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Protein

Non-specific lipid-transfer protein

Gene

SCP2

Organism
Homo sapiens (Human)
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.2 Publications

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

  • cholesterol binding Source: UniProtKB
  • fatty-acyl-CoA binding Source: UniProtKB
  • long-chain fatty acyl-CoA binding Source: UniProtKB
  • oleic acid binding Source: UniProtKB
  • phosphatidylinositol transporter activity Source: UniProtKB
  • propanoyl-CoA C-acyltransferase activity Source: UniProtKB-EC
  • receptor binding Source: UniProtKB

GO - Biological processi

  • alpha-linolenic acid metabolic process Source: Reactome
  • bile acid biosynthetic process Source: Reactome
  • bile acid metabolic process Source: Reactome
  • cellular lipid metabolic process Source: Reactome
  • fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
  • inositol trisphosphate biosynthetic process Source: UniProtKB
  • lipid hydroperoxide transport Source: UniProtKB
  • lipid transport Source: UniProtKB-KW
  • peroxisome organization Source: Ensembl
  • phospholipid transport Source: UniProtKB
  • positive regulation of intracellular cholesterol transport Source: UniProtKB
  • positive regulation of steroid metabolic process Source: UniProtKB
  • progesterone biosynthetic process Source: UniProtKB
  • protein localization to plasma membrane Source: UniProtKB
  • small molecule metabolic process Source: Reactome
  • steroid biosynthetic process Source: UniProtKB
  • unsaturated fatty acid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03991-MONOMER.
BRENDAi2.3.1.176. 2681.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17017. Beta-oxidation of pristanoyl-CoA.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10606. SCP2.

Subcellular locationi

Isoform SCPx :
  • Peroxisome

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

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • peroxisomal matrix Source: Reactome
  • peroxisome Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

Pathology & Biotechi

Involvement in diseasei

Leukoencephalopathy, with dystonia and motor neuropathy (LDMN)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613724

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi528 – 5281N → D: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-530. 1 Publication
Mutagenesisi528 – 5281N → I: Strongly reduces sterol carrier and phosphatidylcholine transfer activity. 1 Publication
Mutagenesisi530 – 5301G → D: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-528. 1 Publication

Organism-specific databases

MIMi613724. phenotype.
Orphaneti163684. Leukoencephalopathy - dystonia - motor neuropathy.
PharmGKBiPA35014.

Polymorphism and mutation databases

BioMutaiSCP2.
DMDMi2507456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Non-specific lipid-transfer proteinPRO_0000034091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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; alternate1 Publication
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; alternate1 Publication
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; alternate1 Publication
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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP22307.
PaxDbiP22307.
PRIDEiP22307.

2D gel databases

REPRODUCTION-2DPAGEIPI00026105.

PTM databases

PhosphoSiteiP22307.

Expressioni

Tissue specificityi

Liver, fibroblasts, and placenta.

Inductioni

Up-regulated by 4-hydroxy-tamoxifen.1 Publication

Gene expression databases

BgeeiP22307.
CleanExiHS_SCP2.
ExpressionAtlasiP22307. baseline and differential.
GenevisibleiP22307. HS.

Organism-specific databases

HPAiHPA027101.
HPA027135.
HPA027317.

Interactioni

Subunit structurei

Interacts with PEX5.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CAV1Q031353EBI-1050999,EBI-603614
Cav1P498173EBI-1050999,EBI-1161338From a different organism.
TRIP13Q156454EBI-1050999,EBI-358993

Protein-protein interaction databases

BioGridi112246. 36 interactions.
IntActiP22307. 10 interactions.
MINTiMINT-3009685.
STRINGi9606.ENSP00000360569.

Structurei

Secondary structure

1
547
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni427 – 4304Combined sources
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
Turni509 – 5113Combined sources
Helixi514 – 5196Combined sources
Beta strandi524 – 5274Combined sources
Helixi529 – 5335Combined sources
Helixi534 – 5385Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QNDNMR-A425-547[»]
2C0LX-ray2.30B426-547[»]
ProteinModelPortaliP22307.
SMRiP22307. Positions 12-393, 426-547.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22307.

