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Protein

Ceramide-1-phosphate transfer protein

Gene

CPTP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mediates the intracellular transfer of ceramide-1-phosphate (C1P) between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1-phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is stimulated by phosphatidylserine in C1P source vesicles (PubMed:28011644). Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis (PubMed:29164996).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei56Phosphoceramide1 Publication1
Binding sitei60Phosphoceramide1 Publication1
Binding sitei106Phosphoceramide1 Publication1
Binding sitei110Phosphoceramide1 Publication1
Binding sitei150Phosphoceramide1 Publication1

GO - Molecular functioni

  • ceramide 1-phosphate binding Source: UniProtKB
  • ceramide 1-phosphate transporter activity Source: UniProtKB
  • intermembrane lipid transfer activity Source: InterPro
  • phospholipid binding Source: UniProtKB
  • phospholipid transporter activity Source: UniProtKB

GO - Biological processi

  • ceramide 1-phosphate transport Source: UniProtKB
  • glycosphingolipid metabolic process Source: Reactome
  • negative regulation of autophagy Source: UniProtKB
  • negative regulation of interleukin-1 beta secretion Source: UniProtKB
  • negative regulation of NLRP3 inflammasome complex assembly Source: UniProtKB

Keywordsi

Biological processLipid transport, Transport
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-1660662 Glycosphingolipid metabolism

Chemistry databases

SwissLipidsiSLP:000000406

Names & Taxonomyi

Protein namesi
Recommended name:
Ceramide-1-phosphate transfer protein1 PublicationCurated
Short name:
CPTP1 PublicationCurated
Alternative name(s):
Glycolipid transfer protein domain-containing protein 1Curated
Short name:
GLTP domain-containing protein 11 PublicationCurated
Gene namesi
Name:CPTPImported
Synonyms:GLTPD11 PublicationImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000224051.6
HGNCiHGNC:28116 CPTP
MIMi615467 gene
neXtProtiNX_Q5TA50

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi42F → A: Increases phosphoceramide transfer. 1 Publication1
Mutagenesisi43L → R: Nearly abolishes phosphoceramide transfer. 1 Publication1
Mutagenesisi50F → R: Slightly reduces phosphoceramide transfer. 1 Publication1
Mutagenesisi53I → N: Slightly decreases phosphoceramide transfer. 1 Publication1
Mutagenesisi56D → V: Slightly decreases phosphoceramide transfer. 1 Publication1
Mutagenesisi60K → A: Nearly abolishes phosphoceramide transfer. Induces autophagy in a dominant negatif manner. 2 Publications1
Mutagenesisi97R → L: No effect. 1 Publication1
Mutagenesisi106R → L: Nearly abolishes phosphoceramide transfer. Induces autophagy in a dominant negatif manner. 2 Publications1
Mutagenesisi110R → L: Reduces phosphoceramide transfer. 1 Publication1
Mutagenesisi113R → E or L: Strongly reduces phosphoceramide transfer. 1 Publication1
Mutagenesisi117W → A: Slightly reduces phosphoceramide transfer. 1 Publication1
Mutagenesisi118L → R: Abolishes phosphoceramide transfer. 1 Publication1
Mutagenesisi149Y → A: Reduces phosphoceramide transfer. 1 Publication1
Mutagenesisi158V → N: Abolishes phosphoceramide transfer. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000224051
PharmGKBiPA162389853

Polymorphism and mutation databases

BioMutaiGLTPD1
DMDMi74745771

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003171561 – 214Ceramide-1-phosphate transfer proteinAdd BLAST214

Proteomic databases

EPDiQ5TA50
PaxDbiQ5TA50
PeptideAtlasiQ5TA50
PRIDEiQ5TA50

PTM databases

iPTMnetiQ5TA50

Expressioni

Tissue specificityi

Ubiquitous. Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.1 Publication

Gene expression databases

BgeeiENSG00000224051
CleanExiHS_GLTPD1
ExpressionAtlasiQ5TA50 baseline and differential
GenevisibleiQ5TA50 HS

