CPTP_XENLA
ID CPTP_XENLA Reviewed; 215 AA.
AC Q5HZ92;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 61.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) 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; BC089129; AAH89129.1; -; mRNA.
DR RefSeq; NP_001089978.1; NM_001096509.1.
DR AlphaFoldDB; Q5HZ92; -.
DR SMR; Q5HZ92; -.
DR MaxQB; Q5HZ92; -.
DR DNASU; 735049; -.
DR GeneID; 735049; -.
DR KEGG; xla:735049; -.
DR CTD; 735049; -.
DR Xenbase; XB-GENE-974135; cptp.L.
DR OMA; YKFFQLM; -.
DR OrthoDB; 1423493at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 735049; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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: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..215
FT /note="Ceramide-1-phosphate transfer protein"
FT /id="PRO_0000317160"
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 61
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 111
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 151
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
SQ SEQUENCE 215 AA; 24680 MW; C431592BBEE30600 CRC64;
MSSTEEKFSL KEVLVSFKAC LIDDDKDVIL EHYVNGWKGL VRFMSSLGTI FSFVSKDAVS
KIQIMESYLA GPNGERYRTL QSMVEYELSS DLVDLTKRSD HTDSGCRTLL RLHRALRWLQ
LFLEKLRVSN EDSKTSTLCT EAYNDSLANF HPWIVRKAAT VSFIALPYRN TFFEIMNVGT
TEEVVAMLGE SMPYVTKVYD FTQEVYSQHN LLELP
