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Q5TA50 (CPTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ceramide-1-phosphate transfer protein

Short name=CPTP
Alternative name(s):
Glycolipid transfer protein domain-containing protein 1
Short name=GLTP domain-containing protein 1
Gene names
Name:GLTPD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the intracellular transfer of ceramide-1-phosphate 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. Ref.5

Subcellular location

Cytoplasmcytosol. Golgi apparatustrans-Golgi network membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein. Nucleus outer membrane; Peripheral membrane protein Ref.5.

Tissue specificity

Ubiquitous. Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. Ref.5

Sequence similarities

Belongs to the GLTP family.

Sequence caution

The sequence EAW56230.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 214214Ceramide-1-phosphate transfer protein
PRO_0000317156

Sites

Binding site561Phosphoceramide
Binding site601Phosphoceramide
Binding site1061Phosphoceramide
Binding site1101Phosphoceramide
Binding site1501Phosphoceramide

Experimental info

Mutagenesis421F → A: Increases phosphoceramide transfer. Ref.5
Mutagenesis431L → R: Nearly abolishes phosphoceramide transfer. Ref.5
Mutagenesis501F → R: Slightly reduces phosphoceramide transfer. Ref.5
Mutagenesis531I → N: Slightly decreases phosphoceramide transfer. Ref.5
Mutagenesis561D → V: Slightly decreases phosphoceramide transfer. Ref.5
Mutagenesis601K → A: Nearly abolishes phosphoceramide transfer. Ref.5
Mutagenesis971R → L: No effect. Ref.5
Mutagenesis1061R → L: Nearly abolishes phosphoceramide transfer. Ref.5
Mutagenesis1101R → L: Reduces phosphoceramide transfer. Ref.5
Mutagenesis1131R → E or L: Strongly reduces phosphoceramide transfer. Ref.5
Mutagenesis1171W → A: Slightly reduces phosphoceramide transfer. Ref.5
Mutagenesis1181L → R: Abolishes phosphoceramide transfer. Ref.5
Mutagenesis1491Y → A: Reduces phosphoceramide transfer. Ref.5
Mutagenesis1581V → N: Abolishes phosphoceramide transfer. Ref.5

Secondary structure

............................ 214
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5TA50 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: B66F4581FD9C60A0

FASTA21424,365
        10         20         30         40         50         60 
MDDSETGFNL KVVLVSFKQC LDEKEEVLLD PYIASWKGLV RFLNSLGTIF SFISKDVVSK 

        70         80         90        100        110        120 
LRIMERLRGG PQSEHYRSLQ AMVAHELSNR LVDLERRSHH PESGCRTVLR LHRALHWLQL 

       130        140        150        160        170        180 
FLEGLRTSPE DARTSALCAD SYNASLAAYH PWVVRRAVTV AFCTLPTREV FLEAMNVGPP 

       190        200        210 
EQAVQMLGEA LPFIQRVYNV SQKLYAEHSL LDLP 

« Hide

References

« Hide 'large scale' references
[1]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: B-cell.
[2]"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. expand/collapse author list , 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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] OF 55-214.
Tissue: Neuroblastoma.
[5]"Non-vesicular trafficking by a ceramide-1-phosphate transfer protein regulates eicosanoids."
Simanshu D.K., Kamlekar R.K., Wijesinghe D.S., Zou X., Zhai X., Mishra S.K., Molotkovsky J.G., Malinina L., Hinchcliffe E.H., Chalfant C.E., Brown R.E., Patel D.J.
Nature 500:463-467(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH CERAMIDE-1-PHOSPHATE, FUNCTION, SUBCELLULAR LOCATION, LIPID-BINDING, MUTAGENESIS OF PHE-42; LEU-43; PHE-50; ILE-53; ASP-56; LYS-60; ARG-97; ARG-106; ARG-110; ARG-113; TRP-117; LEU-118; TYR-149 AND VAL-158, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR599582 mRNA. No translation available.
AL139287 Genomic DNA. Translation: CAI23183.1.
CH471183 Genomic DNA. Translation: EAW56230.1. Sequence problems.
BC098429 mRNA. Translation: AAH98429.1.
CCDSCCDS30555.1.
RefSeqNP_001025056.1. NM_001029885.1.
XP_005244858.1. XM_005244801.1.
UniGeneHs.515689.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ5TA50.
SMRQ5TA50. Positions 7-214.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123305. 8 interactions.
IntActQ5TA50. 7 interactions.
STRING9606.ENSP00000343890.

Polymorphism databases

DMDM74745771.

Proteomic databases

MaxQBQ5TA50.
PaxDbQ5TA50.
PeptideAtlasQ4G0E6.
PRIDEQ5TA50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343938; ENSP00000343890; ENSG00000224051.
GeneID80772.
KEGGhsa:80772.
UCSCuc001aeo.3. human.

Organism-specific databases

CTD80772.
GeneCardsGC01P001251.
HGNCHGNC:28116. GLTPD1.
HPAHPA056832.
MIM615467. gene.
neXtProtNX_Q5TA50.
PharmGKBPA162389853.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG309816.
HOGENOMHOG000046738.
HOVERGENHBG100515.
InParanoidQ5TA50.
OMAQSMVAYE.
OrthoDBEOG7BW0MQ.
PhylomeDBQ5TA50.
TreeFamTF316097.

Gene expression databases

ArrayExpressQ5TA50.
BgeeQ5TA50.
CleanExHS_GLTPD1.
GenevestigatorQ5TA50.

Family and domain databases

Gene3D1.10.3520.10. 1 hit.
InterProIPR014830. Glycolipid_transfer_prot_dom.
[Graphical view]
PfamPF08718. GLTP. 1 hit.
[Graphical view]
SUPFAMSSF110004. SSF110004. 1 hit.
ProtoNetSearch...

Other

NextBio71160.
PROQ5TA50.
SOURCESearch...

Entry information

Entry nameCPTP_HUMAN
AccessionPrimary (citable) accession number: Q5TA50
Secondary accession number(s): Q4G0E6, Q7L5A4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM