SCP2

Protein

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)^[1]

Band	1p32.3	Start	52,927,276 bp^[1]
Band	1p32.3	End	53,051,698 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4 C7\|4 50.2 cM	Start	107,901,036 bp^[2]
Band	4 C7\|4 50.2 cM	End	108,002,195 bp^[2]

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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.^[5]^[6]

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.^[7]

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.^[7]

Interactions

SCP2 has been shown to interact with Caveolin 1^[8] and peroxisomal receptor PEX5.^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000116171 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028603 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Yamamoto R, Kallen CB, Babalola GO, Rennert H, Billheimer JT, Strauss JF (January 1991). "Cloning and expression of a cDNA encoding human sterol carrier protein 2". Proc. Natl. Acad. Sci. U.S.A. 88 (2): 463–7. Bibcode:1991PNAS...88..463Y. doi:10.1073/pnas.88.2.463. PMC 50831. PMID 1703300.
^ He Z, Yamamoto R, Furth EE, Schantz LJ, Naylor SL, George H, Billheimer JT, Strauss JF (October 1991). "cDNAs encoding members of a family of proteins related to human sterol carrier protein 2 and assignment of the gene to human chromosome 1 p21----pter". DNA Cell Biol. 10 (8): 559–69. doi:10.1089/dna.1991.10.559. PMID 1718316.
^ ^a ^b "Entrez Gene: SCP2 sterol carrier protein 2".
^ Zhou M, Parr RD, Petrescu AD, Payne HR, Atshaves BP, Kier AB, Ball JM, Schroeder F (June 2004). "Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo". Biochemistry. 43 (23): 7288–306. doi:10.1021/bi035914n. PMID 15182174.
^ Stanley WA, Filipp FV, Kursula P, Schüller N, Erdmann R, Schliebs W, Sattler M, Wilmanns M (December 2006). "Recognition of a functional peroxisome type 1 target by the dynamic import receptor pex5p". Mol. Cell. 24 (5): 653–63. doi:10.1016/j.molcel.2006.10.024. PMC 5030714. PMID 17157249.

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.

PDB gallery

1c44: STEROL CARRIER PROTEIN 2 (SCP2) FROM RABBIT
1qnd: STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES
2c0l: TPR DOMAIN OF HUMAN PEX5P IN COMPLEX WITH HUMAN MSCP2

v t e Transferases: acyltransferases (EC 2.3)
2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase N-Acetylglutamate synthase Choline acetyltransferase Dihydrolipoyl transacetylase Acetyl-CoA C-acyltransferase Beta-galactoside transacetylase Chloramphenicol acetyltransferase N-acetyltransferase Serotonin N-acetyl transferase HGSNAT ARD1A Histone acetyltransferase P300/CBP NAT2 palmitoyltransferases: Carnitine O-palmitoyltransferase CPT1 CPT2 Serine C-palmitoyltransferase SPTLC1 SPTLC2 other: Acyltransferase like 2 Aminolevulinic acid synthase Beta-ketoacyl-ACP synthase Glyceronephosphate O-acyltransferase Lecithin—cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase 2-acylglycerol-3-phosphate O-acyltransferase ABHD5
2.3.2: Aminoacyltransferases	Gamma-glutamyl transpeptidase Peptidyl transferase Transglutaminase Tissue transglutaminase Keratinocyte transglutaminase Factor XIII
2.3.3: converted into alkyl on transfer	Citrate synthase Decylcitrate synthase Citrate (Re)-synthase Decylhomocitrate synthase 2-methylcitrate synthase 2-ethylmalate synthase 3-ethylmalate synthase ATP citrate lyase Malate synthase HMG-CoA synthase HMGCS2 2-hydroxyglutarate synthase 3-propylmalate synthase 2-isopropylmalate synthase Homocitrate synthase Sulfoacetaldehyde acetyltransferase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)