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

eggNOGiCOG0183.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000221741.
HOVERGENiHBG006506.
InParanoidiP22307.
KOiK08764.
OMAiSIIKMVG.
OrthoDBiEOG78H3T0.
PhylomeDBiP22307.
TreeFamiTF300574.

Family and domain databases

Gene3Di3.30.1050.10. 1 hit.
3.40.47.10. 4 hits.
InterProiIPR003033. 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]
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 (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform SCPx (identifier: P22307-1) [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
MSSSPWEPAT LRRVFVVGVG MTKFVKPGAE NSRDYPDLAE EAGKKALADA
60 70 80 90 100
QIPYSAVDQA CVGYVFGDST CGQRAIYHSL GMTGIPIINV NNNCATGSTA
110 120 130 140 150
LFMARQLIQG GVAECVLALG FEKMSKGSLG IKFSDRTIPT DKHVDLLINK
160 170 180 190 200
YGLSAHPVAP QMFGYAGKEH MEKYGTKIEH FAKIGWKNHK HSVNNPYSQF
210 220 230 240 250
QDEYSLDEVM ASKEVFDFLT ILQCCPTSDG AAAAILASEA FVQKYGLQSK
260 270 280 290 300
AVEILAQEMM TDLPSSFEEK SIIKMVGFDM SKEAARKCYE KSGLTPNDID
310 320 330 340 350
VIELHDCFST NELLTYEALG LCPEGQGATL VDRGDNTYGG KWVINPSGGL
360 370 380 390 400
ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGIGGAVVV
410 420 430 440 450
TLYKMGFPEA ASSFRTHQIE AVPTSSASDG FKANLVFKEI EKKLEEEGEQ
460 470 480 490 500
FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPNSD KKADCTITMA
510 520 530 540
DSDFLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL QPGNAKL
Length:547
Mass (Da):58,994
Last modified:November 1, 1997 - v2
Checksum:i29F7551465C7143A
GO
Isoform SCP2 (identifier: P22307-2) [UniParc]FASTAAdd to basket

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.Curated
Show »
Length:143
Mass (Da):15,401
Checksum:iDE7FD93BB320BB30
GO
Isoform 3 (identifier: P22307-3) [UniParc]FASTAAdd to basket

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

Show »
Length:322
Mass (Da):34,975
Checksum:iFC4864F7E46C77F7
GO
Isoform 4 (identifier: P22307-4) [UniParc]FASTAAdd to basket

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

Note: Produced by alternative splicing. No experimental confirmation available.
Show »
Length:466
Mass (Da):50,342
Checksum:i47E3BAB70472FF31
GO
Isoform 5 (identifier: P22307-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-404: Missing.
     447-463: EGEQFVKKIGGIFAFKV → IRRLTAQSQWLTQTSWL
     464-547: Missing.

Show »
Length:59
Mass (Da):6,699
Checksum:i8C1F69316F4AF3A9
GO
Isoform 6 (identifier: P22307-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-404: Missing.
     412-414: Missing.

Show »
Length:140
Mass (Da):15,079
Checksum:iB4FED0091257ACC1
GO
Isoform 7 (identifier: P22307-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-110: Missing.

Note: Produced by alternative splicing.
Show »
Length:503
Mass (Da):54,415
Checksum:i26B3C3FC9F326D3E
GO
Isoform 8 (identifier: P22307-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-66: Missing.

Note: Produced by alternative splicing.
Show »
Length:523
Mass (Da):56,497
Checksum:iCC516256338B09FA
GO

Sequence cautioni

The sequence AAA03558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101T → A in AAB41286 (PubMed:7698762).Curated
Sequence conflicti56 – 561A → V in AK308105 (PubMed:14702039).Curated
Sequence conflicti116 – 1161V → A in AK308105 (PubMed:14702039).Curated
Sequence conflicti341 – 3411K → Q in BAG57810 (PubMed:14702039).Curated
Sequence conflicti393 – 3931G → D in AAB41286 (PubMed:7698762).Curated
Sequence conflicti472 – 4721A → D in AAB24921 (PubMed:1483685).Curated
Sequence conflicti482 – 4821K → Q in AAB24921 (PubMed:1483685).Curated
Sequence conflicti501 – 5011D → A in AAB24921 (PubMed:1483685).Curated
Sequence conflicti522 – 5221K → P in AAB24921 (PubMed:1483685).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551A → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_035706

