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Non-specific lipid-transfer protein (NSL-TP) (EC 2.3.1.176) (Propanoyl-CoA C-acyltransferase) (SCP-chi) (SCPX) (Sterol carrier protein 2) (SCP-2) (Sterol carrier protein X) (SCP-X)

 NLTP_HUMAN              Reviewed;         547 AA.
P22307; A6NM69; B4DGJ9; B4DHP6; C9JC79; D3DQ37; E1B6W5; F2Z3J1;
Q15432; Q16622; Q5VVZ1; Q6NXF4; Q99430;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
27-SEP-2017, entry version 200.
RecName: Full=Non-specific lipid-transfer protein;
Short=NSL-TP;
EC=2.3.1.176;
AltName: Full=Propanoyl-CoA C-acyltransferase;
AltName: Full=SCP-chi;
AltName: Full=SCPX;
AltName: Full=Sterol carrier protein 2;
Short=SCP-2;
AltName: Full=Sterol carrier protein X;
Short=SCP-X;
Name=SCP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SCPX).
TISSUE=Liver;
PubMed=7698762; DOI=10.1006/geno.1994.1630;
Ohba T., Rennert H., Pfeifer S.M., He Z., Yamamoto R., Holt J.A.,
Billheimer J.T., Strauss J.F. III;
"The structure of the human sterol carrier protein X/sterol carrier
protein 2 gene (SCP2).";
Genomics 24:370-374(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCPX).
TISSUE=Liver;
PubMed=1718316; DOI=10.1089/dna.1991.10.559;
He Z., Yamamoto R., Furth E.E., Schantz L.J., Naylor S.L., George H.,
Billheimer J.T., Strauss J.F. III;
"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. 10:559-569(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCP2).
TISSUE=Liver;
PubMed=1703300; DOI=10.1073/pnas.88.2.463;
Yamamoto R., Kallen C.B., Babalola G.O., Rennert H., Billheimer J.T.,
Strauss J.F. III;
"Cloning and expression of a cDNA encoding human sterol carrier
protein 2.";
Proc. Natl. Acad. Sci. U.S.A. 88:463-467(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCP2).
TISSUE=Liver;
PubMed=1483685;
Yamamoto R.;
"Localization of human sterol carrier protein 2 gene and cDNA
expression in COS-7 cell.";
Hokkaido Igaku Zasshi 67:839-848(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 8), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-218 (ISOFORM 7).
TISSUE=Brain, Caudate nucleus, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Heil O., Ebert L., Hennig S., Henze S., Radelof U., Schneider D.,
Korn B.;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND SCP2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
The MGC Project Team;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 455-462; 512-522 AND 535-546, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[12]
ALTERNATIVE PROMOTER USAGE, AND INDUCTION BY 4-HYDROXY-TAMOXIFEN.
PubMed=14563822; DOI=10.1194/jlr.M300111-JLR200;
Dansen T.B., Kops G.J., Denis S., Jelluma N., Wanders R.J., Bos J.L.,
Burgering B.M., Wirtz K.W.;
"Regulation of sterol carrier protein gene expression by the forkhead
transcription factor FOXO3a.";
J. Lipid Res. 45:81-88(2004).
[13]
INVOLVEMENT IN LKDMN.
PubMed=16685654; DOI=10.1086/503921;
Ferdinandusse S., Kostopoulos P., Denis S., Rusch H., Overmars H.,
Dillmann U., Reith W., Haas D., Wanders R.J., Duran M., Marziniak M.;
"Mutations in the gene encoding peroxisomal sterol carrier protein X
(SCPx) cause leukencephalopathy with dystonia and motor neuropathy.";
Am. J. Hum. Genet. 78:1046-1052(2006).
[14]
MUTAGENESIS OF ASN-528 AND GLY-530, AND FUNCTION.
PubMed=8300590;
Seedorf U., Scheek S., Engel T., Steif C., Hinz H.-J., Assmann G.;
"Structure-activity studies of human sterol carrier protein 2.";
J. Biol. Chem. 269:2613-2618(1994).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-183; LYS-438 AND LYS-470,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
STRUCTURE BY NMR OF SCP2.
