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EIF2D
Identifiers
Aliases	EIF2D, HCA56, LGTN, eukaryotic translation initiation factor 2D
External IDs	OMIM: 613709; MGI: 109342; HomoloGene: 38244; GeneCards: EIF2D; OMA:EIF2D - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q32.1 Start 206,571,292 bp End 206,612,465 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 E4|1 56.9 cM Start 131,080,918 bp End 131,115,395 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left ovary body of uterus right ovary right uterine tube glutes muscle of thigh parotid gland body of pancreas muscle layer of sigmoid colon canal of the cervix Top expressed in Paneth cell fossa condyle hair follicle internal carotid artery lacrimal gland primitive streak external carotid artery endothelial cell of lymphatic vessel epiblast More reference expression data BioGPS More reference expression data
Gene ontology Molecular function translation initiation factor activity RNA binding signaling receptor activity Cellular component cytoplasm cytosolic small ribosomal subunit cytosol nuclear body Biological process translational initiation intracellular protein transport ribosome disassembly protein biosynthesis formation of translation preinitiation complex IRES-dependent viral translational initiation signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1939 16865 Ensembl ENSG00000143486 ENSMUSG00000026427 UniProt P41214 Q5SY38 Q61211 RefSeq (mRNA) NM_001201478 NM_006893 NM_001136070 NM_010709 RefSeq (protein) NP_001188407 NP_008824 NP_001129542 NP_034839 Location (UCSC) Chr 1: 206.57 – 206.61 Mb Chr 1: 131.08 – 131.12 Mb PubMed search
Wikidata
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Ligatin, otherwise known as eIF2D, is a protein that in humans is encoded by the LGTN gene. This protein is not a component of the heterotrimeric eIF2 complex, but instead functions in different pathways of eukaryotic translation.

Function

This gene encodes a protein receptor that localizes phosphoglycoproteins within endosomes and at the cell periphery. This trafficking receptor for phosphoglycoproteins may play a role in neuroplasticity by modulating cell-cell interactions, intracellular adhesion, and protein binding at membrane surfaces. In hippocampal neurons, long-lasting down-regulation of ligation mRNA levels occurs via post-transcriptional RNA processing following glutamate receptor activation. This protein contains single PUA and SUI1 domains and these domains may function in RNA binding and translation initiation, respectively.

See also

• Eukaryotic translation
• Eukaryotic initiation factor

References

1. ^ GRCh38: Ensembl release 89: ENSG00000143486 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000026427 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Jakoi ER, Brown AL, Ho YS, Snyderman R (June 1989). "Molecular cloning of the cDNA for ligatin". Journal of Cell Science. 93 ( Pt 2) (2): 227–32. doi:10.1242/jcs.93.2.227. PMID 2482295.
6. ^ "Entrez Gene: LGTN ligatin".

Further reading

• Jakoi ER, Ross PE, Ping Ting-Beall H, Kaufman B, Vanaman TC (January 1987). "Ligatin: a peripheral membrane protein with covalently bound palmitic acid". The Journal of Biological Chemistry. 262 (3): 1300–4. doi:10.1016/S0021-9258(19)75786-X. PMID 3805022.
• Gaston SM, Marchase RB, Jakoi ER (1982). "Brain ligatin: a membrane lectin that binds acetylcholinesterase". Journal of Cellular Biochemistry. 18 (4): 447–59. doi:10.1002/jcb.1982.240180406. PMID 7085778. S2CID 22975039.
• Marchase RB, Koro LA, Kelly CM, McClay DR (1982). "A possible role for ligatin and the phosphoglycoproteins it binds in calcium-dependent retinal cell adhesion". Journal of Cellular Biochemistry. 18 (4): 461–8. doi:10.1002/jcb.1982.240180407. PMID 7085779. S2CID 44992995.
• Jakoi ER, Kempe K, Gaston SM (1982). "Ligatin binds phosphohexose residues on acidic hydrolases". Journal of Supramolecular Structure and Cellular Biochemistry. 16 (2): 139–53. doi:10.1002/jsscb.1981.380160205. PMID 7299841.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Wang Y, Han KJ, Pang XW, Vaughan HA, Qu W, Dong XY, Peng JR, Zhao HT, Rui JA, Leng XS, Cebon J, Burgess AW, Chen WF (July 2002). "Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies". Journal of Immunology. 169 (2): 1102–9. doi:10.4049/jimmunol.169.2.1102. PMID 12097419.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

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