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Protein

Non-specific lipid-transfer protein

Gene

Scp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis.

Catalytic activityi

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.

GO - Molecular functioni

  • acetyl-CoA C-acyltransferase activity Source: RGD
  • cholesterol transporter activity Source: RGD
  • lipid binding Source: UniProtKB-KW
  • phosphatidylcholine transporter activity Source: RGD
  • phosphatidylethanolamine transporter activity Source: RGD
  • propanoyl-CoA C-acyltransferase activity Source: UniProtKB-EC
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • cellular response to cholesterol Source: RGD
  • cholesterol transport Source: GOC
  • phospholipid transport Source: GOC
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of cholesterol biosynthetic process Source: RGD
  • positive regulation of cholesterol import Source: RGD
  • positive regulation of steroid biosynthetic process Source: UniProtKB
  • response to estradiol Source: RGD
  • response to luteinizing hormone Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14332.
SABIO-RKP11915.

Chemistry

SwissLipidsiSLP:000001233. [P11915-1]

Names & Taxonomyi

Protein namesi
Recommended name:
Non-specific lipid-transfer protein (EC:2.3.1.176)
Short name:
NSL-TP
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 namesi
Name:Scp2
Synonyms:Scp-2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3642. Scp2.

Subcellular locationi

  • Cytoplasm
  • Mitochondrion

  • Note: Cytoplasmic in the liver and also associated with mitochondria especially in steroidogenic tissues.
Isoform SCPx :
  • Peroxisome

  • Note: Interaction with PEX5 is essential for peroxisomal import.By similarity
Isoform SCP2 :

GO - Cellular componenti

  • cytosol Source: RGD
  • endoplasmic reticulum Source: RGD
  • extrinsic component of membrane Source: RGD
  • extrinsic component of mitochondrial outer membrane Source: RGD
  • membrane Source: RGD
  • mitochondrion Source: RGD
  • nucleus Source: RGD
  • peroxisomal matrix Source: RGD
  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Non-specific lipid-transfer proteinPRO_0000034097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31PhosphoserineCombined sources
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei40 – 401N6-succinyllysineBy similarity
Modified residuei132 – 1321N6-acetyllysine; alternateBy similarity
Modified residuei132 – 1321N6-succinyllysine; alternateBy similarity
Modified residuei168 – 1681N6-succinyllysineBy similarity
Modified residuei177 – 1771N6-acetyllysineBy similarity
Modified residuei183 – 1831N6-acetyllysine; alternateBy similarity
Modified residuei183 – 1831N6-succinyllysine; alternateBy similarity
Modified residuei211 – 2111N6-succinyllysineBy similarity
Modified residuei282 – 2821N6-succinyllysineBy similarity
Modified residuei341 – 3411N6-acetyllysine; alternateBy similarity
Modified residuei341 – 3411N6-succinyllysine; alternateBy similarity
Modified residuei432 – 4321N6-acetyllysine; alternateBy similarity
Modified residuei432 – 4321N6-succinyllysine; alternateBy similarity
Modified residuei438 – 4381N6-acetyllysine; alternateBy similarity
Modified residuei438 – 4381N6-succinyllysine; alternateBy similarity
Modified residuei443 – 4431N6-acetyllysine; alternateBy similarity
Modified residuei443 – 4431N6-succinyllysine; alternateBy similarity
Modified residuei453 – 4531N6-acetyllysine; alternateBy similarity
Modified residuei453 – 4531N6-succinyllysine; alternateBy similarity
Modified residuei464 – 4641N6-succinyllysineBy similarity
Modified residuei470 – 4701N6-acetyllysine; alternateBy similarity
Modified residuei470 – 4701N6-succinyllysine; alternateBy similarity
Modified residuei479 – 4791N6-succinyllysineBy similarity
Modified residuei491 – 4911N6-acetyllysineBy similarity
Modified residuei492 – 4921N6-succinyllysineBy similarity
Modified residuei511 – 5111N6-succinyllysineBy similarity
Modified residuei516 – 5161PhosphoserineBy similarity
Modified residuei522 – 5221N6-succinyllysineBy similarity
Modified residuei534 – 5341N6-succinyllysineBy similarity
Modified residuei537 – 5371PhosphoserineCombined sources
Modified residuei544 – 5441N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP11915.
PRIDEiP11915.

PTM databases

iPTMnetiP11915.
PhosphoSiteiP11915.

Expressioni

Tissue specificityi

Liver > intestine > brain > lung, colon, stomach, spleen, kidney, heart and ovary.

Interactioni

Subunit structurei

Interacts with PEX5.By similarity

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP11915. 1 interaction.
STRINGi10116.ENSRNOP00000015420.

