ID SCP2_HUMAN Reviewed; 547 AA. AC P22307; A6NM69; B4DGJ9; B4DHP6; C9JC79; D3DQ37; E1B6W5; F2Z3J1; Q15432; AC Q16622; Q5VVZ1; Q6NXF4; Q99430; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 24-JAN-2024, entry version 239. DE RecName: Full=Sterol carrier protein 2; DE Short=SCP-2; DE AltName: Full=Acetyl-CoA C-myristoyltransferase; DE EC=2.3.1.155 {ECO:0000250|UniProtKB:P11915}; DE AltName: Full=Non-specific lipid-transfer protein {ECO:0000305}; DE Short=NSL-TP; DE AltName: Full=Propanoyl-CoA C-acyltransferase; DE EC=2.3.1.176 {ECO:0000305|PubMed:10706581}; DE AltName: Full=SCP-2/3-oxoacyl-CoA thiolase; DE AltName: Full=SCP-2/thiolase; DE EC=2.3.1.16 {ECO:0000250|UniProtKB:P11915}; DE AltName: Full=SCP-chi; DE AltName: Full=SCPX; DE AltName: Full=Sterol carrier protein X; DE Short=SCP-X; GN Name=SCP2 {ECO:0000312|HGNC:HGNC:10606}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SCPX). RC TISSUE=Liver; RX PubMed=7698762; DOI=10.1006/geno.1994.1630; RA Ohba T., Rennert H., Pfeifer S.M., He Z., Yamamoto R., Holt J.A., RA Billheimer J.T., Strauss J.F. III; RT "The structure of the human sterol carrier protein X/sterol carrier protein RT 2 gene (SCP2)."; RL Genomics 24:370-374(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCPX). RC TISSUE=Liver; RX PubMed=1718316; DOI=10.1089/dna.1991.10.559; RA He Z., Yamamoto R., Furth E.E., Schantz L.J., Naylor S.L., George H., RA Billheimer J.T., Strauss J.F. III; RT "cDNAs encoding members of a family of proteins related to human sterol RT carrier protein 2 and assignment of the gene to human chromosome 1 p21- RT pter."; RL DNA Cell Biol. 10:559-569(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCP2). RC TISSUE=Liver; RX PubMed=1703300; DOI=10.1073/pnas.88.2.463; RA Yamamoto R., Kallen C.B., Babalola G.O., Rennert H., Billheimer J.T., RA Strauss J.F. III; RT "Cloning and expression of a cDNA encoding human sterol carrier protein RT 2."; RL Proc. Natl. Acad. Sci. U.S.A. 88:463-467(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCP2). RC TISSUE=Liver; RX PubMed=1483685; RA Yamamoto R.; RT "Localization of human sterol carrier protein 2 gene and cDNA expression in RT COS-7 cell."; RL Hokkaido Igaku Zasshi 67:839-848(1992). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 8), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-218 (ISOFORM 7). RC TISSUE=Brain, Caudate nucleus, and Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RA Heil O., Ebert L., Hennig S., Henze S., Radelof U., Schneider D., Korn B.; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND SCP2). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RG The MGC Project Team; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP PROTEIN SEQUENCE OF 455-462; 512-522 AND 535-546, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (MAR-2005) to UniProtKB. RN [12] RP MUTAGENESIS OF ASN-528 AND GLY-530, AND FUNCTION. RX PubMed=8300590; DOI=10.1016/s0021-9258(17)41988-0; RA Seedorf U., Scheek S., Engel T., Steif C., Hinz H.-J., Assmann G.; RT "Structure-activity studies of human sterol carrier protein 2."; RL J. Biol. Chem. 269:2613-2618(1994). RN [13] RP FUNCTION (ISOFORM SCP2), INVOLVEMENT IN DISEASE, AND CATALYTIC ACTIVITY RP (ISOFORM SCP2). RX PubMed=7642518; DOI=10.1074/jbc.270.32.18723; RA Puglielli L., Rigotti A., Greco A.V., Santos M.J., Nervi F.; RT "Sterol carrier protein-2 is involved in cholesterol transfer from the RT endoplasmic reticulum to the plasma membrane in human fibroblasts."; RL J. Biol. Chem. 270:18723-18726(1995). RN [14] RP FUNCTION (ISOFORM SCPX), AND CATALYTIC ACTIVITY. RX PubMed=10706581; RA Ferdinandusse S., Denis S., van Berkel E., Dacremont G., Wanders R.J.; RT "Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier RT protein X (SCPx). Activity measurements in liver and fibroblasts using a RT newly developed method."; RL J. Lipid Res. 41:336-342(2000). RN [15] RP ALTERNATIVE PROMOTER USAGE, AND INDUCTION BY 4-HYDROXY-TAMOXIFEN. RX PubMed=14563822; DOI=10.1194/jlr.m300111-jlr200; RA Dansen T.B., Kops G.J., Denis S., Jelluma N., Wanders R.J., Bos J.L., RA Burgering B.M., Wirtz K.W.; RT "Regulation of sterol carrier protein gene expression by the forkhead RT transcription factor FOXO3a."; RL J. Lipid Res. 45:81-88(2004). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-183; LYS-438 AND LYS-470, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [20] RP STRUCTURE BY NMR OF SCP2. RX PubMed=8243660; DOI=10.1016/0014-5793(93)80431-s; RA Szyperski T., Scheek S., Johansson J., Assmann G., Seedorf U., RA Wuethrich K.; RT "NMR determination of the secondary structure and the three-dimensional RT polypeptide backbone fold of the human sterol carrier protein 2."; RL FEBS Lett. 335:18-26(1993). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 426-547 IN COMPLEX WITH PEX5, RP FUNCTION (ISOFORM SCP2), SUBCELLULAR LOCATION (ISOFORM SCP2), AND RP INTERACTION WITH PEX5 (ISOFORM SCP2). RX PubMed=17157249; DOI=10.1016/j.molcel.2006.10.024; RA Stanley W.A., Filipp F.V., Kursula P., Schueller N., Erdmann R., RA Schliebs W., Sattler M., Wilmanns M.; RT "Recognition of a functional peroxisome type 1 target by the dynamic import RT receptor Pex5p."; RL Mol. Cell 24:653-663(2006). RN [22] RP INVOLVEMENT IN LKDMN. RX PubMed=16685654; DOI=10.1086/503921; RA Ferdinandusse S., Kostopoulos P., Denis S., Rusch H., Overmars H., RA Dillmann U., Reith W., Haas D., Wanders R.J., Duran M., Marziniak M.; RT "Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) RT cause leukencephalopathy with dystonia and motor neuropathy."; RL Am. J. Hum. Genet. 78:1046-1052(2006). RN [23] RP VARIANT [LARGE SCALE ANALYSIS] ASP-155. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: [Isoform SCPx]: Plays a crucial role in the peroxisomal CC oxidation of branched-chain fatty acids (PubMed:10706581). Catalyzes CC the last step of the peroxisomal beta-oxidation of branched chain fatty CC acids and the side chain of the bile acid intermediates di- and CC trihydroxycoprostanic acids (DHCA and THCA) (PubMed:10706581). Also CC active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates CC the microsomal conversion of 7-dehydrocholesterol to cholesterol and CC transfers phosphatidylcholine and 7-dehydrocholesterol between CC membrances, in vitro (By similarity). Isoforms SCP2 and SCPx cooperate CC in peroxisomal oxidation of certain naturally occurring tetramethyl- CC branched fatty acyl-CoAs (By similarity). CC {ECO:0000250|UniProtKB:P11915, ECO:0000250|UniProtKB:P32020, CC ECO:0000269|PubMed:10706581}. CC -!- FUNCTION: [Isoform SCP2]: Mediates the transfer of all common CC phospholipids, cholesterol and gangliosides from the endoplasmic CC reticulum to the plasma membrane. May play a role in regulating CC steroidogenesis (PubMed:17157249, PubMed:8300590, PubMed:7642518). CC Stimulates the microsomal conversion of 7-dehydrocholesterol to CC cholesterol (By similarity). Also binds fatty acids and fatty acyl CC Coenzyme A (CoA) such as phytanoyl-CoA. Involved in the regulation CC phospholipid synthesis in endoplasmic reticulum enhancing the CC incorporation of exogenous fatty acid into glycerides. Seems to CC stimulate the rate-limiting step in phosphatidic acid formation CC mediated by GPAT3. Isoforms SCP2 and SCPx cooperate in peroxisomal CC oxidation of certain naturally occurring tetramethyl-branched fatty CC acyl-CoAs (By similarity). {ECO:0000250|UniProtKB:P11915, CC ECO:0000250|UniProtKB:P32020, ECO:0000269|PubMed:17157249, CC ECO:0000269|PubMed:7642518, ECO:0000269|PubMed:8300590}. CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha- CC trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA; CC Xref=Rhea:RHEA:16865, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58507; EC=2.3.1.176; CC Evidence={ECO:0000305|PubMed:10706581}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16867; CC Evidence={ECO:0000305|PubMed:10706581}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3- CC oxopristanoyl-CoA + CoA; Xref=Rhea:RHEA:10408, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57291, ChEBI:CHEBI:57351, ChEBI:CHEBI:57392; CC EC=2.3.1.176; Evidence={ECO:0000250|UniProtKB:P11915, CC ECO:0000250|UniProtKB:P32020}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10410; CC Evidence={ECO:0000250|UniProtKB:P11915, CC ECO:0000250|UniProtKB:P32020}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:62619, ChEBI:CHEBI:62620; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA + CC tetradecanedioyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=propanoyl-CoA + tetradecanoyl-CoA = 3-oxo-2- CC methylhexadecanoyl-CoA + CoA; Xref=Rhea:RHEA:46344, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57392, CC ChEBI:CHEBI:86042; Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:46346; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31111, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57371, ChEBI:CHEBI:62418; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31087, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57386, ChEBI:CHEBI:62548; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:61430, ChEBI:CHEBI:62615; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31091, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57375, ChEBI:CHEBI:62543; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=acetyl-CoA + hexadecanoyl-CoA = 3-oxooctadecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:35279, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57379, ChEBI:CHEBI:71407; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=3-oxo-(9Z-octadecenoyl)-CoA + CoA = (7Z)-hexadecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:47400, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:87695, ChEBI:CHEBI:87698; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47401; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]: CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out); CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759; CC Evidence={ECO:0000250|UniProtKB:P11915}; CC -!- CATALYTIC ACTIVITY: [Isoform SCP2]: CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out); CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759; CC Evidence={ECO:0000269|PubMed:7642518}; CC -!- SUBUNIT: [Isoform SCP2]: Interacts with PEX5; the interaction is CC essential for peroxisomal import. {ECO:0000269|PubMed:17157249}. CC -!- INTERACTION: CC P22307; Q03135: CAV1; NbExp=3; IntAct=EBI-1050999, EBI-603614; CC P22307; Q15645: TRIP13; NbExp=4; IntAct=EBI-1050999, EBI-358993; CC P22307; P49817: Cav1; Xeno; NbExp=3; IntAct=EBI-1050999, EBI-1161338; CC P22307-3; P55212: CASP6; NbExp=3; IntAct=EBI-25834804, EBI-718729; CC P22307-3; O00291: HIP1; NbExp=3; IntAct=EBI-25834804, EBI-473886; CC P22307-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25834804, EBI-21591415; CC P22307-3; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-25834804, EBI-5280197; CC P22307-3; P62826: RAN; NbExp=3; IntAct=EBI-25834804, EBI-286642; CC -!- SUBCELLULAR LOCATION: [Isoform SCP2]: Peroxisome CC {ECO:0000250|UniProtKB:P32020}. Cytoplasm {ECO:0000269|PubMed:10706581, CC ECO:0000269|PubMed:17157249}. Mitochondrion CC {ECO:0000269|PubMed:17157249}. Endoplasmic reticulum CC {ECO:0000250|UniProtKB:P32020}. Mitochondrion CC {ECO:0000250|UniProtKB:P32020}. CC -!- SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome CC {ECO:0000250|UniProtKB:P11915}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=8; CC Name=SCPx {ECO:0000303|PubMed:17157249}; CC IsoId=P22307-1; Sequence=Displayed; CC Name=SCP2 {ECO:0000303|PubMed:17157249}; CC IsoId=P22307-2; Sequence=VSP_018977; CC Name=3; CC IsoId=P22307-3; Sequence=VSP_042686, VSP_042687; CC Name=4; CC IsoId=P22307-4; Sequence=VSP_045187; CC Name=5; CC IsoId=P22307-5; Sequence=VSP_018977, VSP_047269, VSP_047270; CC Name=6; CC IsoId=P22307-6; Sequence=VSP_018977, VSP_047268; CC Name=7; CC IsoId=P22307-7; Sequence=VSP_042686; CC Name=8; CC IsoId=P22307-8; Sequence=VSP_047267; CC -!- TISSUE SPECIFICITY: Liver, fibroblasts, and placenta. CC -!