P22307 (NLTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Non-specific lipid-transfer protein
Short name=NSL-TP
EC=2.3.1.176

Alternative name(s):
Propanoyl-CoA C-acyltransferase
SCP-chi
SCPX
Sterol carrier protein 2
Short name=SCP-2
Sterol carrier protein X
Short name=SCP-X

Gene names

Name:

SCP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis. Ref.12 Ref.16
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 structure	Interacts with PEX5.
Subcellular location	Cytoplasm. Mitochondrion. Note: Cytoplasmic in the liver and also associated with mitochondria especially in steroidogenic tissues. Ref.16 Isoform SCPx: Peroxisome. Note: Interaction with PEX5 is essential for peroxisomal import. Ref.16 Isoform SCP2: Mitochondrion Probable Ref.16.
Tissue specificity	Liver, fibroblasts, and placenta.
Induction	Up-regulated by 4-hydroxy-tamoxifen. Ref.10
Involvement in disease	Leukoencephalopathy, with dystonia and motor neuropathy (LDMN) [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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11
Sequence similarities	In the N-terminal section; belongs to the thiolase family. Contains 1 SCP2 domain.
Sequence caution	The sequence AAA03558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Cytoplasm Mitochondrion Peroxisome
Coding sequence diversity	Alternative initiation Alternative promoter usage Alternative splicing Polymorphism
Ligand	Lipid-binding
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	alpha-linolenic acid metabolic process Traceable author statement. Source: Reactome bile acid biosynthetic process Traceable author statement. Source: Reactome fatty acid beta-oxidation using acyl-CoA oxidase Traceable author statement. Source: Reactome inositol trisphosphate biosynthetic process Inferred from direct assay PubMed 12641450. Source: UniProtKB lipid hydroperoxide transport Inferred from direct assay PubMed 15449949. Source: UniProtKB lipid transport Inferred from electronic annotation. Source: UniProtKB-KW peroxisome organization Inferred from electronic annotation. Source: Compara positive regulation of intracellular cholesterol transport Inferred from direct assay PubMed 15449949. Source: UniProtKB positive regulation of steroid metabolic process Inferred from direct assay Ref.3. Source: UniProtKB progesterone biosynthetic process Inferred from direct assay Ref.3. Source: UniProtKB protein localization to plasma membrane Inferred from direct assay PubMed 12641450. Source: UniProtKB
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA peroxisomal matrix Traceable author statement. Source: Reactome protein complex Inferred from direct assay PubMed 19584060. Source: UniProtKB
Molecular_function	cholesterol binding Inferred from direct assay PubMed 18465878. Source: UniProtKB long-chain fatty acyl-CoA binding Inferred from direct assay PubMed 17418802. Source: UniProtKB oleic acid binding Inferred from direct assay PubMed 18465878. Source: UniProtKB phosphatidylinositol transporter activity Inferred from direct assay PubMed 12641450. Source: UniProtKB propanoyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAV1	Q03135	3	EBI-1050999,EBI-603614
Cav1	P49817	3	EBI-1050999,EBI-1161338	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform SCPx (identifier: P22307-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform SCP2 (identifier: P22307-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-404: Missing.

Note: Contains a mitochondrial transit peptide at positions 1-20 (Potential).

Isoform 3 (identifier: P22307-3)

The sequence of this isoform differs from the canonical sequence as follows:
     67-110: Missing.
     362-547: LAQCAELCWQ...LQLQPGNAKL → GHSCS

Isoform 4 (identifier: P22307-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Note: Produced by alternative splicing. No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 547

547

Non-specific lipid-transfer protein

PRO_0000034091

Regions

Domain

433 – 543

111

SCP2

Motif

545 – 547

3

Microbody targeting signal Potential

Amino acid modifications

Modified residue

142

1

N6-acetyllysine By similarity

Modified residue

173

1

N6-acetyllysine By similarity

Modified residue

183

1

N6-acetyllysine Ref.13

Modified residue

282

1

N6-acetyllysine By similarity

Modified residue

341

1

N6-acetyllysine By similarity

Modified residue

425

1

Phosphoserine By similarity

Modified residue

438

1

N6-acetyllysine Ref.13

Modified residue

453

1

N6-acetyllysine By similarity

Modified residue

470

1

N6-acetyllysine Ref.13

Natural variations

Alternative sequence

1 – 404

404

Missing in isoform SCP2.

