ID A0A3Q0FX45_ALLSI Unreviewed; 1127 AA.
AC A0A3Q0FX45;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=LOC102379089 {ECO:0000313|RefSeq:XP_025050730.1};
GN Synonyms=EIF3C {ECO:0000256|HAMAP-Rule:MF_03002}, EIF3S8
GN {ECO:0000256|HAMAP-Rule:MF_03002};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025050730.1};
RN [1] {ECO:0000313|RefSeq:XP_025050730.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the battenin family.
CC {ECO:0000256|ARBA:ARBA00007467}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC Rule:MF_03002}.
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DR RefSeq; XP_025050730.1; XM_025194945.1.
DR STRING; 38654.A0A3Q0FX45; -.
DR KEGG; asn:102379089; -.
DR InParanoid; A0A3Q0FX45; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000189705; Unplaced.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProt.
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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR003492; Battenin_disease_Cln3.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
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; PF02487; CLN3; 2.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR PRINTS; PR01315; BATTENIN.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 885..1061
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 10..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..456
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 126979 MW; 891211DF2A80C19D CRC64;
MLSAAHDVLR RHQGPPNGTQ PGPLEPLSPN GSSHYDCNAM STGAVLLADI LPTLVIKVSA
PFYIHLLPYG LRVGICVLSA WGSFLLVAVA PSVALSLAGV VLASVSSGLG EITFLALTAF
YPSGPVSWWS SGTGAAGLLG AVSYLGLTQA GLSPPQTLLA MMGVPLVLLL SYWCLLLPPT
PETPSPTRQP LLEGGPPKPE PGPAALSLAD KGRIMKVSCG QGGGVSMYQL LYQLGVFISR
SSLRCVRLRA TWVLALLQRD PVAPRRFEEL TNLIRTIRNA MKIRDVTKCL EEFELLGRAY
SKAKSIVDKE GVPRFYVRLL ADLEDYLNEL WEDKEGKKRM NKNNAKALST LRQKLRKYNR
DYEALIAAYK QNPEQSADED EEKKSDDSEG SSSSSEDDDD EGISAAAFLK KKEVQGGDTR
AKFLKKMEDE DSDSESSDDD EDWVSSDSDS DSESDEDDGK FTSLASKFLK KDEDKRSSEK
KREEKAKKKH DRKARRDEDE DEDAEGGEWE KVKGGVPMSK PKMFAKGTEI THAVVVKKLN
EILQARGKKG TDRAGQIDLL QLLVAIAAEN NLGVAMEVKI KFNIVASLYD YNPNLAPYMK
VWGXXXXPEM WQKCLASIDE LLDILFANPN IFIGENILEE SENLGNPEQP FRVRGCILTL
VERMDEEFTK IMQNTDPHSQ EYVEHLKDEG RVCGIVARLQ RYLQDKGSTE ELCRVYLRRV
LHTYYKFDYK ALQRQRGPAG DSKSEQDQAE NEGEDSAVLM ERLCKFIYAR DRTDRIRTCA
ILCHIYHHAL HSRWYAARDL MLMSHLQDNI QHADPPVQIL YNRTMVQLGI CAFRQGLIKD
AHNALLDIQS SGRAKELLGQ GLLLRSLQER NSEQEKVEKR RQVPFHMHVN LELLECVYLV
SAMLLEIPYM AAHELDARRR MISKQFHHQL RVGERQPLLG PPESMREHVV AASKAMKMGD
WRTCHRFIVN EKMNGKVWDL FPEADKVRDM LVRKIQEESL RTYLFTYSSV YDSISMEILA
DMFQLDLPTV HSIISKMIIN EELMASLDQP TQTVAMHRTE PTAQQTLALQ LAEKLGALVE
NNERVLDHKQ GSYGGGYFRD QKDGYRKNEG GYMRRGGYRQ QERSSNY
//
