SEC14L2

Protein-coding gene in the species Homo sapiens
SEC14L2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1O6U, 1OLM, 4OMJ, 4OMK,%%s1O6U, 1OLM

Identifiers
AliasesSEC14L2, C22orf6, SPF, TAP, TAP1, SEC14 like lipid binding 2
External IDsOMIM: 607558; MGI: 1915065; HomoloGene: 8245; GeneCards: SEC14L2; OMA:SEC14L2 - orthologs
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for SEC14L2
Genomic location for SEC14L2
Band22q12.2Start30,396,941 bp[1]
End30,425,303 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for SEC14L2
Genomic location for SEC14L2
Band11|11 A1Start4,047,039 bp[2]
End4,073,415 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 11: 4.05 – 4.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

SEC14L2 is a gene that, in humans, encodes the protein SEC14-like protein 2.[5][6]

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 metabolism of cholesterol.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100003 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003585 – 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. ^ Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (Dec 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
  6. ^ a b "Entrez Gene: SEC14L2 SEC14-like 2 (S. cerevisiae)".

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". J. Biol. Chem. 255 (8): 3575–80. 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): 171–4. 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". J. Immunol. 158 (5): 2236–41. 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): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Sanger Centre, The; Washington University Genome Sequencing Cente, The (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. 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 Res. 6 (5): 329–36. 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". J. Biol. Chem. 275 (33): 25672–80. doi:10.1074/jbc.M000851200. PMID 10829015.
  • Shibata N, Arita M, Misaki Y, Dohmae N, Takio K, Ono T, Inoue K, Arai H (2001). "Supernatant protein factor, which stimulates the conversion of squalene to lanosterol, is a cytosolic squalene transfer protein and enhances cholesterol biosynthesis". Proc. Natl. Acad. Sci. U.S.A. 98 (5): 2244–9. 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 Res. 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". Biochem. Biophys. Res. Commun. 285 (2): 295–9. 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): 1533–40. 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". J. Biol. Chem. 278 (8): 5646–51. 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 Radic. Biol. Med. 34 (11): 1458–72. 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". J. Mol. Biol. 332 (4): 759–65. 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". Biochem. Biophys. Res. Commun. 316 (3): 688–92. doi:10.1016/j.bbrc.2004.02.103. PMID 15033454.
  • Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 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, Long J, Stern D, Tammana H, Helt G, Sementchenko V, Piccolboni A, Bekiranov S, Bailey DK, Ganesh M, Ghosh S, Bell I, Gerhard DS, Gingeras TR (2005). "Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution". Science. 308 (5725): 1149–54. Bibcode:2005Sci...308.1149C. doi:10.1126/science.1108625. PMID 15790807. S2CID 13047538.
  • v
  • t
  • e
  • 1o6u: THE CRYSTAL STRUCTURE OF HUMAN SUPERNATANT PROTEIN FACTOR
    1o6u: THE CRYSTAL STRUCTURE OF HUMAN SUPERNATANT PROTEIN FACTOR
  • 1olm: SUPERNATANT PROTEIN FACTOR IN COMPLEX WITH RRR-ALPHA-TOCOPHERYLQUINONE: A LINK BETWEEN OXIDIZED VITAMIN E AND CHOLESTEROL BIOSYNTHESIS
    1olm: SUPERNATANT PROTEIN FACTOR IN COMPLEX WITH RRR-ALPHA-TOCOPHERYLQUINONE: A LINK BETWEEN OXIDIZED VITAMIN E AND CHOLESTEROL BIOSYNTHESIS


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