ID V8PF84_OPHHA Unreviewed; 1322 AA.
AC V8PF84;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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 ECO:0000313|EMBL:ETE72673.1};
GN Synonyms=EIF3S8 {ECO:0000256|HAMAP-Rule:MF_03002};
GN ORFNames=L345_01468 {ECO:0000313|EMBL:ETE72673.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE72673.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE72673.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE72673.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE72673.1}.
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DR EMBL; AZIM01000190; ETE72673.1; -; Genomic_DNA.
DR Proteomes; UP000018936; Unassembled 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.20.20.220; -; 2.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR002872; Proline_DH_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; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF01619; Pro_dh; 2.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 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}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT DOMAIN 666..848
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 151274 MW; 3CB0FA143F1EBB0C CRC64;
MSRFFTTGSD SESESSLSGD ELVTKPVGGN FGKQPLLLSE DEEDTKRVVR SAKDKRFEEL
TNLIKTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPHFYIRIL ADLEDYLNEL
WEDKEGKKKM NKNNAKALST LRQKIRKYNR DYETQITAYR QNPELSADED EDKKSDDSEG
SSSSSEDDDD EGISAAAFLK KKEGAVESRS KFLKKIEDED EEEEESDDED WGSSDSESDS
ESDEDEGKYT SLASKFLKKV GTEEEKRILE KKKEDKAKKK QDRKSKKYED DEDDNEGGEW
EKVKGGVPLV KEKPKMFAKG TEINHAVVVK KLNEILQARG KKGTDRAAQI DLLQLLVGIA
AENNLGIAID LKIKFNIVAS LYDYNPNLAT YMKKCLSSID ELLDILFAHD NIFIGQNIAE
DSENLANAEQ PLRIRGCILT LVERMDEEFV KIMQNTDPHS QEYVDHLKDE ARVCKIIERV
QTYLQDKGTT DEICRVYLRC ILHTYYKFDY KAHQRQQGPA GDSKSEQDQA ENEGEDSAVL
MERLCKFIYA KDRTDRIRTC AILCHIYHHA LHDRWYQARD LMLMSHLQDN IQHADPPVQI
LYNRTMVQLG ICAFRQGLIK DAHNALLDIQ SSGRAKELLG QGLLMRSMQE RNQEQEKIEK
RRQVPFHMHI NLELLECVYL VSAMLLEIPY MAAHEFDARR RMISKQFHHQ LRVGERQPLL
GPPESMREHV VAASKAMKMG DWKTCHRFIV NEKMNGKVWD LFPEADKVRS MLVRSVARKL
KIQEESLRTY LFTYSSVYDS ISMEILSDMF ELDLPTVHSI ISKMIINEEL MASLDQPTQT
VVMHRTEPTT QQNLALQLAE KLGSLVENNE RVFDQKQGTY GGYFRVPPNQ LVSYLADQKD
GYRKNEGGYL RRGGYRQQEL PETASKKPQS SSSSLNLDDG KVFRLKTKWE LSRGLLVFFL
CSSPWLVQKA PKLLSFTRHI LGRRLWTSAL RLTLYGQFVA GETHKEIKET LQRLQHLGVR
PLLAVPIEED VGEEKEGEGW YDKNAQSMIT CLDLSVGGAP NPMMQLKVTA LMAAELCKTI
TLCLQNKEGI SDLSIERVMA VMSGCEVSFS CLSQEENQHF QKSLRRLNSV AECAVEKGVR
VLVDAEYTYI NPALTLVTIA LMATWNTQKP WIWNTYQAYL KDTLERLKQD VALAERLGVC
FGIKLVRGAY LNKERKLAKE KGYPDPVQPS WEATNERMSQ MGINKNAGPI SFGQLLGMCD
QVSLALGQAG YAIYKSIPYG SVEEVIPYLI RRAHENQSVL LGIRKERDLL RLELWRRILR
RP
//