Organism-specific databases

HPAiHPA056832

Interactioni

Protein-protein interaction databases

BioGridi1233057 interactors.
IntActiQ5TA50 8 interactors.
STRINGi9606.ENSP00000343890

Structurei

Secondary structure

1214
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 15Combined sources6
Helixi16 – 20Combined sources5
Helixi29 – 46Combined sources18
Helixi48 – 50Combined sources3
Helixi51 – 69Combined sources19
Helixi73 – 76Combined sources4
Helixi79 – 88Combined sources10
Beta strandi94 – 96Combined sources3
Helixi104 – 127Combined sources24
Helixi134 – 144Combined sources11
Helixi146 – 149Combined sources4
Helixi152 – 162Combined sources11
Helixi168 – 174Combined sources7
Beta strandi177 – 179Combined sources3
Helixi180 – 207Combined sources28

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4K80X-ray2.05A1-214[»]
4K84X-ray1.90A/B1-214[»]
4K85X-ray1.90A/B/C/D1-214[»]
4K8NX-ray3.10A/B/C/D/E/F1-214[»]
4KBSX-ray1.90A/B1-214[»]
4KF6X-ray3.20A/B/C/D/E/F1-214[»]
ProteinModelPortaliQ5TA50
SMRiQ5TA50
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GLTP family.Curated

Phylogenomic databases

eggNOGiKOG4189 Eukaryota
ENOG4111NKT LUCA
GeneTreeiENSGT00530000063818
HOGENOMiHOG000046738
HOVERGENiHBG100515
InParanoidiQ5TA50
OMAiDSGCRTV
OrthoDBiEOG091G0LIV
PhylomeDBiQ5TA50
TreeFamiTF316097

Family and domain databases

Gene3Di1.10.3520.101 hit
InterProiView protein in InterPro
IPR036497 GLTP_sf
IPR014830 Glycolipid_transfer_prot_dom
PfamiView protein in Pfam
PF08718 GLTP, 1 hit
SUPFAMiSSF110004 SSF110004, 1 hit

Sequencei

Sequence statusi: Complete.

Q5TA50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDSETGFNL KVVLVSFKQC LDEKEEVLLD PYIASWKGLV RFLNSLGTIF
60 70 80 90 100
SFISKDVVSK LRIMERLRGG PQSEHYRSLQ AMVAHELSNR LVDLERRSHH
110 120 130 140 150
PESGCRTVLR LHRALHWLQL FLEGLRTSPE DARTSALCAD SYNASLAAYH
160 170 180 190 200
PWVVRRAVTV AFCTLPTREV FLEAMNVGPP EQAVQMLGEA LPFIQRVYNV
210
SQKLYAEHSL LDLP
Length:214
Mass (Da):24,365
Last modified:December 21, 2004 - v1
Checksum:iB66F4581FD9C60A0
GO

Sequence cautioni

The sequence EAW56230 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR599582 mRNA No translation available.
AL139287 Genomic DNA No translation available.
CH471183 Genomic DNA Translation: EAW56230.1 Sequence problems.
BC098429 mRNA Translation: AAH98429.1
CCDSiCCDS30555.1
RefSeqiNP_001025056.1, NM_001029885.1
XP_005244858.1, XM_005244801.3
XP_011540502.1, XM_011542200.2
UniGeneiHs.515689

Genome annotation databases

EnsembliENST00000343938; ENSP00000343890; ENSG00000224051
GeneIDi80772
KEGGihsa:80772

Similar proteinsi

Entry informationi

Entry nameiCPTP_HUMAN
AccessioniPrimary (citable) accession number: Q5TA50
Secondary accession number(s): Q4G0E6, Q7L5A4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 21, 2004
Last modified: April 25, 2018
This is version 100 of the entry and version 1 of the sequence. See 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, Reference proteome