VSP_018977

Alternative sequence

1 – 81

81

Missing in isoform 4.

VSP_045187

Alternative sequence

67 – 110

44

Missing in isoform 3.

VSP_042686

Alternative sequence

362 – 547

186

LAQCA…GNAKL → GHSCS in isoform 3.

VSP_042687

Natural variant

155

1

A → D in a breast cancer sample; somatic mutation. Ref.17

VAR_035706

Experimental info

Mutagenesis

528

1

N → D: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-530. Ref.12

Mutagenesis

528

1

N → I: Strongly reduces sterol carrier and phosphatidylcholine transfer activity. Ref.12

Mutagenesis

530

1

G → D: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-528. Ref.12

Sequence conflict

10

1

T → A in AAB41286. Ref.1

Sequence conflict

393

1

G → D in AAB41286. Ref.1

Sequence conflict

472

1

A → D in AAB24921. Ref.4

Sequence conflict

482

1

K → Q in AAB24921. Ref.4

Sequence conflict

501

1

D → A in AAB24921. Ref.4

Sequence conflict

522

1

K → P in AAB24921. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

547

Helix Strand Turn

Details...

Turn

427 – 430

4

Helix

432 – 454

23

Beta strand

457 – 465

9

Helix

467 – 469

3

Beta strand

472 – 480

9

Beta strand

484 – 487

4

Beta strand

494 – 500

7

Helix

501 – 508

8

Turn

509 – 511

3

Helix

514 – 519

6

Beta strand

524 – 527

4

Helix

529 – 533

5

Helix

534 – 538

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform SCPx [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 29F7551465C7143A	FASTA	547	58,994
	10 20 30 40 50 60 MSSSPWEPAT LRRVFVVGVG MTKFVKPGAE NSRDYPDLAE EAGKKALADA QIPYSAVDQA 70 80 90 100 110 120 CVGYVFGDST CGQRAIYHSL GMTGIPIINV NNNCATGSTA LFMARQLIQG GVAECVLALG 130 140 150 160 170 180 FEKMSKGSLG IKFSDRTIPT DKHVDLLINK YGLSAHPVAP QMFGYAGKEH MEKYGTKIEH 190 200 210 220 230 240 FAKIGWKNHK HSVNNPYSQF QDEYSLDEVM ASKEVFDFLT ILQCCPTSDG AAAAILASEA 250 260 270 280 290 300 FVQKYGLQSK AVEILAQEMM TDLPSSFEEK SIIKMVGFDM SKEAARKCYE KSGLTPNDID 310 320 330 340 350 360 VIELHDCFST NELLTYEALG LCPEGQGATL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT 370 380 390 400 410 420 GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGIGGAVVV TLYKMGFPEA ASSFRTHQIE 430 440 450 460 470 480 AVPTSSASDG FKANLVFKEI EKKLEEEGEQ FVKKIGGIFA FKVKDGPGGK EATWVVDVKN 490 500 510 520 530 540 GKGSVLPNSD KKADCTITMA DSDFLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL QPGNAKL
	Isoform SCP2 [UniParc]. Checksum: DE7FD93BB320BB30	FASTA	143	15,401
	10 20 30 40 50 60 MGFPEAASSF RTHQIEAVPT SSASDGFKAN LVFKEIEKKL EEEGEQFVKK IGGIFAFKVK 70 80 90 100 110 120 DGPGGKEATW VVDVKNGKGS VLPNSDKKAD CTITMADSDF LALMTGKMNP QSAFFQGKLK 130 140 ITGNMGLAMK LQNLQLQPGN AKL
	Isoform 3 [UniParc]. Checksum: FC4864F7E46C77F7	FASTA	322	34,975
	10 20 30 40 50 60 MSSSPWEPAT LRRVFVVGVG MTKFVKPGAE NSRDYPDLAE EAGKKALADA QIPYSAVDQA 70 80 90 100 110 120 CVGYVFGVAE CVLALGFEKM SKGSLGIKFS DRTIPTDKHV DLLINKYGLS AHPVAPQMFG 130 140 150 160 170 180 YAGKEHMEKY GTKIEHFAKI GWKNHKHSVN NPYSQFQDEY SLDEVMASKE VFDFLTILQC 190 200 210 220 230 240 CPTSDGAAAA ILASEAFVQK YGLQSKAVEI LAQEMMTDLP SSFEEKSIIK MVGFDMSKEA 250 260 270 280 290 300 ARKCYEKSGL TPNDIDVIEL HDCFSTNELL TYEALGLCPE GQGATLVDRG DNTYGGKWVI 310 320 NPSGGLISKG HPLGATGGHS CS
	Isoform 4 [UniParc]. Checksum: 47E3BAB70472FF31	FASTA	466	50,342
	10 20 30 40 50 60 MTGIPIINVN NNCATGSTAL FMARQLIQGG VAECVLALGF EKMSKGSLGI KFSDRTIPTD 70 80 90 100 110 120 KHVDLLINKY GLSAHPVAPQ MFGYAGKEHM EKYGTKIEHF AKIGWKNHKH SVNNPYSQFQ 130 140 150 160 170 180 DEYSLDEVMA SKEVFDFLTI LQCCPTSDGA AAAILASEAF VQKYGLQSKA VEILAQEMMT 190 200 210 220 230 240 DLPSSFEEKS IIKMVGFDMS KEAARKCYEK SGLTPNDIDV IELHDCFSTN ELLTYEALGL 250 260 270 280 290 300 CPEGQGATLV DRGDNTYGGK WVINPSGGLI SKGHPLGATG LAQCAELCWQ LRGEAGKRQV 310 320 330 340 350 360 PGAKVALQHN LGIGGAVVVT LYKMGFPEAA SSFRTHQIEA VPTSSASDGF KANLVFKEIE 370 380 390 400 410 420 KKLEEEGEQF VKKIGGIFAF KVKDGPGGKE ATWVVDVKNG KGSVLPNSDK KADCTITMAD 430 440 450 460 SDFLALMTGK MNPQSAFFQG KLKITGNMGL AMKLQNLQLQ PGNAKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The structure of the human sterol carrier protein X/sterol carrier protein 2 gene (SCP2)." Ohba T., Rennert H., Pfeifer S.M., He Z., Yamamoto R., Holt J.A., Billheimer J.T., Strauss J.F. III Genomics 24:370-374(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SCPX). Tissue: Liver.
[2]	"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." He Z., Yamamoto R., Furth E.E., Schantz L.J., Naylor S.L., George H., Billheimer J.T., Strauss J.F. III DNA Cell Biol. 10:559-569(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCPX). Tissue: Liver.
[3]	"Cloning and expression of a cDNA encoding human sterol carrier protein 2." Yamamoto R., Kallen C.B., Babalola G.O., Rennert H., Billheimer J.T., Strauss J.F. III Proc. Natl. Acad. Sci. U.S.A. 88:463-467(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCP2). Tissue: Liver.
[4]	"Localization of human sterol carrier protein 2 gene and cDNA expression in COS-7 cell." Yamamoto R. Hokkaido Igaku Zasshi 67:839-848(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCP2). Tissue: Liver.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Caudate nucleus.
[6]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND SCP2). Tissue: Brain.
[9]	Bienvenut W.V. Submitted (MAR-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 455-462; 512-522 AND 535-546, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[10]	"Regulation of sterol carrier protein gene expression by the forkhead transcription factor FOXO3a." Dansen T.B., Kops G.J., Denis S., Jelluma N., Wanders R.J., Bos J.L., Burgering B.M., Wirtz K.W. J. Lipid Res. 45:81-88(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE PROMOTER USAGE, INDUCTION BY 4-HYDROXY-TAMOXIFEN.
[11]	"Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) cause leukencephalopathy with dystonia and motor neuropathy." Ferdinandusse S., Kostopoulos P., Denis S., Rusch H., Overmars H., Dillmann U., Reith W., Haas D., Wanders R.J., Duran M., Marziniak M. Am. J. Hum. Genet. 78:1046-1052(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN LDMN.
[12]	"Structure-activity studies of human sterol carrier protein 2." Seedorf U., Scheek S., Engel T., Steif C., Hinz H.-J., Assmann G. J. Biol. Chem. 269:2613-2618(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASN-528 AND GLY-530, FUNCTION.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-183; LYS-438 AND LYS-470, MASS SPECTROMETRY.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2." Szyperski T., Scheek S., Johansson J., Assmann G., Seedorf U., Wuethrich K. FEBS Lett. 335:18-26(1993) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF SCP2.
[16]	"Recognition of a functional peroxisome type 1 target by the dynamic import receptor Pex5p." Stanley W.A., Filipp F.V., Kursula P., Schueller N., Erdmann R., Schliebs W., Sattler M., Wilmanns M. Mol. Cell 24:653-663(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 426-547 IN COMPLEX WITH PEX5, FUNCTION, SUBCELLULAR LOCATION.
[17]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-155.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U11313 , U11297, U11299, U11300, U11301, U11302, U11303, U11304, U11305, U11306, U11307, U11308, U11309, U11310, U11311, U11312 Genomic DNA. Translation: AAB41286.1.
M75883 mRNA. Translation: AAA03557.1.
M75884 mRNA. Translation: AAA03558.1. Different initiation.
M55421 mRNA. Translation: AAA03559.1.
S52450 mRNA. Translation: AAB24921.1.
AK295214 mRNA. Translation: BAG58208.1.
AL445183, AC099677 Genomic DNA. Translation: CAH72590.1.
CH471059 Genomic DNA. Translation: EAX06760.1.
CH471059 Genomic DNA. Translation: EAX06761.1.
BC005911 mRNA. Translation: AAH05911.1.
BC067108 mRNA. Translation: AAH67108.1.

IPI

IPI00026105.
IPI00433347.
IPI00943320.
IPI00977865.

PIR

B40407.
I38205.

RefSeq

NP_001007099.1. NM_001007098.2.
NP_001007100.1. NM_001007099.2.
NP_001007101.1. NM_001007100.2.
NP_001007251.1. NM_001007250.2.
NP_001180546.1. NM_001193617.1.
NP_002970.2. NM_002979.4.

UniGene

Hs.476365.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QND	NMR	-	A	425-547	[»]
2C0L	X-ray	2.30	B	426-547	[»]

ProteinModelPortal

P22307.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22307. 6 interactions.

STRING

9606.ENSP00000360569.

PTM databases

PhosphoSite

P22307.

Polymorphism databases

DMDM

2507456.

2D gel databases

REPRODUCTION-2DPAGE

IPI00026105.

Proteomic databases

PaxDb

P22307.

PRIDE

P22307.

Protocols and materials databases

DNASU

6342.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371513; ENSP00000360568; ENSG00000116171.
ENST00000371514; ENSP00000360569; ENSG00000116171.
ENST00000435345; ENSP00000396413; ENSG00000116171.
ENST00000528311; ENSP00000434132; ENSG00000116171.

GeneID

6342.

KEGG

hsa:6342.

UCSC

uc001cur.2. human.
uc001cus.2. human.

Organism-specific databases

CTD

6342.

GeneCards

GC01P053392.

HGNC

HGNC:10606. SCP2.

HPA

HPA027101.
HPA027135.
HPA027317.

MIM

184755. gene.
613724. phenotype.

neXtProt

NX_P22307.

Orphanet

163684. Leukoencephalopathy - dystonia - motor neuropathy.

PharmGKB

PA35014.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0183.

HOGENOM

HOG000221741.

HOVERGEN

HBG006506.

InParanoid

P22307.

KO

K08764.

OMA

GNAGREH.

OrthoDB

EOG40K7ZM.

PhylomeDB

P22307.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P22307.

Bgee

P22307.

CleanEx

HS_SCP2.

Genevestigator

P22307.

GermOnline

ENSG00000116171. Homo sapiens.

Family and domain databases

Gene3D

3.40.47.10. 4 hits.

InterPro

IPR003033. SCP2_sterol-bd_dom.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]

Pfam

PF02036. SCP2. 1 hit.
PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]

SUPFAM

SSF55718. SCP2. 1 hit.
SSF53901. Thiolase-like. 2 hits.

PROSITE

PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5950.

ChiTaRS

SCP2. human.

EvolutionaryTrace

P22307.

GenomeRNAi

6342.

NextBio

24628.

SOURCE

Search...

Entry information

Entry name

NLTP_HUMAN

Accession

Primary (citable) accession number: P22307
Secondary accession number(s): B4DHP6 , D3DQ37, Q15432, Q16622, Q5VVZ1, Q6NXF4, Q99430

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 154 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.