SEC14L2

SEC14L2
Identifiers
Aliases	SEC14L2, C22orf6, SPF, TAP, TAP1, SEC14 like lipid binding 2
External IDs	OMIM: 607558; MGI: 1915065; GeneCards: SEC14L2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1O6U, 1OLM, 4OMJ, 4OMK,%%s1O6U, 1OLM
Gene location (Human) Chr. Chromosome 22 (human) Band 22q12.2 Start 30,396,941 bp End 30,425,303 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 A1 Start 4,047,039 bp End 4,073,415 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver right frontal lobe prefrontal cortex nucleus accumbens amygdala C1 segment cingulate gyrus caudate nucleus putamen anterior cingulate cortex Top expressed in superior surface of tongue left lobe of liver gallbladder olfactory epithelium yolk sac neural layer of retina dentate gyrus of hippocampal formation granule cell jejunum retinal pigment epithelium cingulate gyrus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function vitamin E binding phospholipid binding lipid binding transporter activity Cellular component cytoplasm integral component of membrane extracellular exosome intracellular anatomical structure nucleus cytosol Biological process regulation of cholesterol biosynthetic process positive regulation of transcription, DNA-templated regulation of transcription, DNA-templated transcription, DNA-templated transport Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 23541 67815 Ensembl ENSG00000100003 ENSMUSG00000003585 UniProt O76054 Q99J08 RefSeq (mRNA) NM_033382 NM_001204204 NM_001291932 NM_012429 NM_144520 RefSeq (protein) NP_001191133 NP_001278861 NP_036561 NP_203740 NP_036561.1 NP_653103 Location (UCSC) Chr 22: 30.4 – 30.43 Mb Chr 11: 4.05 – 4.07 Mb PubMed search
Wikidata
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SEC14L2 is a gene that, in humans, encodes the protein SEC14-like protein 2.

Function

This gene encodes a cytosolic protein which belongs to a family of lipid-binding proteins including Sec14p, alpha-tocopherol transfer protein, and cellular retinol-binding protein. The encoded protein stimulates squalene monooxygenase which is a downstream enzyme in biosynthesis and metabolism of cholesterol.

Further reading

• Caras IW, Friedlander EJ, Bloch K (1980). "Interactions of supernatant protein factor with components of the microsomal squalene epoxidase system. Binding of supernatant protein factor to anionic phospholipids". The Journal of Biological Chemistry. 255 (8): 3575–3580. doi:10.1016/S0021-9258(19)85740-X. PMID 7364757.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Solheim JC, Harris MR, Kindle CS, Hansen TH (1997). "Prominence of beta 2-microglobulin, class I heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing". Journal of Immunology. 158 (5): 2236–2241. doi:10.4049/jimmunol.158.5.2236. PMID 9036970. S2CID 30900833.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• "Toward a complete human genome sequence". Genome Research. 8 (11): 1097–1108. November 1998. doi:10.1101/gr.8.11.1097. PMID 9847074.
• Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O (2000). "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain". DNA Research. 6 (5): 329–336. doi:10.1093/dnares/6.5.329. PMID 10574461.
• Zimmer S, Stocker A, Sarbolouki MN, Spycher SE, Sassoon J, Azzi A (2000). "A novel human tocopherol-associated protein: cloning, in vitro expression, and characterization". The Journal of Biological Chemistry. 275 (33): 25672–25680. doi:10.1074/jbc.M000851200. PMID 10829015.
• Shibata N, Arita M, Misaki Y, Dohmae N, Takio K, Ono T, et al. (2001). "Supernatant protein factor, which stimulates the conversion of squalene to lanosterol, is a cytosolic squalene transfer protein and enhances cholesterol biosynthesis". Proceedings of the National Academy of Sciences of the United States of America. 98 (5): 2244–2249. Bibcode:2001PNAS...98.2244S. doi:10.1073/pnas.041620398. PMC 30123. PMID 11226224.
• Hirosawa M, Nagase T, Murahashi Y, Kikuno R, Ohara O (2001). "Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping". DNA Research. 8 (1): 1–9. doi:10.1093/dnares/8.1.1. PMID 11258795.
• Yamauchi J, Iwamoto T, Kida S, Masushige S, Yamada K, Esashi T (2001). "Tocopherol-associated protein is a ligand-dependent transcriptional activator". Biochemical and Biophysical Research Communications. 285 (2): 295–299. doi:10.1006/bbrc.2001.5162. PMID 11444841.
• Stocker A, Tomizaki T, Schulze-Briese C, Baumann U (2003). "Crystal structure of the human supernatant protein factor". Structure. 10 (11): 1533–1540. doi:10.1016/S0969-2126(02)00884-5. PMID 12429094.
• Singh DK, Mokashi V, Elmore CL, Porter TD (2003). "Phosphorylation of supernatant protein factor enhances its ability to stimulate microsomal squalene monooxygenase". The Journal of Biological Chemistry. 278 (8): 5646–5651. doi:10.1074/jbc.M211750200. PMID 12454003.
• Kempná P, Zingg JM, Ricciarelli R, Hierl M, Saxena S, Azzi A (2004). "Cloning of novel human SEC14p-like proteins: ligand binding and functional properties". Free Radical Biology & Medicine. 34 (11): 1458–1472. doi:10.1016/S0891-5849(03)00173-4. PMID 12757856.
• Stocker A, Baumann U (2003). "Supernatant protein factor in complex with RRR-alpha-tocopherylquinone: a link between oxidized Vitamin E and cholesterol biosynthesis". Journal of Molecular Biology. 332 (4): 759–765. doi:10.1016/S0022-2836(03)00924-0. PMID 12972248.
• Mokashi V, Singh DK, Porter TD (2004). "Rat supernatant protein factor-like protein stimulates squalene monooxygenase and is activated by protein kinase A". Biochemical and Biophysical Research Communications. 316 (3): 688–692. doi:10.1016/j.bbrc.2004.02.103. PMID 15033454.
• Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biology. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
• Cheng J, Kapranov P, Drenkow J, Dike S, Brubaker S, Patel S, et al. (2005). "Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution". Science. 308 (5725): 1149–1154. Bibcode:2005Sci...308.1149C. doi:10.1126/science.1108625. PMID 15790807. S2CID 13047538.