PubMed=8243660; DOI=10.1016/0014-5793(93)80431-S;
Szyperski T., Scheek S., Johansson J., Assmann G., Seedorf U.,
Wuethrich K.;
"NMR determination of the secondary structure and the three-
dimensional polypeptide backbone fold of the human sterol carrier
protein 2.";
FEBS Lett. 335:18-26(1993).
[20]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 426-547 IN COMPLEX WITH PEX5,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17157249; DOI=10.1016/j.molcel.2006.10.024;
Stanley W.A., Filipp F.V., Kursula P., Schueller N., Erdmann R.,
Schliebs W., Sattler M., Wilmanns M.;
"Recognition of a functional peroxisome type 1 target by the dynamic
import receptor Pex5p.";
Mol. Cell 24:653-663(2006).
[21]
VARIANT [LARGE SCALE ANALYSIS] ASP-155.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Mediates in vitro the transfer of all common
phospholipids, cholesterol and gangliosides between membranes. May
play a role in regulating steroidogenesis.
{ECO:0000269|PubMed:17157249, ECO:0000269|PubMed:8300590}.
-!- CATALYTIC ACTIVITY: 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-
cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-
trihydroxy-24-oxo-5-beta-cholestanoyl-CoA.
-!- SUBUNIT: Interacts with PEX5. {ECO:0000269|PubMed:17157249}.
-!- INTERACTION:
Q03135:CAV1; NbExp=3; IntAct=EBI-1050999, EBI-603614;
P49817:Cav1 (xeno); NbExp=3; IntAct=EBI-1050999, EBI-1161338;
Q15645:TRIP13; NbExp=4; IntAct=EBI-1050999, EBI-358993;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17157249}.
Mitochondrion {ECO:0000269|PubMed:17157249}. Note=Cytoplasmic in
the liver and also associated with mitochondria especially in
steroidogenic tissues.
-!- SUBCELLULAR LOCATION: Isoform SCPx: Peroxisome. Note=Interaction
with PEX5 is essential for peroxisomal import.
-!- SUBCELLULAR LOCATION: Isoform SCP2: Mitochondrion {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=8;
Name=SCPx;
IsoId=P22307-1; Sequence=Displayed;
Name=SCP2;
IsoId=P22307-2; Sequence=VSP_018977;
Note=Contains a mitochondrial transit peptide at positions 1-20.
{ECO:0000305};
Name=3;
IsoId=P22307-3; Sequence=VSP_042686, VSP_042687;
Name=4;
IsoId=P22307-4; Sequence=VSP_045187;
Note=Produced by alternative splicing. No experimental
confirmation available.;
Name=5;
IsoId=P22307-5; Sequence=VSP_018977, VSP_047269, VSP_047270;
Name=6;
IsoId=P22307-6; Sequence=VSP_018977, VSP_047268;
Name=7;
IsoId=P22307-7; Sequence=VSP_042686;
Note=Produced by alternative splicing.;
Name=8;
IsoId=P22307-8; Sequence=VSP_047267;
Note=Produced by alternative splicing.;
-!- TISSUE SPECIFICITY: Liver, fibroblasts, and placenta.
-!- INDUCTION: Up-regulated by 4-hydroxy-tamoxifen.
{ECO:0000269|PubMed:14563822}.
-!- DISEASE: Leukoencephalopathy with dystonia and motor neuropathy
(LKDMN) [MIM:613724]: A syndrome characterized by
leukoencephalopathy, dystonic head tremor, spasmodic torticollis
and reduced tendon reflexes in lower extremities. Additional
features include hyposmia, pathologic saccadic eye movements, a
slight hypoacusis, accumulation of branched-chain pristanic acid
in plasma, and the presence of abnormal bile alcohol glucuronides
in urine. {ECO:0000269|PubMed:16685654}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: In the N-terminal section; belongs to the thiolase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA03558.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U11313; AAB41286.1; -; Genomic_DNA.
EMBL; U11297; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11299; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11300; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11301; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11302; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11303; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11304; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11305; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11306; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11307; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11308; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11309; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11310; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11311; AAB41286.1; JOINED; Genomic_DNA.
