ID A0A2K5MAS3_CERAT Unreviewed; 1621 AA.
AC A0A2K5MAS3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Eukaryotic translation initiation factor 4 gamma 3 {ECO:0000313|Ensembl:ENSCATP00000022299.1};
GN Name=EIF4G3 {ECO:0000313|Ensembl:ENSCATP00000022299.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000022299.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000022299.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
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DR RefSeq; XP_011935695.1; XM_012080305.1.
DR Ensembl; ENSCATT00000046506.1; ENSCATP00000022299.1; ENSCATG00000034614.1.
DR GeneID; 105595036; -.
DR CTD; 8672; -.
DR GeneTree; ENSGT00940000156454; -.
DR OrthoDB; 92033at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000034614; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd11559; W2_eIF4G1_like; 1.
DR Gene3D; 1.25.40.180; -; 3.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR PANTHER; PTHR23253:SF23; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 3; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 1257..1379
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 1452..1621
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1621 AA; 180367 MW; DFD993B0206ED28F CRC64;
MNSQPQTRSP FFQRPQIQPP RATIPNSSPS IRPGAQTPTA VYQANQHIMM VNHLPMPYPV
PQGPQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG PGDFPNAYGT PFYPSQPVYQ
SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG GKDITEEIMS GGGSRNPTPP IGRPTSTPTP
PQLPSQVPEH SPVVYGTVES AHLAVSTPVT AASDQKQEEK PKPDPVLKSP SPVLRLVLSG
EKKEQEGQTS ETTAIVSIAE LPLPPSPTTV SSIARSTIAS PTSSALSSQP LFTTAIDDRC
ELSSSREDTV PVPSLTSCTE TSDPLPTNEN DGDICKKPCS VAPNDIPLIS STTLINEING
VSEKLPATES TVEIVKQEVL PLTLELEILE NPPEEMKLEC IPTPITPSTV PSFPPTPPTP
PTSPPPTPVI VPAAATTVSS PSAAITVQRV LEEDESIRTC LSEDTKEIQN KIEVEADGQT
EEILDSQNLN SRRSPVPAQI AITVPKTWKK PKDRTRTTEE MLEAELEPKA EEELSVDKVL
ESEQDKMSQG FHPERDPSDL KKVKAVEENG EEAEPVRNGA ESVSEGEGID ANSGSTDSSG
DGVTFPFKPE SWKPTDTEGK KQYDREFLLD FQFMPACIQK PEGLPPISDV VLDKINQPKL
PMRTLDPRIL PRGPDFTPAF ADFGRQTPGG RGVPICKVQS RHGLPILEQS KAPTCPPLAM
SHPPMKSLPL GLLNVGPRRS QPGQRREPRK IITVSVKEDV HLKKAENAWK PSQKRDSQAD
DPENIKTQEL FRKVRSILNK LTPQMFNQLM KQVSGLTVDT EERLKGVIDL VFEKAIDEPS
FSVAYANMCR CLVTLKVPMA DKPGNTVNFR KLLLNRCQKE FEKDKADDDV FEKKQKELEA
ASAPEERTRL HDELEEAKDK ARRRSIGNIK FIGELFKLKM LTEAIMHDCV VKLLKNHDEE
SLECLCRLLT TIGKDLDFEK AKPRMDQYFN QMEKIVKERK TSSRIRFMLQ DVIDLRLCNW
VSRRADQGPK TIEQIHKEAK IEEQEEQRKV QQLMTKEKRR PGVQRVDEGG WNTVQGAKNS
RVLDPSKFLK ITKPTIDEKI QLVPKAQLGS WGKGSSGGAK ASETDALRSS ASSLNRFSAL
QPPAPSGSTP STPVEFDSRR TITSRGSMGR EKNDKPLPSA TARPNTFMRG GSSKDLLDNQ
SQEEQRREML ETVKQLTGAV DVERNSTDAE RNKTRESAKP EISAVSAPDK AALSEEEMER
KSKSIIDEFL HINDFKEAVQ CVEELNTQGL LHVFVRVGVE STLERSQITR DHMGQLLYQL
VQSEKLSKQD FFKGFSETLE LADDMAIDIP HIWLYLAELV TPMLKEGGIS MRELTTEFSK
PLLPVGRAGV LLSEILHLLC KQMSHKKVGA LWREADLSWK DFLPEGEDVH NFLLEQKLDF
IESDSPCSSE ALSKKELSAE ELYKRLEKLI IEDKANDEQI FDWVEANLDE SQMSSPTFLR
ALMTAVCKAA IIADSSTFRV DTAVIKQRVP ILLKYLDSDT EKELQALYAL QASIVKLDQP
ANLLRMFFDC LYDEEVISED AFYKWESSKD PAEQNGKGVA LKSVTAFFTW LREAEEESED
N
//
