SCP2

Non-specific lipid-transfer protein also known as sterol carrier protein 2 (SCP-2) or propanoyl-CoA C-acyltransferase is a protein that in humans is encoded by the SCP2 gene.

SCP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1QND, 2C0L
Identifiers
Aliases	SCP2, NLTP, NSL-TP, SCP-2, SCP-CHI, SCP-X, SCPX, sterol carrier protein 2, SCOX
External IDs	OMIM: 184755; MGI: 98254; HomoloGene: 37717; GeneCards: SCP2; OMA:SCP2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p32.3 Start 52,927,276 bp End 53,051,698 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4 C7|4 50.2 cM Start 107,901,036 bp End 108,002,195 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa right lobe of liver palpebral conjunctiva germinal epithelium duodenum rectum epithelium of nasopharynx mucosa of sigmoid colon gallbladder pylorus Top expressed in proximal tubule right kidney white adipose tissue hepatobiliary system liver jejunum granulocyte duodenum human kidney colon More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity phosphatidylinositol transfer activity fatty-acyl-CoA binding acyltransferase activity, transferring groups other than amino-acyl groups sterol transporter activity oleic acid binding long-chain fatty acyl-CoA binding cholesterol binding protein binding propanoyl-CoA C-acyltransferase activity catalytic activity signaling receptor binding acyltransferase activity lipid binding propionyl-CoA C2-trimethyltridecanoyltransferase activity Cellular component membrane intracellular membrane-bounded organelle peroxisome nucleoplasm peroxisomal matrix mitochondrion extracellular exosome cytoplasm cytosol protein-containing complex Biological process progesterone biosynthetic process peroxisome organization lipid transport inositol trisphosphate biosynthetic process alpha-linolenic acid metabolic process positive regulation of steroid metabolic process lipid hydroperoxide transport positive regulation of intracellular cholesterol transport fatty acid beta-oxidation using acyl-CoA oxidase metabolism protein localization to plasma membrane bile acid biosynthetic process sterol transport steroid biosynthetic process phospholipid transport transport protein targeting to peroxisome Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6342 20280 Ensembl ENSG00000116171 ENSMUSG00000028603 UniProt P22307 P32020 RefSeq (mRNA) NM_001007098 NM_001007099 NM_001007100 NM_001007250 NM_001193599 NM_001193600 NM_001193617 NM_002979 NM_001330587 NM_011327 RefSeq (protein) NP_001007099 NP_001007100 NP_001007101 NP_001007251 NP_001180528 NP_001180529 NP_001180546 NP_001317516 NP_002970 NP_035457 Location (UCSC) Chr 1: 52.93 – 53.05 Mb Chr 4: 107.9 – 108 Mb PubMed search
Wikidata
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Function

This gene encodes two proteins: sterol carrier protein X (SCPx) and sterol carrier protein 2 (SCP2), as a result of transcription initiation from 2 independently regulated promoters. The transcript initiated from the proximal promoter encodes the longer SCPx protein, and the transcript initiated from the distal promoter encodes the shorter SCP2 protein, with the 2 proteins sharing a common C-terminus. Evidence suggests that the SCPx protein is a peroxisome-associated thiolase that is involved in the oxidation of branched chain fatty acids, while the SCP2 protein is thought to be an intracellular lipid transfer protein. Alternative splicing of this gene produces multiple transcript variants, some encoding different isoforms. The full-length nature of all transcript variants has not been determined.

Clinical significance

This gene is highly expressed in organs involved in lipid metabolism, and may play a role in Zellweger syndrome, in which cells are deficient in peroxisomes and have impaired bile acid synthesis.

Interactions

SCP2 has been shown to interact with Caveolin 1 and peroxisomal receptor PEX5.