EMBL; U11312; AAB41286.1; JOINED; Genomic_DNA.
EMBL; M75883; AAA03557.1; -; mRNA.
EMBL; M75884; AAA03558.1; ALT_INIT; mRNA.
EMBL; M55421; AAA03559.1; -; mRNA.
EMBL; S52450; AAB24921.1; -; mRNA.
EMBL; AK294631; BAG57810.1; -; mRNA.
EMBL; AK295214; BAG58208.1; -; mRNA.
EMBL; AK308105; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CR995014; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL445183; CAH72590.1; -; Genomic_DNA.
EMBL; AC099677; CAH72590.1; JOINED; Genomic_DNA.
EMBL; CH471059; EAX06760.1; -; Genomic_DNA.
EMBL; CH471059; EAX06761.1; -; Genomic_DNA.
EMBL; BC005911; AAH05911.1; -; mRNA.
EMBL; BC067108; AAH67108.1; -; mRNA.
EMBL; CB997588; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS30719.1; -. [P22307-5]
CCDS; CCDS41338.1; -. [P22307-3]
CCDS; CCDS44149.1; -. [P22307-2]
CCDS; CCDS44150.1; -. [P22307-6]
CCDS; CCDS53317.1; -. [P22307-7]
CCDS; CCDS53318.1; -. [P22307-8]
CCDS; CCDS53319.1; -. [P22307-4]
CCDS; CCDS572.1; -. [P22307-1]
PIR; B40407; B40407.
PIR; I38205; I38205.
RefSeq; NP_001007099.1; NM_001007098.2. [P22307-3]
RefSeq; NP_001007100.1; NM_001007099.2. [P22307-2]
RefSeq; NP_001007101.1; NM_001007100.2. [P22307-6]
RefSeq; NP_001007251.1; NM_001007250.2. [P22307-5]
RefSeq; NP_001180528.1; NM_001193599.1. [P22307-8]
RefSeq; NP_001180546.1; NM_001193617.1. [P22307-4]
RefSeq; NP_002970.2; NM_002979.4. [P22307-1]
RefSeq; XP_016857535.1; XM_017002046.1. [P22307-2]
UniGene; Hs.476365; -.
PDB; 1QND; NMR; -; A=425-547.
PDB; 2C0L; X-ray; 2.30 A; B=426-547.
PDBsum; 1QND; -.
PDBsum; 2C0L; -.
ProteinModelPortal; P22307; -.
SMR; P22307; -.
BioGrid; 112246; 38.
ELM; P22307; -.
IntAct; P22307; 12.
MINT; MINT-3009685; -.
STRING; 9606.ENSP00000360569; -.
BindingDB; P22307; -.
ChEMBL; CHEMBL5950; -.
iPTMnet; P22307; -.
PhosphoSitePlus; P22307; -.
SwissPalm; P22307; -.
BioMuta; SCP2; -.
DMDM; 2507456; -.
REPRODUCTION-2DPAGE; IPI00026105; -.
EPD; P22307; -.
MaxQB; P22307; -.
PaxDb; P22307; -.
PeptideAtlas; P22307; -.
PRIDE; P22307; -.
TopDownProteomics; P22307-1; -. [P22307-1]
TopDownProteomics; P22307-2; -. [P22307-2]
TopDownProteomics; P22307-4; -. [P22307-4]
DNASU; 6342; -.
Ensembl; ENST00000371509; ENSP00000360564; ENSG00000116171. [P22307-7]
Ensembl; ENST00000371513; ENSP00000360568; ENSG00000116171. [P22307-3]
Ensembl; ENST00000371514; ENSP00000360569; ENSG00000116171. [P22307-1]
Ensembl; ENST00000407246; ENSP00000384569; ENSG00000116171. [P22307-8]
Ensembl; ENST00000408941; ENSP00000386214; ENSG00000116171. [P22307-5]
Ensembl; ENST00000430330; ENSP00000406636; ENSG00000116171. [P22307-6]
Ensembl; ENST00000435345; ENSP00000396413; ENSG00000116171. [P22307-2]
Ensembl; ENST00000488965; ENSP00000435783; ENSG00000116171. [P22307-5]
Ensembl; ENST00000528311; ENSP00000434132; ENSG00000116171. [P22307-4]
GeneID; 6342; -.