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 404404Missing in isoform SCP2, isoform 5 and isoform 6. 5 PublicationsVSP_018977Add
BLAST
Alternative sequencei1 – 8181Missing in isoform 4. 1 PublicationVSP_045187Add
BLAST
Alternative sequencei43 – 6624Missing in isoform 8. 1 PublicationVSP_047267Add
BLAST
Alternative sequencei67 – 11044Missing in isoform 3 and isoform 7. 2 PublicationsVSP_042686Add
BLAST
Alternative sequencei362 – 547186LAQCA…GNAKL → GHSCS in isoform 3. 1 PublicationVSP_042687Add
BLAST
Alternative sequencei412 – 4143Missing in isoform 6. 1 PublicationVSP_047268
Alternative sequencei447 – 46317EGEQF…FAFKV → IRRLTAQSQWLTQTSWL in isoform 5. 1 PublicationVSP_047269Add
BLAST
Alternative sequencei464 – 54784Missing in isoform 5. 1 PublicationVSP_047270Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK294631 mRNA. Translation: BAG57810.1.
AK295214 mRNA. Translation: BAG58208.1.
AK308105 mRNA. No translation available.
CR995014 mRNA. No translation available.
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.
CB997588 mRNA. No translation available.
CCDSiCCDS30719.1. [P22307-5]
CCDS41338.1. [P22307-3]
CCDS44149.1. [P22307-2]
CCDS44150.1. [P22307-6]
CCDS53317.1. [P22307-7]
CCDS53318.1. [P22307-8]
CCDS53319.1. [P22307-4]
CCDS572.1. [P22307-1]
PIRiB40407.
I38205.
RefSeqiNP_001007099.1. NM_001007098.2. [P22307-3]
NP_001007100.1. NM_001007099.2. [P22307-2]
NP_001007101.1. NM_001007100.2. [P22307-6]
NP_001007251.1. NM_001007250.2. [P22307-5]
NP_001180528.1. NM_001193599.1. [P22307-8]
NP_001180546.1. NM_001193617.1. [P22307-4]
NP_002970.2. NM_002979.4. [P22307-1]
UniGeneiHs.476365.

Genome annotation databases

EnsembliENST00000371509; ENSP00000360564; ENSG00000116171. [P22307-7]
ENST00000371513; ENSP00000360568; ENSG00000116171. [P22307-3]
ENST00000371514; ENSP00000360569; ENSG00000116171. [P22307-1]
ENST00000407246; ENSP00000384569; ENSG00000116171. [P22307-8]
ENST00000408941; ENSP00000386214; ENSG00000116171. [P22307-5]
ENST00000430330; ENSP00000406636; ENSG00000116171. [P22307-6]
ENST00000435345; ENSP00000396413; ENSG00000116171. [P22307-2]
ENST00000488965; ENSP00000435783; ENSG00000116171. [P22307-5]
ENST00000528311; ENSP00000434132; ENSG00000116171. [P22307-4]
GeneIDi6342.
KEGGihsa:6342.
UCSCiuc001cuq.2. human. [P22307-3]
uc001cur.2. human. [P22307-1]
uc001cus.2. human. [P22307-2]
uc001cuu.2. human.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK294631 mRNA. Translation: BAG57810.1.
AK295214 mRNA. Translation: BAG58208.1.
AK308105 mRNA. No translation available.
CR995014 mRNA. No translation available.
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.
CB997588 mRNA. No translation available.
CCDSiCCDS30719.1. [P22307-5]
CCDS41338.1. [P22307-3]
CCDS44149.1. [P22307-2]
CCDS44150.1. [P22307-6]
CCDS53317.1. [P22307-7]
CCDS53318.1. [P22307-8]
CCDS53319.1. [P22307-4]
CCDS572.1. [P22307-1]
PIRiB40407.
I38205.
RefSeqiNP_001007099.1. NM_001007098.2. [P22307-3]
NP_001007100.1. NM_001007099.2. [P22307-2]
NP_001007101.1. NM_001007100.2. [P22307-6]
NP_001007251.1. NM_001007250.2. [P22307-5]
NP_001180528.1. NM_001193599.1. [P22307-8]
NP_001180546.1. NM_001193617.1. [P22307-4]
NP_002970.2. NM_002979.4. [P22307-1]
UniGeneiHs.476365.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QNDNMR-A425-547[»]
2C0LX-ray2.30B426-547[»]
ProteinModelPortaliP22307.
SMRiP22307. Positions 12-393, 426-547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112246. 36 interactions.
IntActiP22307. 10 interactions.
MINTiMINT-3009685.
STRINGi9606.ENSP00000360569.

