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Database: UniProt
Entry: G1SLW8_RABIT
LinkDB: G1SLW8_RABIT
Original site: G1SLW8_RABIT 
ID   G1SLW8_RABIT            Unreviewed;       374 AA.
AC   G1SLW8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit M {ECO:0000256|HAMAP-Rule:MF_03012};
DE            Short=eIF3m {ECO:0000256|HAMAP-Rule:MF_03012};
GN   Name=EIF3M {ECO:0000256|HAMAP-Rule:MF_03012,
GN   ECO:0000313|Ensembl:ENSOCUP00000003873.3};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000003873.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000003873.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000003873.3,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0007829|PDB:5A5T}
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.00 ANGSTROMS).
RX   PubMed=26344199; DOI=10.1038/NATURE14891;
RA   des Georges A., Dhote V., Kuhn L., Hellen C.U., Pestova T.V., Frank J.,
RA   Hashem Y.;
RT   "Structure of mammalian eIF3 in the context of the 43S preinitiation
RT   complex.";
RL   Nature 525:491-495(2015).
RN   [3] {ECO:0007829|PDB:6W2S, ECO:0007829|PDB:6W2T}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS).
RX   PubMed=32286223; DOI=10.7554/eLife.54575;
RA   Neupane R., Pisareva V.P., Rodriguez C.F., Pisarev A.V., Fernandez I.S.;
RT   "A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S
RT   complex via an uAUG intermediate.";
RL   Elife 9:e54575-e54575(2020).
RN   [4] {ECO:0007829|PDB:6YAM}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS).
RA   Simonetti A., Guca E., Bochler A., Kuhn L., Hashem Y.;
RT   "Structural insights into the mammalian late-stage initiation complexes.";
RL   Submitted (MAR-2020) to the PDB data bank.
RN   [5] {ECO:0000313|Ensembl:ENSOCUP00000003873.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000003873.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is required for several steps in the initiation
CC       of protein synthesis. The eIF-3 complex associates with the 40S
CC       ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC       2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC       (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC       and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC       required for disassembly and recycling of post-termination ribosomal
CC       complexes and subsequently prevents premature joining of the 40S and
CC       60S ribosomal subunits prior to initiation. The eIF-3 complex
CC       specifically targets and initiates translation of a subset of mRNAs
CC       involved in cell proliferation, including cell cycling, differentiation
CC       and apoptosis, and uses different modes of RNA stem-loop binding to
CC       exert either translational activation or repression.
CC       {ECO:0000256|HAMAP-Rule:MF_03012}.
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. The eIF-3 complex appears to include 3 stable modules: module A
CC       is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC       EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC       EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC       EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC       subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC       interacts with RPS6KB1 under conditions of nutrient depletion.
CC       Mitogenic stimulation leads to binding and activation of a complex
CC       composed of MTOR and RPTOR, leading to phosphorylation and release of
CC       RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000256|HAMAP-
CC       Rule:MF_03012}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03012}.
CC   -!- SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008482}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit M family. {ECO:0000256|HAMAP-
CC       Rule:MF_03012}.
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DR   EMBL; AAGW02037548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02037549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02037550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002709079.1; XM_002709033.3.
DR   PDB; 5A5T; EM; 6.00 A; M=1-374.
DR   PDB; 6W2S; EM; 3.00 A; 8=1-374.
DR   PDB; 6W2T; EM; 3.36 A; 8=1-374.
DR   PDB; 6YAM; EM; 3.60 A; u=1-374.
DR   PDBsum; 5A5T; -.
DR   PDBsum; 6W2S; -.
DR   PDBsum; 6W2T; -.
DR   PDBsum; 6YAM; -.
DR   AlphaFoldDB; G1SLW8; -.
DR   EMDB; EMD-10761; -.
DR   EMDB; EMD-21529; -.
DR   EMDB; EMD-21530; -.
DR   SMR; G1SLW8; -.
DR   DIP; DIP-61831N; -.
DR   IntAct; G1SLW8; 1.
DR   PaxDb; 9986-ENSOCUP00000003873; -.
DR   Ensembl; ENSOCUT00000004484.4; ENSOCUP00000003873.3; ENSOCUG00000004483.4.
DR   GeneID; 100359271; -.
DR   KEGG; ocu:100359271; -.
DR   CTD; 10480; -.
DR   eggNOG; KOG2753; Eukaryota.
DR   GeneTree; ENSGT00390000004456; -.
DR   HOGENOM; CLU_035254_1_0_1; -.
DR   OMA; AQRCILA; -.
DR   OrthoDB; 2875448at2759; -.
DR   TreeFam; TF106148; -.
DR   Proteomes; UP000001811; Chromosome 1.
DR   Bgee; ENSOCUG00000004483; Expressed in aorta and 15 other cell types or tissues.
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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03012; eIF3m; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045237; COPS7/eIF3m.
DR   InterPro; IPR027528; eIF3m.
DR   InterPro; IPR040750; eIF3m_C_helix.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR15350; COP9 SIGNALOSOME COMPLEX SUBUNIT 7/DENDRITIC CELL PROTEIN GA17; 1.
DR   PANTHER; PTHR15350:SF2; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT M; 1.
DR   Pfam; PF18005; eIF3m_C_helix; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5A5T, ECO:0007829|PDB:6W2S};
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_03012};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03012};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_03012};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_03012}; Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03012"
FT   DOMAIN          180..339
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03012"
SQ   SEQUENCE   374 AA;  42503 MW;  63736CA2B093D794 CRC64;
     MSVPAFIDIS EEDQAAELRA YLKSKGAEIS EENSEGGLHV DLAQIIEACD VCLKEDDKDV
     ESVMNSVVSL LLILEPDKQE ALIESLCEKL VKFREGERPS LRLQLLSNLF HGMDKNTPVR
     YTVYCSLIKV AASCGAIQYI PTELDQVRKW ISDWNLTTEK KHTLLRLLYE ALVDCKKSDA
     ASKVMVELLG SYTEDNASQA RVDAHRCIVR ALKDPNAFLF DHLLTLKPVK FLEGELIHDL
     LTIFVSAKLA SYVKFYQNNK DFIDSLGLLH EQNMAKMRLL TFMGMAVENK EISFDTMQQE
     LQIGADDVEA FVIDAVRTKM VYCKIDQTQR KVVVSHSTHR TFGKQQWQQL YDTLNAWKQN
     LNKVKNSLLS LSDT
//
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