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Database: UniProt
Entry: A0A498MDP4_LABRO
LinkDB: A0A498MDP4_LABRO
Original site: A0A498MDP4_LABRO 
ID   A0A498MDP4_LABRO        Unreviewed;       898 AA.
AC   A0A498MDP4;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
GN   ORFNames=ROHU_036968 {ECO:0000313|EMBL:RXN18330.1};
OS   Labeo rohita (Indian major carp) (Cyprinus rohita).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Labeoninae; Labeonini; Labeo.
OX   NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN18330.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN18330.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN18330.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN18330.1};
RA   Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA   Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA   Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA   Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA   Shah T.M., Rai A., Jena J.K.;
RT   "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Appears to play a role in the switch from cap-dependent to
CC       IRES-mediated translation during mitosis, apoptosis and viral
CC       infection. Cleaved by some caspases and viral proteases.
CC       {ECO:0000256|ARBA:ARBA00037759}.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000256|ARBA:ARBA00005775}.
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:RXN18330.1}.
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DR   EMBL; QBIY01012722; RXN18330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498MDP4; -.
DR   STRING; 84645.A0A498MDP4; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
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:SF82; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 2; 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   1: Evidence at protein level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Initiation factor {ECO:0000313|EMBL:RXN18330.1};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Protein biosynthesis {ECO:0000313|EMBL:RXN18330.1};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MDP4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          535..658
FT                   /note="MI"
FT                   /evidence="ECO:0000259|PROSITE:PS51366"
FT   DOMAIN          712..895
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          12..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..503
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   898 AA;  102091 MW;  E833ECA511815580 CRC64;
     MPLKVAAWDI SASSGGGGGR GAPQHYPKTV GNSEYLGKTP GPSVQRWVPS RSTRRDVNSS
     NEKEHHDAIF RKVRGILNKL TPEKFDKLCL ELLNVGVDSK LVLKGIILLI VDKALEEPKY
     SSLYAQLCLR LAEDAPNFDG PTPEIQSSQK QSTTFRRLLI TKLQDEFENR TKNVDIYDKQ
     DNPLTSEEEE QRAIAKIKML GNIKFIGELG KLDLIHESIL HKCIKTLLEK KKRVQLKDMG
     EDLECLCQIM RTVGPRLDHE KAKSLMDQYF GRMRSLMNNK DLPARIRFLL QDTVELRENN
     WVPRKAFIDN GPKTINQIRQ DAVKDLGVFI PPMNQGLRMD FFLEGPFMPN RMKLDRETLG
     GLADMFGQMP GSGIGTGPGV IQDRFSPTLG RHRTNPLFNG HSGHMASQPQ SQFDLGMKPF
     IKSNQGQNQH FHNQNQNHSN QQQAQSKDMP PRFKKGQLNA DEISLRPAQS FLMNKNQVPK
     LQPQIPTMIP PSAQPPRTQT PPLGQPPQLG LKTNPPLIQE KPQKTTKKPA PTKEELLKMT
     ENVVTEYLNS KNMEDAVSGV KEMKAPKHFL PEMLSKIILC SLERTDEDRE QASTLIHTLR
     TEGFITGENF MQALLNVLDQ CPKIEVDIPL VKSYLAQFAA RAVIAELVSV AELAHPLENG
     NHFPLFLLCL QQASKLKDRE WLTDLFQQSK VNMQKMLPEI DQNKDRMLEV LEGKGLSFLF
     PLLKLEKELL MQIKTDPSPQ AIYKWIKDNI SPKLHTDKGF INILMTSFLH YIFAELGVNE
     GDEQLASPSK EQLDQEKQLL LSFKPVMQKF LHDHPDLQVS ALYALQVHCN ASAFPKGMLL
     RYFVNFYDME IIEEEGFLAW KEDISQEFPG KGKALFQVNQ WLTWLETAEE EESEEEAD
//
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