EIF2D_MOUSE
ID EIF2D_MOUSE Reviewed; 570 AA.
AC Q61211; Q3TDE0; Q3THV5; Q3TTP4; Q8C491; Q8CBF1; Q8CC17; Q8R1I9; Q8R3M5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Eukaryotic translation initiation factor 2D;
DE Short=eIF2D;
DE AltName: Full=Ligatin;
GN Name=Eif2d; Synonyms=Lgtn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Adrenal gland, Cerebellum, Diencephalon, Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-550.
RX PubMed=9070942; DOI=10.1006/geno.1996.4550;
RA Malnar-Dragojevic D., Trachtulec Z., Vincek V.;
RT "Assignment of the mouse ligatin gene (Lgtn) to chromosome 1F by in situ
RT hybridization.";
RL Genomics 40:192-193(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238 AND SER-241, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Translation initiation factor that is able to deliver tRNA to
CC the P-site of the eukaryotic ribosome in a GTP-independent manner. The
CC binding of Met-tRNA(I) occurs after the AUG codon finds its position in
CC the P-site of 40S ribosomes, the situation that takes place during
CC initiation complex formation on some specific RNAs. Its activity in
CC tRNA binding with 40S subunits does not require the presence of the
CC aminoacyl moiety. Possesses the unique ability to deliver non-Met
CC (elongator) tRNAs into the P-site of the 40S subunit. In addition to
CC its role in initiation, can promote release of deacylated tRNA and mRNA
CC from recycled 40S subunits following ABCE1-mediated dissociation of
CC post-termination ribosomal complexes into subunits (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61211-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61211-2; Sequence=VSP_016233;
CC -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53056.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK034115; BAC28591.1; -; mRNA.
DR EMBL; AK036154; BAC29323.1; -; mRNA.
DR EMBL; AK046539; BAC32777.1; -; mRNA.
DR EMBL; AK082748; BAC38598.1; -; mRNA.
DR EMBL; AK083638; BAC38976.1; -; mRNA.
DR EMBL; AK139052; BAE23874.1; -; mRNA.
DR EMBL; AK161269; BAE36281.1; -; mRNA.
DR EMBL; AK167980; BAE39972.1; -; mRNA.
DR EMBL; AK168120; BAE40091.1; -; mRNA.
DR EMBL; AK170252; BAE41662.1; -; mRNA.
DR EMBL; AK170448; BAE41806.1; -; mRNA.
DR EMBL; AK171115; BAE42257.1; -; mRNA.
DR EMBL; BC024501; AAH24501.1; -; mRNA.
DR EMBL; BC025036; AAH25036.1; -; mRNA.
DR EMBL; U58337; AAC53056.1; ALT_FRAME; mRNA.
DR CCDS; CCDS48354.1; -. [Q61211-1]
DR RefSeq; NP_001129542.1; NM_001136070.1. [Q61211-1]
DR RefSeq; NP_034839.2; NM_010709.3.
DR RefSeq; XP_006529228.1; XM_006529165.3.
DR AlphaFoldDB; Q61211; -.
DR SMR; Q61211; -.
DR BioGRID; 201151; 2.
DR STRING; 10090.ENSMUSP00000063894; -.
DR iPTMnet; Q61211; -.
DR PhosphoSitePlus; Q61211; -.
DR SwissPalm; Q61211; -.
DR EPD; Q61211; -.
DR MaxQB; Q61211; -.
DR PaxDb; Q61211; -.
DR PRIDE; Q61211; -.
DR ProteomicsDB; 275448; -. [Q61211-1]
DR ProteomicsDB; 275449; -. [Q61211-2]
DR Antibodypedia; 34586; 122 antibodies from 26 providers.
DR DNASU; 16865; -.
DR Ensembl; ENSMUST00000068805; ENSMUSP00000063894; ENSMUSG00000026427. [Q61211-1]
DR Ensembl; ENSMUST00000151874; ENSMUSP00000138061; ENSMUSG00000026427. [Q61211-1]
DR GeneID; 16865; -.
DR KEGG; mmu:16865; -.
