CPTP_DANRE
ID CPTP_DANRE Reviewed; 211 AA.
AC Q6DBQ8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ceramide-1-phosphate transfer protein;
DE AltName: Full=Glycolipid transfer protein domain-containing protein 1;
DE Short=CPTP;
GN Name=cptp; Synonyms=gltpd1; ORFNames=zgc:92000;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the intracellular transfer of ceramide-1-phosphate
CC (C1P) between organelle membranes and the cell membrane. Required for
CC normal structure of the Golgi stacks. Can bind phosphoceramides with a
CC variety of aliphatic chains, but has a preference for lipids with
CC saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is
CC inefficient with phosphoceramides containing lignoceryl (C24:0). Plays
CC a role in the regulation of the cellular levels of ceramide-1-
CC phosphate, and thereby contributes to the regulation of phospholipase
CC PLA2G4A activity and the release of arachidonic acid. Has no activity
CC with galactosylceramide, lactosylceramide, sphingomyelin,
CC phosphatidylcholine, phosphatidic acid and ceramide. C1P transfer is
CC stimulated by phosphatidylserine in C1P source vesicles. Regulates
CC autophagy and pyroptosis, but not apoptosis.
CC {ECO:0000250|UniProtKB:Q5TA50}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(hexadecanoyl)-sphing-4-enine-1-phosphate(in) = N-
CC (hexadecanoyl)-sphing-4-enine-1-phosphate(out); Xref=Rhea:RHEA:45680,
CC ChEBI:CHEBI:72963; Evidence={ECO:0000250|UniProtKB:Q5TA50};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45681;
CC Evidence={ECO:0000250|UniProtKB:Q5TA50};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(9Z-octadecenoyl)-sphing-4-enine-1-phosphate(in) = N-(9Z-
CC octadecenoyl)-sphing-4-enine-1-phosphate(out); Xref=Rhea:RHEA:45688,
CC ChEBI:CHEBI:85378; Evidence={ECO:0000250|UniProtKB:Q5TA50};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45689;
CC Evidence={ECO:0000250|UniProtKB:Q5TA50};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q5TA50}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5TA50}. Cell membrane
CC {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5TA50}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q5TA50}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5TA50}. Nucleus outer membrane
CC {ECO:0000250|UniProtKB:Q5TA50}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5TA50}.
CC -!- SIMILARITY: Belongs to the GLTP family. {ECO:0000305}.
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DR EMBL; BC078407; AAH78407.1; -; mRNA.
DR RefSeq; NP_001003497.1; NM_001003497.1.
DR AlphaFoldDB; Q6DBQ8; -.
DR SMR; Q6DBQ8; -.
DR STRING; 7955.ENSDARP00000068896; -.
DR PaxDb; Q6DBQ8; -.
DR DNASU; 791641; -.
DR GeneID; 791641; -.
DR KEGG; dre:791641; -.
DR CTD; 80772; -.
DR ZFIN; ZDB-GENE-040801-240; cptp.
DR eggNOG; KOG4189; Eukaryota.
DR InParanoid; Q6DBQ8; -.
DR OrthoDB; 1423493at2759; -.
DR PhylomeDB; Q6DBQ8; -.
DR Reactome; R-DRE-1660662; Glycosphingolipid metabolism.
DR PRO; PR:Q6DBQ8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1902387; F:ceramide 1-phosphate binding; ISS:UniProtKB.
DR GO; GO:1902388; F:ceramide 1-phosphate transfer activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:1902389; P:ceramide 1-phosphate transport; ISS:UniProtKB.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR Gene3D; 1.10.3520.10; -; 1.
DR InterPro; IPR036497; GLTP_sf.
DR InterPro; IPR014830; Glycolipid_transfer_prot_dom.
DR Pfam; PF08718; GLTP; 1.
DR SUPFAM; SSF110004; SSF110004; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Endosome; Golgi apparatus; Lipid transport;
KW Lipid-binding; Membrane; Nucleus; Reference proteome; Transport.
FT CHAIN 1..211
FT /note="Ceramide-1-phosphate transfer protein"
FT /id="PRO_0000317159"
FT BINDING 53
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 57
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 103
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 107
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 147
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
SQ SEQUENCE 211 AA; 23993 MW; E57D58D6AF0E6D7D CRC64;
MADAFSLQRV LETFRSSLSE NKEVYIKYYI AGWQELVSFM NSLGNVFSFI SKDVVSKIQI
LENFLSGENG SNYVTIQSMV KYELENDLVD LTKRGSHPES GCRTLLRLHR ALRWLELFLE
RLRTSTEDSK TSVMCSDAYN ESLANHHPWL IRKAVGVAFC ALPGRETFFD VMNAGDHTQV
VALLGESLPL IAEVYQITED LYAKNNLLEL P
