CPTP_BOVIN
ID CPTP_BOVIN Reviewed; 214 AA.
AC Q0VCQ0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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, inflammasome mediated IL1B and IL18 processing, and
CC pyroptosis, but not apoptosis. {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; BC120059; AAI20060.1; -; mRNA.
DR RefSeq; NP_001068650.1; NM_001075182.2.
DR RefSeq; XP_005217094.1; XM_005217037.3.
DR RefSeq; XP_005217095.1; XM_005217038.2.
DR AlphaFoldDB; Q0VCQ0; -.
DR SMR; Q0VCQ0; -.
DR STRING; 9913.ENSBTAP00000010025; -.
DR PaxDb; Q0VCQ0; -.
DR PRIDE; Q0VCQ0; -.
DR Ensembl; ENSBTAT00000010025; ENSBTAP00000010025; ENSBTAG00000007623.
DR GeneID; 505009; -.
DR KEGG; bta:505009; -.
DR CTD; 80772; -.
DR VEuPathDB; HostDB:ENSBTAG00000007623; -.
DR VGNC; VGNC:27680; CPTP.
DR eggNOG; KOG4189; Eukaryota.
DR GeneTree; ENSGT00940000161763; -.
DR HOGENOM; CLU_079649_1_0_1; -.
DR InParanoid; Q0VCQ0; -.
DR OMA; YKFFQLM; -.
DR OrthoDB; 1423493at2759; -.
DR TreeFam; TF316097; -.
DR Reactome; R-BTA-1660662; Glycosphingolipid metabolism.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000007623; Expressed in zone of skin and 105 other tissues.
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..214
FT /note="Ceramide-1-phosphate transfer protein"
FT /id="PRO_0000317155"
FT BINDING 56
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 60
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 106
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 110
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 150
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
SQ SEQUENCE 214 AA; 24574 MW; 50089ED405CC413F CRC64;
MDDLESEFNL KVVLVSFKQC LNEKEEVLLE YYLAGWRGLV RFLNSLGTIF SFISKDVVTK
LQIMDQLRSG PQQEHYSSLQ AMVAYEVGNQ LVDLERRSRH PDSGCRTVLR LHRALRWLQL
FLEGVRTSPE DARTSVLCTD SYNASLATYH PWIIRRAVTV AFCALPTRKV FLESMNVGSS
EQAVEMLNEA LPFIERVYNI SQKLYAEHAL LDLP
