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P22307

- NLTP_HUMAN

UniProt

P22307 - NLTP_HUMAN

Protein

Non-specific lipid-transfer protein

Gene

SCP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    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

    1. cholesterol binding Source: UniProtKB
    2. fatty-acyl-CoA binding Source: UniProtKB
    3. long-chain fatty acyl-CoA binding Source: UniProtKB
    4. oleic acid binding Source: UniProtKB
    5. phosphatidylinositol transporter activity Source: UniProtKB
    6. propanoyl-CoA C-acyltransferase activity Source: UniProtKB-EC
    7. protein binding Source: UniProtKB
    8. receptor binding Source: UniProtKB

    GO - Biological processi

    1. alpha-linolenic acid metabolic process Source: Reactome
    2. bile acid biosynthetic process Source: Reactome
    3. bile acid metabolic process Source: Reactome
    4. cellular lipid metabolic process Source: Reactome
    5. fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
    6. inositol trisphosphate biosynthetic process Source: UniProtKB
    7. lipid hydroperoxide transport Source: UniProtKB
    8. lipid transport Source: UniProtKB-KW
    9. peroxisome organization Source: Ensembl
    10. phospholipid transport Source: UniProtKB
    11. positive regulation of intracellular cholesterol transport Source: UniProtKB
    12. positive regulation of steroid metabolic process Source: UniProtKB
    13. progesterone biosynthetic process Source: UniProtKB
    14. protein localization to plasma membrane Source: UniProtKB
    15. small molecule metabolic process Source: Reactome
    16. steroid biosynthetic process Source: UniProtKB
    17. unsaturated fatty acid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03991-MONOMER.
    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10606. SCP2.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion 1 Publication
    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.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. intracellular membrane-bounded organelle Source: HPA
    4. membrane Source: UniProtKB
    5. mitochondrion Source: UniProtKB-SubCell
    6. nucleus Source: HPA
    7. peroxisomal matrix Source: Reactome
    8. peroxisome Source: UniProtKB
    9. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    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.

    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

    ArrayExpressiP22307.
    BgeeiP22307.
    CleanExiHS_SCP2.
    GenevestigatoriP22307.

    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.

    Protein-protein interaction databases

    BioGridi112246. 29 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 – 4304
    Helixi432 – 45423
    Beta strandi457 – 4659
    Helixi467 – 4693
    Beta strandi472 – 4809
    Beta strandi484 – 4874
    Beta strandi494 – 5007
    Helixi501 – 5088
    Turni509 – 5113
    Helixi514 – 5196
    Beta strandi524 – 5274
    Helixi529 – 5335
    Helixi534 – 5385

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000221741.
    HOVERGENiHBG006506.
    InParanoidiP22307.
    KOiK08764.
    OMAiPQMFGNA.
    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. Align

    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

    MSSSPWEPAT LRRVFVVGVG MTKFVKPGAE NSRDYPDLAE EAGKKALADA    50
    QIPYSAVDQA CVGYVFGDST CGQRAIYHSL GMTGIPIINV NNNCATGSTA 100
    LFMARQLIQG GVAECVLALG FEKMSKGSLG IKFSDRTIPT DKHVDLLINK 150
    YGLSAHPVAP QMFGYAGKEH MEKYGTKIEH FAKIGWKNHK HSVNNPYSQF 200
    QDEYSLDEVM ASKEVFDFLT ILQCCPTSDG AAAAILASEA FVQKYGLQSK 250
    AVEILAQEMM TDLPSSFEEK SIIKMVGFDM SKEAARKCYE KSGLTPNDID 300
    VIELHDCFST NELLTYEALG LCPEGQGATL VDRGDNTYGG KWVINPSGGL 350
    ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGIGGAVVV 400
    TLYKMGFPEA ASSFRTHQIE AVPTSSASDG FKANLVFKEI EKKLEEEGEQ 450
    FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPNSD KKADCTITMA 500
    DSDFLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL QPGNAKL 547
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi2507456.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS30719.1. [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 ]
    PIRi B40407.
    I38205.
    RefSeqi NP_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 ]
    UniGenei Hs.476365.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QND NMR - A 425-547 [» ]
    2C0L X-ray 2.30 B 426-547 [» ]
    ProteinModelPortali P22307.
    SMRi P22307. Positions 12-393, 426-547.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112246. 29 interactions.
    IntActi P22307. 10 interactions.
    MINTi MINT-3009685.
    STRINGi 9606.ENSP00000360569.

    Chemistry

    ChEMBLi CHEMBL5950.

    PTM databases

    PhosphoSitei P22307.

    Polymorphism databases

    DMDMi 2507456.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00026105.

    Proteomic databases

    MaxQBi P22307.
    PaxDbi P22307.
    PRIDEi P22307.

    Protocols and materials databases

    DNASUi 6342.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371509 ; 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 ]
    GeneIDi 6342.
    KEGGi hsa:6342.
    UCSCi uc001cuq.2. human. [P22307-3 ]
    uc001cur.2. human. [P22307-1 ]
    uc001cus.2. human. [P22307-2 ]

    Organism-specific databases

    CTDi 6342.
    GeneCardsi GC01P053392.
    HGNCi HGNC:10606. SCP2.
    HPAi HPA027101.
    HPA027135.
    HPA027317.
    MIMi 184755. gene.
    613724. phenotype.
    neXtProti NX_P22307.
    Orphaneti 163684. Leukoencephalopathy - dystonia - motor neuropathy.
    PharmGKBi PA35014.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0183.
    HOGENOMi HOG000221741.
    HOVERGENi HBG006506.
    InParanoidi P22307.
    KOi K08764.
    OMAi PQMFGNA.
    OrthoDBi EOG78H3T0.
    PhylomeDBi P22307.
    TreeFami TF300574.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03991-MONOMER.
    Reactomei REACT_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

    ChiTaRSi SCP2. human.
    EvolutionaryTracei P22307.
    GeneWikii SCP2.
    GenomeRNAii 6342.
    NextBioi 24628.
    PROi P22307.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22307.
    Bgeei P22307.
    CleanExi HS_SCP2.
    Genevestigatori P22307.

    Family and domain databases

    Gene3Di 3.30.1050.10. 1 hit.
    3.40.47.10. 4 hits.
    InterProi 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 ]
    Pfami PF02036. SCP2. 1 hit.
    PF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53901. SSF53901. 2 hits.
    SSF55718. SSF55718. 1 hit.
    PROSITEi PS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    18. "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.
    19. 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: October 1, 2014
    This is version 170 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