SCP2_HUMAN
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 03-AUG-2022, entry version 231.
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};
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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; 54.
DR ELM; P22307; -.
DR IntAct; P22307; 27.
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; P22307; -.
DR PeptideAtlas; P22307; -.
DR PRIDE; 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 TopDownProteomics; P22307-1; -. [P22307-1]
DR TopDownProteomics; P22307-2; -. [P22307-2]
DR TopDownProteomics; P22307-4; -. [P22307-4]
DR Antibodypedia; 19167; 481 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 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 PhylomeDB; P22307; -.
DR TreeFam; TF300574; -.
DR BioCyc; MetaCyc:HS03991-MON; -.
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 1082 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 210 other tissues.
DR ExpressionAtlas; P22307; baseline and differential.
DR Genevisible; P22307; HS.
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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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:UniProtKB.
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:0032934; F:sterol binding; IBA:GO_Central.
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 Gene3D; 3.30.1050.10; -; 1.
DR Gene3D; 3.40.47.10; -; 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 Pfam; PF02036; SCP2; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF55718; SSF55718; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
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