Structurei

3D structure databases

ProteinModelPortaliP11915.
SMRiP11915. Positions 425-547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini433 – 543111SCP2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi545 – 5473Microbody targeting signalSequence analysis

Sequence similaritiesi

In the N-terminal section; belongs to the thiolase family.Curated
Contains 1 SCP2 domain.Curated

Phylogenomic databases

eggNOGiKOG1406. Eukaryota.
KOG4170. Eukaryota.
ENOG410XPRW. LUCA.
HOGENOMiHOG000221741.
HOVERGENiHBG006506.
InParanoidiP11915.
KOiK08764.

Family and domain databases

Gene3Di3.30.1050.10. 1 hit.
3.40.47.10. 4 hits.
InterProiIPR003033. SCP2_sterol-bd_dom.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02036. SCP2. 1 hit.
PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform SCPx (identifier: P11915-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPSVALNSPR LPRVFVVGVG MTKFMKPGGE NSRDYPDLAK EAGQKALADR
60 70 80 90 100
QIPYSAVEQA CVGYVYGEST CGQRAIYHSL GLTGIPIINV NNNCSTGSTA
110 120 130 140 150
LFMAQQLVQG GLANCVLALG FEKMEKGSLG TKYSDRSNPL EKHIDVLINK
160 170 180 190 200
YGMSACPFAP QLFGSAGKEH METYGTKVEH FAKIGWKNHK HSVNNPYSQF
210 220 230 240 250
QDEYSLDEIM KSRPVFDFLT VLQCCPTSDG AAAAIVSSEE FVQKHGLQSK
260 270 280 290 300
AVEIVAQEMV TDMPSTFEEK SVIKMVGYDM SKEAARKCYE KSGLGPSDVD
310 320 330 340 350
VIELHDCFST NELLTYEALG LCPEGQGGAL VDRGDNTYGG KWVINPSGGL
360 370 380 390 400
ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGLGGAAVV
410 420 430 440 450
TLYRMGFPEA ASSFRTHQIS AAPTSSAGDG FKANLIFKEI EKKLEEEGEE
460 470 480 490 500
FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPDSD KKADCTITMA
510 520 530 540
DSDLLALMTG KMNPQSAFFQ GKLKIAGNMG LAMKLQSLQL QPDKAKL
Length:547
Mass (Da):58,813
Last modified:August 1, 1991 - v3
Checksum:iD0D1B435D2DC6AFB
GO
Isoform SCP2 (identifier: P11915-2) [UniParc]FASTAAdd to basket

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

Note: Mitochondrial precursor. Contains a mitochondrial transit peptide at positions 405-424 (Potential).Curated
Show »
Length:143
Mass (Da):15,298
Checksum:iF80FB9B958462F52
GO

Sequence cautioni

The sequence AAA40623.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA43060.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121P → R in AAA40622 (PubMed:2034675).Curated
Sequence conflicti12 – 121P → R in CAA43061 (PubMed:2034675).Curated
Sequence conflicti12 – 121P → R in AAH81713 (PubMed:15489334).Curated
Sequence conflicti50 – 501R → A in AAA40622 (PubMed:2034675).Curated
Sequence conflicti50 – 501R → A in AAH81713 (PubMed:15489334).Curated
Sequence conflicti265 – 2651S → T in AAA42122 (PubMed:1985920).Curated
Sequence conflicti427 – 4282AG → SV AA sequence (PubMed:3395344).Curated
Sequence conflicti436 – 4361I → V AA sequence (PubMed:3395344).Curated
Sequence conflicti446 – 4461E → D AA sequence (PubMed:3395344).Curated
Sequence conflicti450 – 4501E → Q AA sequence (PubMed:3395344).Curated
Sequence conflicti488 – 4881D → N AA sequence (PubMed:3395344).Curated
Sequence conflicti516 – 5161S → T AA sequence (PubMed:3395344).Curated
Sequence conflicti526 – 5261A → N AA sequence (PubMed:3395344).Curated
Sequence conflicti537 – 5371S → N AA sequence (PubMed:3395344).Curated
Sequence conflicti543 – 5431D → G AA sequence (PubMed:3395344).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 404404Missing in isoform SCP2. CuratedVSP_018897Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62763 mRNA. Translation: AAA40622.1.
M62763 mRNA. Translation: AAA40623.1. Different initiation.
M57454 mRNA. Translation: AAA42121.1.
M57453 mRNA. Translation: AAA42122.1.
M58287 mRNA. Translation: AAA41726.1.
BC081713 mRNA. Translation: AAH81713.1.
M34728 mRNA. Translation: AAA42120.1.
X60654 mRNA. Translation: CAA43060.1. Different initiation.
X60654 mRNA. Translation: CAA43061.1.
PIRiA39368.
RefSeqiNP_612517.2. NM_138508.4.
UniGeneiRn.31887.