- INDUCTION: Up-regulated by 4-hydroxy-tamoxifen. CC {ECO:0000269|PubMed:14563822}. CC -!- PTM: [Isoform SCP2]: preSCP2, a protein with a molecular mass of about CC 15 kDa, is processed into its mature form (SCP2) by proteolytic CC cleavage of a 20 residue leader sequence after translocation into CC peroxisomes. {ECO:0000250|UniProtKB:O62742}. CC -!- DISEASE: Leukoencephalopathy with dystonia and motor neuropathy (LKDMN) CC [MIM:613724]: A syndrome characterized by leukoencephalopathy, dystonic CC head tremor, spasmodic torticollis and reduced tendon reflexes in lower CC extremities. Additional features include hyposmia, pathologic saccadic CC eye movements, a slight hypoacusis, accumulation of branched-chain CC pristanic acid in plasma, and the presence of abnormal bile alcohol CC glucuronides in urine. {ECO:0000269|PubMed:16685654}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Note=Expression at protein level is almost abolished in CC Zellweger syndrome. Cholesterol transfer from the endoplasmic reticulum CC to the plasma membrane was reduced in patient fibroblasts compared to CC controls. {ECO:0000269|PubMed:7642518}. CC -!- MISCELLANEOUS: [Isoform SCP2]: Contains a putative mitochondrial CC transit peptide at positions 1-20. {ECO:0000305|PubMed:17157249}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- SIMILARITY: In the N-terminal section; belongs to the thiolase-like CC superfamily. Thiolase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA03558.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U11313; AAB41286.1; -; Genomic_DNA. DR EMBL; U11297; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11299; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11300; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11301; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11302; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11303; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11304; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11305; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11306; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11307; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11308; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11309; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11310; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11311; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; U11312; AAB41286.1; JOINED; Genomic_DNA. DR EMBL; M75883; AAA03557.1; -; mRNA. DR EMBL; M75884; AAA03558.1; ALT_INIT; mRNA. DR EMBL; M55421; AAA03559.1; -; mRNA. DR EMBL; S52450; AAB24921.1; -; mRNA. DR EMBL; AK294631; BAG57810.1; -; mRNA. DR EMBL; AK295214; BAG58208.1; -; mRNA. DR EMBL; AK308105; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CR995014; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC099677; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445183; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06760.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06761.1; -; Genomic_DNA. DR EMBL; BC005911; AAH05911.1; -; mRNA. DR EMBL; BC067108; AAH67108.1; -; mRNA. DR EMBL; CB997588; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS30719.1; -. [P22307-5] DR CCDS; CCDS41338.1; -. [P22307-3] DR CCDS; CCDS44149.1; -. [P22307-2] DR CCDS; CCDS44150.1; -. [P22307-6] DR CCDS; CCDS53317.1; -. [P22307-7] DR CCDS; CCDS53318.1; -. [P22307-8] DR CCDS; CCDS53319.1; -. [P22307-4] DR CCDS; CCDS572.1; -. [P22307-1] DR PIR; B40407; B40407. DR PIR; I38205; I38205. DR RefSeq; NP_001007099.1; NM_001007098.2. [P22307-3] DR RefSeq; NP_001007100.1; NM_001007099.2. [P22307-2] DR RefSeq; NP_001007101.1; NM_001007100.2. [P22307-6] DR RefSeq; NP_001007251.1; NM_001007250.2. [P22307-5] DR RefSeq; NP_001180528.1; NM_001193599.1. [P22307-8] DR RefSeq; NP_001180546.1; NM_001193617.1. [P22307-4] DR RefSeq; NP_002970.2; NM_002979.4. [P22307-1] DR RefSeq; XP_016857535.1; XM_017002046.1. DR PDB; 1QND; NMR; -; A=425-547. DR PDB; 2C0L; X-ray; 2.30 A; B=426-547. DR