KEGG; hsa:6342; -.
UCSC; uc001cuq.3; human. [P22307-1]
CTD; 6342; -.
DisGeNET; 6342; -.
EuPathDB; HostDB:ENSG00000116171.16; -.
GeneCards; SCP2; -.
HGNC; HGNC:10606; SCP2.
HPA; HPA027101; -.
HPA; HPA027135; -.
HPA; HPA027317; -.
MalaCards; SCP2; -.
MIM; 184755; gene.
MIM; 613724; phenotype.
neXtProt; NX_P22307; -.
OpenTargets; ENSG00000116171; -.
Orphanet; 163684; Leukoencephalopathy - dystonia - motor neuropathy.
PharmGKB; PA35014; -.
eggNOG; KOG1406; Eukaryota.
eggNOG; KOG4170; Eukaryota.
eggNOG; ENOG410XPRW; LUCA.
GeneTree; ENSGT00530000062928; -.
HOGENOM; HOG000221741; -.
HOVERGEN; HBG006506; -.
InParanoid; P22307; -.
KO; K08764; -.
OMA; GLKACGH; -.
OrthoDB; EOG091G026S; -.
PhylomeDB; P22307; -.
TreeFam; TF300574; -.
BioCyc; MetaCyc:HS03991-MONOMER; -.
BRENDA; 2.3.1.176; 2681.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
ChiTaRS; SCP2; human.
EvolutionaryTrace; P22307; -.
GeneWiki; SCP2; -.
GenomeRNAi; 6342; -.
PRO; PR:P22307; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116171; -.
CleanEx; HS_SCP2; -.
ExpressionAtlas; P22307; baseline and differential.
Genevisible; P22307; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:UniProtKB.
GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IDA:UniProtKB.
GO; GO:0070538; F:oleic acid binding; IDA:UniProtKB.
GO; GO:0008526; F:phosphatidylinositol transporter activity; IDA:UniProtKB.
GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; EXP:Reactome.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IDA:UniProtKB.
GO; GO:1901373; P:lipid hydroperoxide transport; IDA:UniProtKB.
GO; GO:0007031; P:peroxisome organization; IEA:Ensembl.
GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
GO; GO:0032385; P:positive regulation of intracellular cholesterol transport; IDA:UniProtKB.
GO; GO:0045940; P:positive regulation of steroid metabolic process; IDA:UniProtKB.
GO; GO:0006701; P:progesterone biosynthetic process; IDA:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0006694; P:steroid biosynthetic process; IDA:UniProtKB.
Gene3D; 3.30.1050.10; -; 1.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR003033; SCP2_sterol-bd_dom.
InterPro; IPR016039; Thiolase-like.
InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
InterPro; IPR020617; Thiolase_C.
InterPro; IPR020613; Thiolase_CS.
InterPro; IPR020616; Thiolase_N.
Pfam; PF02036; SCP2; 1.
Pfam; PF02803; Thiolase_C; 1.
Pfam; PF00108; Thiolase_N; 1.
SUPFAM; SSF53901; SSF53901; 2.
SUPFAM; SSF55718; SSF55718; 1.
PROSITE; PS00098; THIOLASE_1; 1.
PROSITE; PS00737; THIOLASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Acyltransferase; Alternative initiation;
Alternative promoter usage; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Lipid transport; Lipid-binding;
Mitochondrion; Peroxisome; Phosphoprotein; Polymorphism;
Reference proteome; Transferase; Transport.
CHAIN 1 547 Non-specific lipid-transfer protein.
/FTId=PRO_0000034091.
DOMAIN 433 543 SCP2.
MOTIF 545 547 Microbody targeting signal.
{ECO:0000255}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P11915}.
MOD_RES 132 132 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 132 132 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 168 168 N6-succinyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 173 173 N6-acetyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 177 177 N6-acetyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 183 183 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 183 183 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 282 282 N6-succinyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 341 341 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 341 341 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 432 432 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 432 432 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 438 438 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 438 438 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 443 443 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 443 443 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 453 453 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 453 453 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 464 464 N6-succinyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 470 470 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 470 470 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 479 479 N6-succinyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 491 491 N6-acetyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 492 492 N6-succinyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 511 511 N6-succinyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 516 516 Phosphoserine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 522 522 N6-succinyllysine.