DR UCSC; uc007cmz.2; mouse. [Q61211-1]
DR CTD; 1939; -.
DR MGI; MGI:109342; Eif2d.
DR VEuPathDB; HostDB:ENSMUSG00000026427; -.
DR eggNOG; KOG2522; Eukaryota.
DR GeneTree; ENSGT00550000074865; -.
DR HOGENOM; CLU_012487_2_0_1; -.
DR InParanoid; Q61211; -.
DR OMA; MFLKPYR; -.
DR OrthoDB; 401807at2759; -.
DR PhylomeDB; Q61211; -.
DR TreeFam; TF105830; -.
DR BioGRID-ORCS; 16865; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Eif2d; mouse.
DR PRO; PR:Q61211; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61211; protein.
DR Bgee; ENSMUSG00000026427; Expressed in paneth cell and 260 other tissues.
DR ExpressionAtlas; Q61211; baseline and differential.
DR Genevisible; Q61211; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0001731; P:formation of translation preinitiation complex; ISO:MGI.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR GO; GO:0032790; P:ribosome disassembly; ISO:MGI.
DR CDD; cd11608; eIF2D_C; 1.
DR InterPro; IPR039757; EIF2D.
DR InterPro; IPR039759; eIF2D_SUI1.
DR InterPro; IPR041366; Pre-PUA.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR PANTHER; PTHR12217; PTHR12217; 1.
DR Pfam; PF17832; Pre-PUA; 1.
DR Pfam; PF01253; SUI1; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR SUPFAM; SSF55159; SSF55159; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS50296; SUI1; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Initiation factor;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..570
FT /note="Eukaryotic translation initiation factor 2D"
FT /id="PRO_0000130612"
FT DOMAIN 93..173
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT DOMAIN 370..454
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT DOMAIN 478..548
FT /note="SUI1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P41214"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41214"
FT VAR_SEQ 551..570
FT /note="YRLPGKYIQGLEKAPKPGKK -> NTGTLHLPAQYPHPHVQNKPEIPHLSCC
FT GLPASHDSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016233"
FT CONFLICT 176..179
FT /note="LWRS -> HASA (in Ref. 2; AAH24501)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="W -> V (in Ref. 3; AAC53056)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="E -> K (in Ref. 1; BAE36281)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="K -> E (in Ref. 1; BAE41662)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="P -> R (in Ref. 1; BAE40091)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="S -> P (in Ref. 1; BAC28591)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="E -> G (in Ref. 1; BAC29323/BAC38598 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 550..552
FT /note="EYR -> IMW (in Ref. 1; BAC28591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 62830 MW; 68DAA2768A595AC8 CRC64;
MFAKAFRVKS NTAIKGSDRR KLRADVTAAF PALGTDQISE LIPGKEELNV VKLYVHKGDS
VTVYTSGGNP ILFELEKNLY PTVYTLWAYP DILPTFITWP LVLEKLVGGA DLMLPGVVVP
PTGLPQVQQG DLCAIALVGN RAPVAIGVAA MSTAQMLASG LKGKGVSVLH TYQDHLWRSG
DKSSPPAIAP LDPTDSCEEK VHLGLQGNLK SLTLDGEEEN GQVPLREASE DTSSRAPSQD
SLDGKPLQEQ MDDLLLRCFL HALKSRVKKA DLPLLTSTLL GSHMFSCCPE GQQLDIKKSS
YKKLSKFLQH MQQEQIVQVK ELSKGVESIV AVDWRHPRIT SFVIPEPSLT SQTVQEVSRE
QPYLPPDIKS LYCVPANMTQ LFLESGHKKG STLEGSEVRK IITDYAKRNR LVDADNRNLV
KLDPILCDCI LEKNEQHLVT KLPWDCLLTR CLKNMQPAYQ VTFPGQEPIL KKGKLCPIDI
TLALKTYNKK VTVVRNLETY GLDPCSVAAI LQQRCQASTI VSPAPGAKDS LQVQVQGNQI
HHLGQLLLEE YRLPGKYIQG LEKAPKPGKK