PDBsum; 1QND; -. DR PDBsum; 2C0L; -. DR AlphaFoldDB; P22307; -. DR BMRB; P22307; -. DR SMR; P22307; -. DR BioGRID; 112246; 62. DR ELM; P22307; -. DR IntAct; P22307; 29. DR MINT; P22307; -. DR STRING; 9606.ENSP00000360569; -. DR BindingDB; P22307; -. DR ChEMBL; CHEMBL5950; -. DR iPTMnet; P22307; -. DR MetOSite; P22307; -. DR PhosphoSitePlus; P22307; -. DR SwissPalm; P22307; -. DR BioMuta; SCP2; -. DR DMDM; 2507456; -. DR REPRODUCTION-2DPAGE; IPI00026105; -. DR EPD; P22307; -. DR jPOST; P22307; -. DR MassIVE; P22307; -. DR MaxQB; P22307; -. DR PaxDb; 9606-ENSP00000360569; -. DR PeptideAtlas; P22307; -. DR ProteomicsDB; 1519; -. DR ProteomicsDB; 15203; -. DR ProteomicsDB; 23994; -. DR ProteomicsDB; 4236; -. DR ProteomicsDB; 53978; -. [P22307-1] DR ProteomicsDB; 53979; -. [P22307-2] DR ProteomicsDB; 53980; -. [P22307-3] DR ProteomicsDB; 9559; -. DR Pumba; P22307; -. DR TopDownProteomics; P22307-1; -. [P22307-1] DR TopDownProteomics; P22307-2; -. [P22307-2] DR TopDownProteomics; P22307-4; -. [P22307-4] DR Antibodypedia; 19167; 526 antibodies from 33 providers. DR DNASU; 6342; -. DR Ensembl; ENST00000371509.8; ENSP00000360564.4; ENSG00000116171.19. [P22307-7] DR Ensembl; ENST00000371513.9; ENSP00000360568.5; ENSG00000116171.19. [P22307-3] DR Ensembl; ENST00000371514.8; ENSP00000360569.3; ENSG00000116171.19. [P22307-1] DR Ensembl; ENST00000407246.6; ENSP00000384569.2; ENSG00000116171.19. [P22307-8] DR Ensembl; ENST00000408941.7; ENSP00000386214.3; ENSG00000116171.19. [P22307-5] DR Ensembl; ENST00000430330.6; ENSP00000406636.2; ENSG00000116171.19. [P22307-6] DR Ensembl; ENST00000435345.6; ENSP00000396413.2; ENSG00000116171.19. [P22307-2] DR Ensembl; ENST00000488965.1; ENSP00000435783.1; ENSG00000116171.19. [P22307-5] DR Ensembl; ENST00000528311.5; ENSP00000434132.1; ENSG00000116171.19. [P22307-4] DR GeneID; 6342; -. DR KEGG; hsa:6342; -. DR MANE-Select; ENST00000371514.8; ENSP00000360569.3; NM_002979.5; NP_002970.2. DR UCSC; uc001cuq.3; human. [P22307-1] DR AGR; HGNC:10606; -. DR CTD; 6342; -. DR DisGeNET; 6342; -. DR GeneCards; SCP2; -. DR HGNC; HGNC:10606; SCP2. DR HPA; ENSG00000116171; Tissue enhanced (liver). DR MalaCards; SCP2; -. DR MIM; 184755; gene. DR MIM; 613724; phenotype. DR neXtProt; NX_P22307; -. DR OpenTargets; ENSG00000116171; -. DR Orphanet; 163684; Leukoencephalopathy-dystonia-motor neuropathy syndrome. DR PharmGKB; PA35014; -. DR VEuPathDB; HostDB:ENSG00000116171; -. DR eggNOG; KOG1406; Eukaryota. DR eggNOG; KOG4170; Eukaryota. DR GeneTree; ENSGT00940000154327; -. DR HOGENOM; CLU_035425_0_1_1; -. DR InParanoid; P22307; -. DR OMA; PSLYAMM; -. DR OrthoDB; 1799125at2759; -. DR PhylomeDB; P22307; -. DR TreeFam; TF300574; -. DR BioCyc; MetaCyc:HS03991-MONOMER; -. DR BRENDA; 2.3.1.176; 2681. DR PathwayCommons; P22307; -. DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol. [P22307-1] DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism. DR Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA. [P22307-1] DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR Reactome; R-HSA-9033500; TYSND1 cleaves peroxisomal proteins. DR SignaLink; P22307; -. DR SIGNOR; P22307; -. DR BioGRID-ORCS; 6342; 12 hits in 1157 CRISPR screens. DR ChiTaRS; SCP2; human. DR EvolutionaryTrace; P22307; -. DR GeneWiki; SCP2; -. DR GenomeRNAi; 6342; -. DR Pharos; P22307; Tchem. DR PRO; PR:P22307; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P22307; Protein. DR Bgee; ENSG00000116171; Expressed in jejunal mucosa and 212 other cell types or tissues. DR ExpressionAtlas; P22307; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:HPA. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; ISS:UniProtKB. DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; ISS:UniProtKB. DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB. DR GO; GO:0120020; F:cholesterol transfer activity; IMP:UniProtKB. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:UniProtKB. DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IDA:UniProtKB. DR GO; GO:0070538; F:oleic acid binding; IDA:UniProtKB. DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS:UniProtKB. DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:UniProtKB. DR GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; EXP:Reactome. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome. DR GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome. DR GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB. DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB. DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome. DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IDA:UniProtKB. DR GO; GO:0032367; P:intracellular cholesterol transport; IMP:UniProtKB. DR GO; GO:1901373; P:lipid hydroperoxide transport; IDA:UniProtKB. DR GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB. DR GO; GO:0032385; P:positive regulation of intracellular cholesterol transport; IDA:UniProtKB. DR GO; GO:0045940; P:positive regulation of steroid metabolic process; IDA:UniProtKB. DR GO; GO:0006701; P:progesterone biosynthetic process; IDA:UniProtKB. DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB. DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; ISS:UniProtKB. DR GO; GO:0006694; P:steroid biosynthetic process; IDA:UniProtKB. DR CDD; cd00826; nondecarbox_cond_enzymes; 1. DR Gene3D; 3.40.47.10; -; 1. DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1. DR InterPro; IPR003033; SCP2_sterol-bd_dom. DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS. DR InterPro; IPR020617; Thiolase_C. DR InterPro; IPR020613; Thiolase_CS. DR InterPro; IPR020616; Thiolase_N. DR PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1. DR PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 1. DR Pfam; PF02036; SCP2; 1. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR SUPFAM; SSF55718; SCP-like; 1. DR SUPFAM; SSF53901; Thiolase-like; 2. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR Genevisible; P22307; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Alternative promoter usage; KW Alternative splicing; Cytoplasm; Direct protein sequencing; KW Endoplasmic reticulum; Lipid metabolism; Lipid transport; Lipid-binding; KW Mitochondrion; Peroxisome; Phosphoprotein; Reference proteome; Transferase; KW Transport. FT CHAIN 1..547 FT /note="Sterol carrier protein 2" FT /id="PRO_0000034091" FT DOMAIN 433..543 FT /note="SCP2" FT MOTIF 545..547 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11915" FT MOD_RES 132 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 132 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 168 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 173 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 177 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 183 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 183 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 282 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 341 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 341 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 432 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 432 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 438 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 438 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 443 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 443 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 453 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 453 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 464 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 470 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 470 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 479 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 491 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 492 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 511 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 522 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT MOD_RES 534 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P32020" FT VAR_SEQ 1..404 FT /note="Missing (in isoform SCP2, isoform 5 and isoform 6)" FT /evidence="ECO:0000303|PubMed:1483685, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1703300, FT ECO:0000303|Ref.10, ECO:0000303|Ref.6" FT /id="VSP_018977" FT VAR_SEQ 1..81 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045187" FT VAR_SEQ 43..66 FT /note="Missing (in isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047267" FT VAR_SEQ 67..110 FT /note="Missing (in isoform 3 and isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_042686" FT VAR_SEQ 362..547 FT /note="LAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLYKMGFPEAASS FT FRTHQIEAVPTSSASDGFKANLVFKEIEKKLEEEGEQFVKKIGGIFAFKVKDGPGGKEA FT TWVVDVKNGKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGL FT AMKLQNLQLQPGNAKL -> GHSCS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042687" FT VAR_SEQ 412..414 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_047268" FT VAR_SEQ 447..463 FT /note="EGEQFVKKIGGIFAFKV -> IRRLTAQSQWLTQTSWL (in isoform FT 5)" FT /evidence="ECO:0000303|Ref.10" FT /id="VSP_047269" FT VAR_SEQ 464..547 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.10" FT /id="VSP_047270" FT VARIANT 155 FT /note="A -> D (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035706" FT MUTAGEN 528 FT /note="N->D: Strongly reduces sterol carrier and FT phosphatidylcholine transfer activity; when associated with FT D-530." FT /evidence="ECO:0000269|PubMed:8300590" FT MUTAGEN 528 FT /note="N->I: Strongly reduces sterol carrier and FT phosphatidylcholine transfer activity." FT /evidence="ECO:0000269|PubMed:8300590" FT MUTAGEN 530 FT /note="G->D: Strongly reduces sterol carrier and FT phosphatidylcholine transfer activity; when associated with FT D-528." FT /evidence="ECO:0000269|PubMed:8300590" FT CONFLICT 10 FT /note="T -> A (in Ref. 1; AAB41286)" FT /evidence="ECO:0000305" FT CONFLICT 56 FT /note="A -> V (in Ref. 5; AK308105)" FT /evidence="ECO:0000305" FT CONFLICT 116 FT /note="V -> A (in Ref. 5; AK308105)" FT /evidence="ECO:0000305" FT CONFLICT 341 FT /note="K -> Q (in Ref. 5; BAG57810)" FT /evidence="ECO:0000305" FT CONFLICT 393 FT /note="G -> D (in Ref. 1; AAB41286)" FT /evidence="ECO:0000305" FT CONFLICT 472 FT /note="A -> D (in Ref. 4; AAB24921)" FT /evidence="ECO:0000305" FT CONFLICT 482 FT /note="K -> Q (in Ref. 4; AAB24921)" FT /evidence="ECO:0000305" FT CONFLICT 501 FT /note="D -> A (in Ref. 4; AAB24921)" FT /evidence="ECO:0000305" FT CONFLICT 522 FT /note="K -> P (in Ref. 4; AAB24921)" FT /evidence="ECO:0000305" FT TURN 427..430 FT /evidence="ECO:0007829|PDB:2C0L" FT HELIX 432..454 FT /evidence="ECO:0007829|PDB:2C0L" FT STRAND 457..465 FT /evidence="ECO:0007829|PDB:2C0L" FT HELIX 467..469 FT /evidence="ECO:0007829|PDB:2C0L" FT STRAND 472..480 FT /evidence="ECO:0007829|PDB:2C0L" FT STRAND 484..487 FT /evidence="ECO:0007829|PDB:1QND" FT STRAND 494..500 FT /evidence="ECO:0007829|PDB:2C0L" FT HELIX 501..508 FT /evidence="ECO:0007829|PDB:2C0L" FT TURN 509..511 FT /evidence="ECO:0007829|PDB:2C0L" FT HELIX 514..519 FT /evidence="ECO:0007829|PDB:2C0L" FT STRAND 524..527 FT /evidence="ECO:0007829|PDB:2C0L" FT HELIX 529..533 FT /evidence="ECO:0007829|PDB:2C0L" FT HELIX 534..538 FT /evidence="ECO:0007829|PDB:2C0L" FT SITE P22307-2:20..21 FT /note="Cleavage" FT /evidence="ECO:0000305" SQ SEQUENCE 547 AA; 58994 MW; 29F7551465C7143A CRC64; MSSSPWEPAT LRRVFVVGVG MTKFVKPGAE NSRDYPDLAE EAGKKALADA QIPYSAVDQA CVGYVFGDST CGQRAIYHSL GMTGIPIINV NNNCATGSTA LFMARQLIQG GVAECVLALG FEKMSKGSLG IKFSDRTIPT DKHVDLLINK YGLSAHPVAP QMFGYAGKEH MEKYGTKIEH FAKIGWKNHK HSVNNPYSQF QDEYSLDEVM ASKEVFDFLT ILQCCPTSDG AAAAILASEA FVQKYGLQSK AVEILAQEMM TDLPSSFEEK SIIKMVGFDM SKEAARKCYE KSGLTPNDID VIELHDCFST NELLTYEALG LCPEGQGATL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGIGGAVVV TLYKMGFPEA ASSFRTHQIE AVPTSSASDG FKANLVFKEI EKKLEEEGEQ FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPNSD KKADCTITMA DSDFLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL QPGNAKL //