Genome annotation databases

GeneIDi25541.
KEGGirno:25541.
UCSCiRGD:3642. rat. [P11915-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62763 mRNA. Translation: AAA40622.1.
M62763 mRNA. Translation: AAA40623.1. Different initiation.
M57454 mRNA. Translation: AAA42121.1.
M57453 mRNA. Translation: AAA42122.1.
M58287 mRNA. Translation: AAA41726.1.
BC081713 mRNA. Translation: AAH81713.1.
M34728 mRNA. Translation: AAA42120.1.
X60654 mRNA. Translation: CAA43060.1. Different initiation.
X60654 mRNA. Translation: CAA43061.1.
PIRiA39368.
RefSeqiNP_612517.2. NM_138508.4.
UniGeneiRn.31887.

3D structure databases

ProteinModelPortaliP11915.
SMRiP11915. Positions 425-547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11915. 1 interaction.
STRINGi10116.ENSRNOP00000015420.

Chemistry

SwissLipidsiSLP:000001233. [P11915-1]

PTM databases

iPTMnetiP11915.
PhosphoSiteiP11915.

Proteomic databases

PaxDbiP11915.
PRIDEiP11915.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25541.
KEGGirno:25541.
UCSCiRGD:3642. rat. [P11915-1]

Organism-specific databases

CTDi6342.
RGDi3642. Scp2.

Phylogenomic databases

eggNOGiKOG1406. Eukaryota.
KOG4170. Eukaryota.
ENOG410XPRW. LUCA.
HOGENOMiHOG000221741.
HOVERGENiHBG006506.
InParanoidiP11915.
KOiK08764.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14332.
SABIO-RKP11915.

Miscellaneous databases

PROiP11915.

Family and domain databases

Gene3Di3.30.1050.10. 1 hit.
3.40.47.10. 4 hits.
InterProiIPR003033. SCP2_sterol-bd_dom.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02036. SCP2. 1 hit.
PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and nucleotide sequence of rat liver sterol carrier protein 2 cDNAs."
    Seedorf U., Assmann G.
    J. Biol. Chem. 266:630-636(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. "Molecular cloning and deduced amino acid sequence of nonspecific lipid transfer protein (sterol carrier protein 2) of rat liver: a higher molecular mass (60 kDa) protein contains the primary sequence of nonspecific lipid transfer protein as its C-terminal part."
    Mori T., Tsukamoto T., Mori H., Tashiro Y., Fujiki Y.
    Proc. Natl. Acad. Sci. U.S.A. 88:4338-4342(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Identification of the cDNA clone which encodes the 58-kDa protein containing the amino acid sequence of rat liver non-specific lipid-transfer protein (sterol-carrier protein 2). Homology with rat peroxisomal and mitochondrial 3-oxoacyl-CoA thiolases."
    Ossendorp B.C., van Heusden G.P.H., de Beer A.L.J., Bos K., Schouten G.L., Wirtz K.W.A.
    Eur. J. Biochem. 201:233-239(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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].
    Tissue: Kidney.
  5. "The amino acid sequence of rat liver non-specific lipid transfer protein (sterol carrier protein 2) is present in a high molecular weight protein: evidence from cDNA analysis."
    Ossendorp B.C., van Heusden G.P.H., Wirtz K.W.A.
    Biochem. Biophys. Res. Commun. 168:631-636(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-547.
    Tissue: Liver.
  6. "Characterization of a cDNA encoding rat sterol carrier protein2."
    Billheimer J.T., Strehl L.L., Davis G.L., Strauss J.F. III, Davis L.G.
    DNA Cell Biol. 9:159-165(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 275-547.
    Strain: CD Charles River.
    Tissue: Liver.
  7. "Primary sequence and structural analysis of sterol carrier protein 2 from rat liver: homology with immunoglobulins."
    Pastuszyn A., Noland B.J., Bazan J.F., Fletterick R.J., Scallen T.J.
    J. Biol. Chem. 262:13219-13227(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 425-547.
    Tissue: Liver.
  8. "A mass spectrometric study of the structure of sterol carrier protein SCP2 from rat liver."
    Morris H.R., Larsen B.S., Billheimer J.T.
    Biochem. Biophys. Res. Commun. 154:476-482(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 425-547.
    Tissue: Liver.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-8 AND SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNLTP_RAT
AccessioniPrimary (citable) accession number: P11915
Secondary accession number(s): Q63383, Q642G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1991
Last modified: June 8, 2016
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.