Chemistry

BindingDBiP22307.
ChEMBLiCHEMBL5950.

PTM databases

PhosphoSiteiP22307.

Polymorphism and mutation databases

BioMutaiSCP2.
DMDMi2507456.

2D gel databases

REPRODUCTION-2DPAGEIPI00026105.

Proteomic databases

MaxQBiP22307.
PaxDbiP22307.
PRIDEiP22307.

Protocols and materials databases

DNASUi6342.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371509; ENSP00000360564; ENSG00000116171. [P22307-7]
ENST00000371513; ENSP00000360568; ENSG00000116171. [P22307-3]
ENST00000371514; ENSP00000360569; ENSG00000116171. [P22307-1]
ENST00000407246; ENSP00000384569; ENSG00000116171. [P22307-8]
ENST00000408941; ENSP00000386214; ENSG00000116171. [P22307-5]
ENST00000430330; ENSP00000406636; ENSG00000116171. [P22307-6]
ENST00000435345; ENSP00000396413; ENSG00000116171. [P22307-2]
ENST00000488965; ENSP00000435783; ENSG00000116171. [P22307-5]
ENST00000528311; ENSP00000434132; ENSG00000116171. [P22307-4]
GeneIDi6342.
KEGGihsa:6342.
UCSCiuc001cuq.2. human. [P22307-3]
uc001cur.2. human. [P22307-1]
uc001cus.2. human. [P22307-2]
uc001cuu.2. human.

Organism-specific databases

CTDi6342.
GeneCardsiGC01P053392.
HGNCiHGNC:10606. SCP2.
HPAiHPA027101.
HPA027135.
HPA027317.
MIMi184755. gene.
613724. phenotype.
neXtProtiNX_P22307.
Orphaneti163684. Leukoencephalopathy - dystonia - motor neuropathy.
PharmGKBiPA35014.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000221741.
HOVERGENiHBG006506.
InParanoidiP22307.
KOiK08764.
OMAiSIIKMVG.
OrthoDBiEOG78H3T0.
PhylomeDBiP22307.
TreeFamiTF300574.

Enzyme and pathway databases

BioCyciMetaCyc:HS03991-MONOMER.
BRENDAi2.3.1.176. 2681.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17017. Beta-oxidation of pristanoyl-CoA.

Miscellaneous databases

ChiTaRSiSCP2. human.
EvolutionaryTraceiP22307.
GeneWikiiSCP2.
GenomeRNAii6342.
NextBioi24628.
PROiP22307.
SOURCEiSearch...

Gene expression databases

BgeeiP22307.
CleanExiHS_SCP2.
ExpressionAtlasiP22307. baseline and differential.
GenevisibleiP22307. HS.

Family and domain databases

Gene3Di3.30.1050.10. 1 hit.
3.40.47.10. 4 hits.
InterProiIPR003033. 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]
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. "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. 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] (ISOFORMS 4 AND 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-218 (ISOFORM 7).
    Tissue: Brain, Caudate nucleus and Tongue.
  6. Heil O., Ebert L., Hennig S., Henze S., Radelof U., Schneider D., Korn B.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
  7. "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].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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.
  10. The MGC Project Team
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
  11. Bienvenut W.V.
    Submitted (MAR-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 455-462; 512-522 AND 535-546, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  12. "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.
  13. "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.
  14. "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.
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "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.
  19. "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.
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-155.

Entry informationi

Entry nameiNLTP_HUMAN
AccessioniPrimary (citable) accession number: P22307
Secondary accession number(s): A6NM69
, B4DGJ9, B4DHP6, C9JC79, D3DQ37, E1B6W5, F2Z3J1, Q15432, Q16622, Q5VVZ1, Q6NXF4, Q99430
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.