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Protein

Non-specific lipid-transfer protein

Gene

SCP2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity1 Publication

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity
  • Mitochondrion By similarity

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

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

GO - Cellular componenti

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_0000034095Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31PhosphoserineBy similarity
Modified residuei7 – 71N6-acetyllysineBy similarity
Modified residuei40 – 401N6-succinyllysineBy similarity
Modified residuei132 – 1321N6-acetyllysine; alternateBy similarity
Modified residuei132 – 1321N6-succinyllysine; alternateBy similarity
Modified residuei168 – 1681N6-succinyllysineBy similarity
Modified residuei173 – 1731N6-acetyllysineBy similarity
Modified residuei177 – 1771N6-acetyllysineBy similarity
Modified residuei183 – 1831N6-acetyllysine; alternateBy similarity
Modified residuei183 – 1831N6-succinyllysine; alternateBy 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 residuei544 – 5441N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiO62742.

Interactioni

Subunit structurei

Interacts with PEX5.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000019823.

Structurei

Secondary structure

1
547
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi432 – 45423Combined sources
Beta strandi457 – 4659Combined sources
Helixi467 – 4693Combined sources
Beta strandi472 – 4809Combined sources
Beta strandi484 – 4874Combined sources
Beta strandi494 – 5007Combined sources
Helixi501 – 5088Combined sources
Helixi514 – 5196Combined sources
Beta strandi524 – 5274Combined sources
Helixi529 – 5368Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C44X-ray1.80A425-547[»]
ProteinModelPortaliO62742.
SMRiO62742. Positions 425-547.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO62742.

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.
InParanoidiO62742.
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: O62742-1) [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
MSSSARKLAP LPRVFVVGVG MTKFVKPGTE DARDYPDMAK EAGQKALADA
60 70 80 90 100
QIPYSAVEQA CIGYVYGDST CGQRAVYHSL GLTGIPIINV NNNCSTGSTA
110 120 130 140 150
LFMGRQLIQG GMAECVLALG FEKMERGSLG AKFPDRTNPM DKHLDVLINK
160 170 180 190 200
YGLSAHPVAP QMFGSAGKEH MEKYGTKIEH FAKIGWKNHK HSVNNPYSQF
210 220 230 240 250
QKEYSLDEVM SSRPIFDFLT VLQCCPTSDG AAAAILASEE FVKKYGLQSK
260 270 280 290 300
AVEILAQEMV TDFPSSFEEK SIIKMVGFDM SKEAARRCYE KSGLRPSDID
310 320 330 340 350
VIELHDCFSA NELLTYEALG LCPEGKGGAL VDRGDNTYGG KWVINPSGGL
360 370 380 390 400
ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGLGGAAVV
410 420 430 440 450
TLYKMGFPEA ASSFRTHQIE AAPTSSAGDG FKANLVFKEI EKKLEEEGEQ
460 470 480 490 500
FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPNSD KKADCTITIA
510 520 530 540
DSDLLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL QPGKAKL
Length:547
Mass (Da):58,904
Last modified:August 1, 1998 - v1
Checksum:i32BE7F7DCBF9BCD7
GO
Isoform SCP2 (identifier: O62742-2) [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 1-20 (Potential).Curated
Show »
Length:143
Mass (Da):15,305
Checksum:i8970B49A3B9E2928
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 404404Missing in isoform SCP2. 1 PublicationVSP_018896Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051897 mRNA. Translation: AAC15422.1.
RefSeqiNP_001075504.1. NM_001082035.1. [O62742-1]
UniGeneiOcu.2203.

Genome annotation databases

GeneIDi100008683.
KEGGiocu:100008683.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051897 mRNA. Translation: AAC15422.1.
RefSeqiNP_001075504.1. NM_001082035.1. [O62742-1]
UniGeneiOcu.2203.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C44X-ray1.80A425-547[»]
ProteinModelPortaliO62742.
SMRiO62742. Positions 425-547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000019823.

Proteomic databases

PRIDEiO62742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008683.
KEGGiocu:100008683.

Organism-specific databases

CTDi6342.

Phylogenomic databases

eggNOGiKOG1406. Eukaryota.
KOG4170. Eukaryota.
ENOG410XPRW. LUCA.
HOGENOMiHOG000221741.
HOVERGENiHBG006506.
InParanoidiO62742.
KOiK08764.

Miscellaneous databases

EvolutionaryTraceiO62742.

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

  1. "In pre-sterol carrier protein 2 (SCP2) in solution the leader peptide 1-20 is flexibly disordered, and residues 21-143 adopt the same globular fold as in mature SCP2."
    Weber F.E., Dyer J.H., Lopez Garcia F., Werder M., Szyperski T., Wuethrich K., Hauser H.
    Cell. Mol. Life Sci. 54:751-759(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SCPX AND SCP2), FUNCTION, STRUCTURE BY NMR OF 405-547.
    Tissue: Intestinal epithelium.
  2. "Crystallization and initial X-ray analysis of rabbit mature sterol carrier protein 2."
    Choinowski T., Dyer J.H., Maderegger B., Winterhalter K.H., Hauser H., Piontek K.
    Acta Crystallogr. D 55:1478-1480(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  3. "Structure of sterol carrier protein 2 at 1.8 A resolution reveals a hydrophobic tunnel suitable for lipid binding."
    Choinowski T., Hauser H., Piontek K.
    Biochemistry 39:1897-1902(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 425-547, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNLTP_RABIT
AccessioniPrimary (citable) accession number: O62742
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: August 1, 1998
Last modified: December 9, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.