEKK KEEKAKKKQH RKVKRKDEEG EEEEDDNEGG
     GEWEKVKGGV PLVKEKPKMF AKGTEITPPI VVKKLNEILQ ARGKKGTDRA AQIDLLHLLA
     GIAEENNLGQ GIAVKIKFNI VASLYDYNTN LATYMKADMW KKCLDSIHDL LDILFANSNM
     FIGEHISEDS ENLSNTDQPL RVRGCILTLI ERMDEEFTKI MQNTDPHSQE YVDNLKDEAR
     VCEVIERAQK YLQEKGSTEE VCRVYLRRIM HTYYKFDYKA HQRQLSTGQE SKSEQDQAEN
     EAEDSAILMD RLCKYIYAKD RTDRIRTCAI LCHIYHHALH NRWFQARDLM LMSHLQDNIQ
     HADPPVQILY NRTMVQLGIC AFRQGMIRDA HNALLDIQSS GRAKELLGQG LLMRTMQERN
     QEQEKIEKRR QIPFHMHINL ELLECVYLVS AMLLEIPYMA AHEFDARRRM ISKQFHHQLR
     VGERQPLLGP PESMREHVVA ASKAMKMGDW KTCKNFIINE KMNGKVWDLF PEAERVRSML
     IRKIQEESLR TYLFTYSSVY DSIRMGILGD MFQLEIPTVH SIISKMIINE ELMASLDQPT
     QTVVMHGTEP SSLQNTALQL AEKLGNLVEN NERIFDHKQG SYGGYFNRGD RGDRDQKDQY
     QRKEGGYMRR GYRRDQQGQS NY
 
 
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