CPTP_MOUSE
ID CPTP_MOUSE Reviewed; 216 AA.
AC Q8BS40; A2ADA2; Q99LU9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ceramide-1-phosphate transfer protein {ECO:0000305};
DE Short=CPTP {ECO:0000305};
DE AltName: Full=Glycolipid transfer protein domain-containing protein 1 {ECO:0000305};
GN Name=Cptp {ECO:0000312|MGI:MGI:1933107};
GN Synonyms=Gltpd1 {ECO:0000312|MGI:MGI:1933107};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
RX PubMed=29164996; DOI=10.1080/15548627.2017.1393129;
RA Mishra S.K., Gao Y.G., Deng Y., Chalfant C.E., Hinchcliffe E.H.,
RA Brown R.E.;
RT "CPTP: A sphingolipid transfer protein that regulates autophagy and
RT inflammasome activation.";
RL Autophagy 14:862-879(2018).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
RX PubMed=23863933; DOI=10.1038/nature12332;
RA Simanshu D.K., Kamlekar R.K., Wijesinghe D.S., Zou X., Zhai X.,
RA Mishra S.K., Molotkovsky J.G., Malinina L., Hinchcliffe E.H.,
RA Chalfant C.E., Brown R.E., Patel D.J.;
RT "Non-vesicular trafficking by a ceramide-1-phosphate transfer protein
RT regulates eicosanoids.";
RL Nature 500:463-467(2013).
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 (By
CC similarity). Regulates autophagy, inflammasome mediated IL1B and IL18
CC processing, and pyroptosis, but not apoptosis (PubMed:29164996).
CC {ECO:0000250|UniProtKB:Q5TA50, ECO:0000269|PubMed:29164996}.
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; AK040664; BAC30659.1; -; mRNA.
DR EMBL; AL670236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002216; AAH02216.1; -; mRNA.
DR CCDS; CCDS19047.1; -.
DR RefSeq; NP_077792.2; NM_024472.4.
DR PDB; 4KBR; X-ray; 2.55 A; A/B/C/D/E/F/G/H=1-216.
DR PDBsum; 4KBR; -.
DR AlphaFoldDB; Q8BS40; -.
DR SMR; Q8BS40; -.
DR BioGRID; 219763; 1.
DR STRING; 10090.ENSMUSP00000030950; -.
DR PhosphoSitePlus; Q8BS40; -.
DR SwissPalm; Q8BS40; -.
DR MaxQB; Q8BS40; -.
DR PaxDb; Q8BS40; -.
DR PRIDE; Q8BS40; -.
DR ProteomicsDB; 284112; -.
DR Antibodypedia; 66414; 19 antibodies from 8 providers.
DR DNASU; 79554; -.
DR Ensembl; ENSMUST00000030950; ENSMUSP00000030950; ENSMUSG00000029073.
DR GeneID; 79554; -.
DR KEGG; mmu:79554; -.
DR UCSC; uc008wfg.1; mouse.
DR CTD; 80772; -.
DR MGI; MGI:1933107; Cptp.
DR VEuPathDB; HostDB:ENSMUSG00000029073; -.
DR eggNOG; KOG4189; Eukaryota.
DR GeneTree; ENSGT00940000161763; -.
DR HOGENOM; CLU_079649_1_0_1; -.
DR InParanoid; Q8BS40; -.
DR OMA; YKFFQLM; -.
DR OrthoDB; 1423493at2759; -.
DR PhylomeDB; Q8BS40; -.
DR TreeFam; TF316097; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR BioGRID-ORCS; 79554; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8BS40; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BS40; protein.
DR Bgee; ENSMUSG00000029073; Expressed in spermatid and 235 other tissues.
DR ExpressionAtlas; Q8BS40; baseline and differential.
DR Genevisible; Q8BS40; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:UniProtKB.
DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Endosome; Golgi apparatus;
KW Lipid transport; Lipid-binding; Membrane; Nucleus; Reference proteome;
KW Transport.
FT CHAIN 1..216
FT /note="Ceramide-1-phosphate transfer protein"
FT /id="PRO_0000317157"
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 108
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 112
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT BINDING 152
FT /ligand="an N-acylsphingoid base 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:84404"
FT /evidence="ECO:0000250|UniProtKB:Q5TA50"
FT CONFLICT 77
FT /note="A -> T (in Ref. 3; AAH02216)"
FT /evidence="ECO:0000305"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 51..69
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 106..129
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:4KBR"
FT HELIX 182..208
FT /evidence="ECO:0007829|PDB:4KBR"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:4KBR"
SQ SEQUENCE 216 AA; 24597 MW; 53A62214D3F0F18A CRC64;
MDDSEKDFNL KVVLVSFKQC LTDKGEVLLD HYIAGWKGLV RFLNSLGAVF SFISKDVVAK
LQIMERLRSS PQSEHYASLQ SMVAYEVSNK LVDMDHRSHP RHPHSGCRTV LRLHRALHWL
QLFLDGLRTS SEDARTSTLC SEAYNATLAN YHSWIVRQAV TVAFCALPSR KVFLEAMNME
STEQAVEMLG EALPFIEHVY DISQKLYAEH SLLDLP
