Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00650
Entry Name
UniProt Accession
Theoretical PI
6.44
Molecular Weight
58993.62
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Non-specific lipid-transfer protein
Protein Synonyms/Alias
NSL-TP; 2.3.1.176; Propanoyl-CoA C-acyltransferase; SCP-chi; SCPX; Sterol carrier protein 2; SCP-2; Sterol carrier protein X; SCP-X;
Gene Name
SCP2
Gene Synonyms/Alias
Created Date
01-AUG-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
224
Canonical
DFLTILQCCPTSDGA
[1]
S-Palmitoylation
225
Canonical
FLTILQCCPTSDGAA
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis.
Sequence Annotation
Domain: 433 543 SCP2.
Motif: 545 547 Microbody targeting signal.
Modified residue: 132 132 N6-acetyllysine; alternate.
Modified residue: 132 132 N6-succinyllysine; alternate.
Modified residue: 168 168 N6-succinyllysine.
Modified residue: 173 173 N6-acetyllysine.
Modified residue: 177 177 N6-acetyllysine.
Modified residue: 183 183 N6-acetyllysine; alternate.
Modified residue: 183 183 N6-succinyllysine; alternate.
Modified residue: 282 282 N6-succinyllysine.
Modified residue: 341 341 N6-acetyllysine; alternate.
Modified residue: 341 341 N6-succinyllysine; alternate.
Modified residue: 432 432 N6-acetyllysine; alternate.
Modified residue: 432 432 N6-succinyllysine; alternate.
Modified residue: 438 438 N6-acetyllysine; alternate.
Modified residue: 438 438 N6-succinyllysine; alternate.
Modified residue: 443 443 N6-acetyllysine; alternate.
Modified residue: 443 443 N6-succinyllysine; alternate.
Modified residue: 453 453 N6-acetyllysine; alternate.
Modified residue: 453 453 N6-succinyllysine; alternate.
Modified residue: 464 464 N6-succinyllysine.
Modified residue: 470 470 N6-acetyllysine; alternate.
Modified residue: 470 470 N6-succinyllysine; alternate.
Modified residue: 479 479 N6-succinyllysine.
Modified residue: 491 491 N6-acetyllysine.
Modified residue: 492 492 N6-succinyllysine.
Modified residue: 511 511 N6-succinyllysine.
Modified residue: 516 516 Phosphoserine.
Modified residue: 522 522 N6-succinyllysine.
Modified residue: 534 534 N6-succinyllysine.
Protein Length
547 AA.
Protein Sequence
(Canonical)
MSSSPWEPAT LRRVFVVGVG MTKFVKPGAE NSRDYPDLAE EAGKKALADA QIPYSAVDQA  60
CVGYVFGDST CGQRAIYHSL GMTGIPIINV NNNCATGSTA LFMARQLIQG GVAECVLALG  120
FEKMSKGSLG IKFSDRTIPT DKHVDLLINK YGLSAHPVAP QMFGYAGKEH MEKYGTKIEH  180
FAKIGWKNHK HSVNNPYSQF QDEYSLDEVM ASKEVFDFLT ILQCCPTSDG AAAAILASEA  240
FVQKYGLQSK AVEILAQEMM TDLPSSFEEK SIIKMVGFDM SKEAARKCYE KSGLTPNDID  300
VIELHDCFST NELLTYEALG LCPEGQGATL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT  360
GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGIGGAVVV TLYKMGFPEA ASSFRTHQIE  420
AVPTSSASDG FKANLVFKEI EKKLEEEGEQ FVKKIGGIFA FKVKDGPGGK EATWVVDVKN  480
GKGSVLPNSD KKADCTITMA DSDFLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL  540
QPGNAKL                                                            547
FASTA
(Canonical)
>LipidDB-9606-00650|P22307
MSSSPWEPATLRRVFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQA
CVGYVFGDSTCGQRAIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALG
FEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHMEKYGTKIEH
FAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEA
FVQKYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDID
VIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGAT
GLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLYKMGFPEAASSFRTHQIE
AVPTSSASDGFKANLVFKEIEKKLEEEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKN
GKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGLAMKLQNLQL
QPGNAKL
Gene Ontology
GO:0005737; C:cytoplasm; IDA:HPA
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005739; C:mitochondrion; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IDA:HPA
GO:0005782; C:peroxisomal matrix; TAS:Reactome
GO:0005777; C:peroxisome; IDA:UniProtKB
GO:0043234; C:protein complex; IDA:UniProtKB
GO:0015485; F:cholesterol binding; IDA:UniProtKB
GO:0000062; F:fatty-acyl-CoA binding; IDA:UniProtKB
GO:0036042; F:long-chain fatty acyl-CoA binding; IDA:UniProtKB
GO:0070538; F:oleic acid binding; IDA:UniProtKB
GO:0008526; F:phosphatidylinositol transporter activity; IDA:UniProtKB
GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC
GO:0005102; F:receptor binding; IPI:UniProtKB
GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome
GO:0006699; P:bile acid biosynthetic process; TAS:Reactome
GO:0008206; P:bile acid metabolic process; TAS:Reactome
GO:0044255; P:cellular lipid metabolic process; TAS:Reactome
GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome
GO:0032959; P:inositol trisphosphate biosynthetic process; IDA:UniProtKB
GO:1901373; P:lipid hydroperoxide transport; IDA:UniProtKB
GO:0006869; P:lipid transport; IEA:UniProtKB-KW
GO:0007031; P:peroxisome organization; IEA:Ensembl
GO:0015914; P:phospholipid transport; IDA:UniProtKB
GO:0032385; P:positive regulation of intracellular cholesterol transport; IDA:UniProtKB
GO:0045940; P:positive regulation of steroid metabolic process; IDA:UniProtKB
GO:0006701; P:progesterone biosynthetic process; IDA:UniProtKB
GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0006694; P:steroid biosynthetic process; IDA:UniProtKB
GO:0033559; P:unsaturated fatty acid metabolic process; TAS:Reactome
Interpro
InterPro; IPR003033; SCP2_sterol-bd_dom
InterPro; IPR016039; Thiolase-like
InterPro; IPR016038; Thiolase-like_subgr
InterPro; IPR020615; Thiolase_acyl_enz_int_AS
InterPro; IPR020617; Thiolase_C
InterPro; IPR020613; Thiolase_CS
InterPro; IPR020616; Thiolase_N
Pfam
Pfam; PF02036; SCP2;
Pfam; PF02803; Thiolase_C;
Pfam; PF00108; Thiolase_N;
SMART
PROSITE
PROSITE; PS00098; THIOLASE_1;
PROSITE; PS00737; THIOLASE_2;
PRINTS