Further reading

• Seedorf U, Ellinghaus P, Roch Nofer J (2000). "Sterol carrier protein-2". Biochim. Biophys. Acta. 1486 (1): 45–54. doi:10.1016/s1388-1981(00)00047-0. PMID 10856712.
• Gallegos AM, Atshaves BP, Storey SM, et al. (2001). "Gene structure, intracellular localization, and functional roles of sterol carrier protein-2". Prog. Lipid Res. 40 (6): 498–563. doi:10.1016/S0163-7827(01)00015-7. PMID 11591437.
• Yamamoto R (1993). "[Localization of human sterol carrier protein 2 gene and cDNA expression in COS-7 cell]". Hokkaido Igaku Zasshi. 67 (6): 839–48. PMID 1483685.
• Baker ME, Billheimer JT, Strauss JF (1992). "Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier protein (SCPx) and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx". DNA Cell Biol. 10 (9): 695–8. doi:10.1089/dna.1991.10.695. PMID 1755959.
• Schroeder F, Butko P, Nemecz G, Scallen TJ (1990). "Interaction of fluorescent delta 5,7,9(11),22-ergostatetraen-3 beta-ol with sterol carrier protein-2". J. Biol. Chem. 265 (1): 151–7. doi:10.1016/S0021-9258(19)40208-1. PMID 2294101.
• Ohba T, Holt JA, Billheimer JT, Strauss JF (1995). "Human sterol carrier protein x/sterol carrier protein 2 gene has two promoters". Biochemistry. 34 (33): 10660–8. doi:10.1021/bi00033a042. PMID 7654720.
• Ohba T, Rennert H, Pfeifer SM, et al. (1995). "The structure of the human sterol carrier protein X/sterol carrier protein 2 gene (SCP2)". Genomics. 24 (2): 370–4. doi:10.1006/geno.1994.1630. PMID 7698762.
• Woodford JK, Colles SM, Myers-Payne S, et al. (1995). "Sterol carrier protein-2 stimulates intermembrane sterol transfer by direct membrane interaction". Chem. Phys. Lipids. 76 (1): 73–84. doi:10.1016/0009-3084(95)02436-M. PMID 7788802.
• Vesa J, Hellsten E, Barnoski BL, et al. (1994). "Assignment of sterol carrier protein X/sterol carrier protein 2 to 1p32 and its exclusion as the causative gene for infantile neuronal ceroid lipofuscinosis". Hum. Mol. Genet. 3 (2): 341–6. doi:10.1093/hmg/3.2.341. PMID 8004106.
• Seedorf U, Brysch P, Engel T, et al. (1994). "Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity". J. Biol. Chem. 269 (33): 21277–83. doi:10.1016/S0021-9258(17)31960-9. PMID 8063752.
• Szyperski T, Scheek S, Johansson J, et al. (1993). "NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2". FEBS Lett. 335 (1): 18–26. doi:10.1016/0014-5793(93)80431-S. PMID 8243660. S2CID 9969358.
• Seedorf U, Scheek S, Engel T, et al. (1994). "Structure-activity studies of human sterol carrier protein 2". J. Biol. Chem. 269 (4): 2613–8. doi:10.1016/S0021-9258(17)41988-0. PMID 8300590.
• Yanase T, Hara T, Sakai Y, et al. (1996). "Expression of sterol carrier protein 2 (SCP2) in human adrenocortical tissue". Eur. J. Endocrinol. 134 (4): 501–7. doi:10.1530/eje.0.1340501. PMID 8640304.
• Stolowich NJ, Frolov A, Atshaves B, et al. (1997). "The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination". Biochemistry. 36 (7): 1719–29. doi:10.1021/bi962317a. PMID 9048555.
• Schalk JA, Offenberg HH, Peters E, et al. (1999). "Isolation and characterization of the human SCP2 cDNA and chromosomal localization of the gene". Mamm. Genome. 10 (6): 642–4. doi:10.1007/s003359901062. PMID 10341103. S2CID 9107396.
• Jatzke C, Hinz HJ, Seedorf U, Assmann G (1999). "Stability and binding properties of wild-type and c17s mutated human sterol carrier protein 2". Biochim. Biophys. Acta. 1432 (2): 265–74. doi:10.1016/S0167-4838(99)00114-4. PMID 10407148.
• Kimura H, Fujii H, Suzuki S, et al. (1999). "Lipid-binding proteins in rat and human kidney". Kidney Int. Suppl. 71: S159–62. doi:10.1046/j.1523-1755.1999.07141.x. PMID 10412765.
• Huang H, Ball JM, Billheimer JT, Schroeder F (1999). "The sterol carrier protein-2 amino terminus: a membrane interaction domain". Biochemistry. 38 (40): 13231–43. doi:10.1021/bi990870x. PMID 10529196.