{ECO:0000250|UniProtKB:P32020}.
MOD_RES 534 534 N6-succinyllysine.
{ECO:0000250|UniProtKB:P32020}.
VAR_SEQ 1 404 Missing (in isoform SCP2, isoform 5 and
isoform 6). {ECO:0000303|PubMed:1483685,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1703300,
ECO:0000303|Ref.10, ECO:0000303|Ref.6}.
/FTId=VSP_018977.
VAR_SEQ 1 81 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045187.
VAR_SEQ 43 66 Missing (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047267.
VAR_SEQ 67 110 Missing (in isoform 3 and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_042686.
VAR_SEQ 362 547 LAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTL
YKMGFPEAASSFRTHQIEAVPTSSASDGFKANLVFKEIEKK
LEEEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGS
VLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKI
TGNMGLAMKLQNLQLQPGNAKL -> GHSCS (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042687.
VAR_SEQ 412 414 Missing (in isoform 6).
{ECO:0000303|Ref.6}.
/FTId=VSP_047268.
VAR_SEQ 447 463 EGEQFVKKIGGIFAFKV -> IRRLTAQSQWLTQTSWL
(in isoform 5). {ECO:0000303|Ref.10}.
/FTId=VSP_047269.
VAR_SEQ 464 547 Missing (in isoform 5).
{ECO:0000303|Ref.10}.
/FTId=VSP_047270.
VARIANT 155 155 A -> D (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035706.
MUTAGEN 528 528 N->D: Strongly reduces sterol carrier and
phosphatidylcholine transfer activity;
when associated with D-530.
{ECO:0000269|PubMed:8300590}.
MUTAGEN 528 528 N->I: Strongly reduces sterol carrier and
phosphatidylcholine transfer activity.
{ECO:0000269|PubMed:8300590}.
MUTAGEN 530 530 G->D: Strongly reduces sterol carrier and
phosphatidylcholine transfer activity;
when associated with D-528.
{ECO:0000269|PubMed:8300590}.
CONFLICT 10 10 T -> A (in Ref. 1; AAB41286).
{ECO:0000305}.
CONFLICT 56 56 A -> V (in Ref. 5; AK308105).
{ECO:0000305}.
CONFLICT 116 116 V -> A (in Ref. 5; AK308105).
{ECO:0000305}.
CONFLICT 341 341 K -> Q (in Ref. 5; BAG57810).
{ECO:0000305}.
CONFLICT 393 393 G -> D (in Ref. 1; AAB41286).
{ECO:0000305}.
CONFLICT 472 472 A -> D (in Ref. 4; AAB24921).
{ECO:0000305}.
CONFLICT 482 482 K -> Q (in Ref. 4; AAB24921).
{ECO:0000305}.
CONFLICT 501 501 D -> A (in Ref. 4; AAB24921).
{ECO:0000305}.
CONFLICT 522 522 K -> P (in Ref. 4; AAB24921).
{ECO:0000305}.
TURN 427 430 {ECO:0000244|PDB:2C0L}.
HELIX 432 454 {ECO:0000244|PDB:2C0L}.
STRAND 457 465 {ECO:0000244|PDB:2C0L}.
HELIX 467 469 {ECO:0000244|PDB:2C0L}.
STRAND 472 480 {ECO:0000244|PDB:2C0L}.
STRAND 484 487 {ECO:0000244|PDB:1QND}.
STRAND 494 500 {ECO:0000244|PDB:2C0L}.
HELIX 501 508 {ECO:0000244|PDB:2C0L}.
TURN 509 511 {ECO:0000244|PDB:2C0L}.
HELIX 514 519 {ECO:0000244|PDB:2C0L}.
STRAND 524 527 {ECO:0000244|PDB:2C0L}.
HELIX 529 533 {ECO:0000244|PDB:2C0L}.
HELIX 534 538 {ECO:0000244|PDB:2C0L}.
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


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