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Database: UniProt
Entry: A0A1B8XV82_XENTR
LinkDB: A0A1B8XV82_XENTR
Original site: A0A1B8XV82_XENTR 
ID   A0A1B8XV82_XENTR        Unreviewed;       912 AA.
AC   A0A1B8XV82;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000256|HAMAP-Rule:MF_03002};
DE            Short=eIF3c {ECO:0000256|HAMAP-Rule:MF_03002};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000256|HAMAP-Rule:MF_03002};
GN   Name=EIF3C {ECO:0000256|HAMAP-Rule:MF_03002};
GN   Synonyms=EIF3S8 {ECO:0000256|HAMAP-Rule:MF_03002};
GN   ORFNames=XENTR_v900264382mg {ECO:0000313|EMBL:OCA14568.1};
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 {ECO:0000313|EMBL:OCA14568.1};
RN   [1] {ECO:0000313|EMBL:OCA14568.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nigerian {ECO:0000313|EMBL:OCA14568.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ottilar R., Schmutz J., Salamov A., Cheng J.F., Lucas S., Pitluck S.,
RA   Gundlach H., Guo Y., Haberer G., Nasrallah J., Mayer K.F.X.,
RA   van de Peer Y., Weigel D., Grigoriev I.V.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OCA14568.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|EMBL:OCA14568.1};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [3] {ECO:0000313|EMBL:OCA14568.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nigerian {ECO:0000313|EMBL:OCA14568.1};
RA   Sessions A., Jenkins J., Mitros T., Lyons J.T., Dichmann D.S., Robert J.,
RA   Harland R.M., Rokhsar D.S.;
RT   "WGS assembly of Xenopus tropicalis.";
RL   Submitted (MAY-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_03002}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC       Rule:MF_03002}.
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DR   EMBL; KV461452; OCA14568.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8XV82; -.
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; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR   PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR   Pfam; PF05470; eIF-3c_N; 2.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03002};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_03002};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_03002}.
FT   DOMAIN          674..850
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          1..36
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   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"
SQ   SEQUENCE   912 AA;  104989 MW;  BBA6114489E64B4F 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 RGDRGKCTLT
     RRISTRGKRA DT
//
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