ID CERT_HUMAN Reviewed; 624 AA. AC Q9Y5P4; A8K7S2; B3KUB7; Q53YV1; Q53YV2; Q96Q85; Q96Q88; Q9H2S7; Q9H2S8; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=Ceramide transfer protein {ECO:0000303|PubMed:14685229, ECO:0000305}; DE Short=hCERT {ECO:0000303|PubMed:14685229}; DE AltName: Full=Collagen type IV alpha-3-binding protein {ECO:0000305}; DE AltName: Full=Goodpasture antigen-binding protein {ECO:0000303|PubMed:10212244}; DE Short=GPBP; DE AltName: Full=START domain-containing protein 11; DE Short=StARD11; DE AltName: Full=StAR-related lipid transfer protein 11; GN Name=CERT1 {ECO:0000312|HGNC:HGNC:2205}; GN Synonyms=CERT, COL4A3BP {ECO:0000312|HGNC:HGNC:2205}, STARD11; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION. RX PubMed=10212244; DOI=10.1074/jbc.274.18.12642; RA Raya A., Revert F., Navarro S., Saus J.; RT "Characterization of a novel type of serine/threonine kinase that RT specifically phosphorylates the human goodpasture antigen."; RL J. Biol. Chem. 274:12642-12649(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). RX PubMed=11007769; DOI=10.1074/jbc.m002769200; RA Raya A., Revert-Ros F., Martinez-Martinez P., Navarro S., Rosello E., RA Vieites B., Granero F., Forteza J., Saus J.; RT "Goodpasture antigen-binding protein, the kinase that phosphorylates the RT Goodpasture antigen, is an alternatively spliced variant implicated in RT autoimmune pathogenesis."; RL J. Biol. Chem. 275:40392-40399(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND DOMAIN START. RX PubMed=14685229; DOI=10.1038/nature02188; RA Hanada K., Kumagai K., Yasuda S., Miura Y., Kawano M., Fukasawa M., RA Nishijima M.; RT "Molecular machinery for non-vesicular trafficking of ceramide."; RL Nature 426:803-809(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Lung, and Synovium; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77. RA Ogi T., Yamamoto Y., Ohmori H.; RT "Homo sapiens genomic sequence, containing DINB1 and GPBP gene."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP INTERACTION WITH VAPA AND VAPB, SUBCELLULAR LOCATION, MUTAGENESIS OF RP ASP-324, DOMAIN FFAT MOTIF, AND DOMAIN PH. RX PubMed=16895911; DOI=10.1074/jbc.m605032200; RA Kawano M., Kumagai K., Nishijima M., Hanada K.; RT "Efficient trafficking of ceramide from the endoplasmic reticulum to the RT Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif RT of CERT."; RL J. Biol. Chem. 281:30279-30288(2006). RN [11] RP PHOSPHORYLATION AT SER-132, FUNCTION, AND MUTAGENESIS OF SER-132. RX PubMed=17591919; DOI=10.1083/jcb.200612017; RA Fugmann T., Hausser A., Schoeffler P., Schmid S., Pfizenmaier K., RA Olayioye M.A.; RT "Regulation of secretory transport by protein kinase D-mediated RT phosphorylation of the ceramide transfer protein."; RL J. Cell Biol. 178:15-22(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP PHOSPHORYLATION BY CSNK1G2/CK1. RX PubMed=19005213; DOI=10.1091/mbc.e08-07-0669; RA Tomishige N., Kumagai K., Kusuda J., Nishijima M., Hanada K.; RT "Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the RT synthesis of sphingomyelin."; RL Mol. Biol. Cell 20:348-357(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; TYR-372; SER-373 AND RP SER-380, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP INVOLVEMENT IN MRD34, AND VARIANT MRD34 LEU-132. RX PubMed=25533962; DOI=10.1038/nature14135; RG Deciphering Developmental Disorders Study; RT "Large-scale discovery of novel genetic causes of developmental RT disorders."; RL Nature 519:223-228(2015). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MOSPD2, SUBCELLULAR RP LOCATION, DOMAIN, FFAT MOTIF, AND MUTAGENESIS OF ASP-324. RX PubMed=29858488; DOI=10.15252/embr.201745453; RA Di Mattia T., Wilhelm L.P., Ikhlef S., Wendling C., Spehner D., Nomine Y., RA Giordano F., Mathelin C., Drin G., Tomasetto C., Alpy F.; RT "Identification of MOSPD2, a novel scaffold for endoplasmic reticulum RT membrane contact sites."; RL EMBO Rep. 19:0-0(2018). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 347-624 IN COMPLEXES WITH RP CERAMIDES AND DIACYLGLYCEROL, MUTAGENESIS OF GLU-472; GLN-493 AND ASN-530, RP FUNCTION, SUBCELLULAR LOCATION, AND CERAMIDE-BINDING. RX PubMed=18184806; DOI=10.1073/pnas.0709191105; RA Kudo N., Kumagai K., Tomishige N., Yamaji T., Wakatsuki S., Nishijima M., RA Hanada K., Kato R.; RT "Structural basis for specific lipid recognition by CERT responsible for RT nonvesicular trafficking of ceramide."; RL Proc. Natl. Acad. Sci. U.S.A. 105:488-493(2008). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 347-624 IN COMPLEXES WITH RP CERAMIDE AND INHIBITOR, MUTAGENESIS OF TRP-499, FUNCTION, AND RP CERAMIDE-BINDING. RX PubMed=20036255; DOI=10.1016/j.jmb.2009.12.029; RA Kudo N., Kumagai K., Matsubara R., Kobayashi S., Hanada K., Wakatsuki S., RA Kato R.; RT "Crystal structures of the CERT START domain with inhibitors provide RT insights into the mechanism of ceramide transfer."; RL J. Mol. Biol. 396:245-251(2010). RN [22] RP VARIANT CYS-138. RX PubMed=23033978; DOI=10.1056/nejmoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., RA Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(2012). RN [23] RP VARIANT MRD34 ARG-243. RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772; RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L., RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E., RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S., RA Rouleau G.A., Michaud J.L.; RT "De novo mutations in moderate or severe intellectual disability."; RL PLoS Genet. 10:E1004772-E1004772(2014). CC -!- FUNCTION: Shelters ceramides and diacylglycerol lipids inside its START CC domain and mediates the intracellular trafficking of ceramides and CC diacylglycerol lipids in a non-vesicular manner. CC {ECO:0000269|PubMed:14685229, ECO:0000269|PubMed:17591919, CC ECO:0000269|PubMed:18184806, ECO:0000269|PubMed:20036255}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-hexadecanoylsphing-4-enine(in) = N-hexadecanoylsphing-4- CC enine(out); Xref=Rhea:RHEA:45720, ChEBI:CHEBI:72959; CC Evidence={ECO:0000250|UniProtKB:Q6VVX2}; CC -!- SUBUNIT: Interacts with VAPA and VAPB. Interaction with VAPB is less CC efficient than with VAPA (PubMed:16895911). Interacts (via FFAT motif) CC with MOSPD2 (via MSP domain) (PubMed:29858488). CC {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:29858488}. CC -!- INTERACTION: CC Q9Y5P4; Q9H568: ACTL8; NbExp=3; IntAct=EBI-739994, EBI-10306917; CC Q9Y5P4; Q15041: ARL6IP1; NbExp=5; IntAct=EBI-739994, EBI-714543; CC Q9Y5P4; P78368: CSNK1G2; NbExp=5; IntAct=EBI-739994, EBI-748380; CC Q9Y5P4; Q13352: ITGB3BP; NbExp=4; IntAct=EBI-739994, EBI-712105; CC Q9Y5P4; O95197: RTN3; NbExp=3; IntAct=EBI-739994, EBI-740467; CC Q9Y5P4; Q9NQC3: RTN4; NbExp=3; IntAct=EBI-739994, EBI-715945; CC Q9Y5P4-1; P02743: APCS; NbExp=6; IntAct=EBI-21199571, EBI-2115799; CC Q9Y5P4-2; Q9H568: ACTL8; NbExp=3; IntAct=EBI-11156432, EBI-10306917; CC Q9Y5P4-2; P02743: APCS; NbExp=4; IntAct=EBI-11156432, EBI-2115799; CC Q9Y5P4-2; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-11156432, EBI-714543; CC Q9Y5P4-2; Q8WZ55: BSND; NbExp=3; IntAct=EBI-11156432, EBI-7996695; CC Q9Y5P4-2; Q9Y5P4-2: CERT1; NbExp=3; IntAct=EBI-11156432, EBI-11156432; CC Q9Y5P4-2; P78368: CSNK1G2; NbExp=4; IntAct=EBI-11156432, EBI-748380; CC Q9Y5P4-2; Q9UET6: FTSJ1; NbExp=3; IntAct=EBI-11156432, EBI-1055987; CC Q9Y5P4-2; Q9UPX6: MINAR1; NbExp=3; IntAct=EBI-11156432, EBI-11977115; CC Q9Y5P4-2; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-11156432, EBI-11339910; CC Q9Y5P4-2; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-11156432, EBI-14065960; CC Q9Y5P4-2; Q2TAY7: SMU1; NbExp=3; IntAct=EBI-11156432, EBI-298027; CC Q9Y5P4-2; P32856-2: STX2; NbExp=3; IntAct=EBI-11156432, EBI-11956649; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16895911, CC ECO:0000269|PubMed:18184806}. Golgi apparatus CC {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806, CC ECO:0000269|PubMed:29858488}. Endoplasmic reticulum CC {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806}. CC Note=Preferentially localized to the Golgi apparatus. CC {ECO:0000305|PubMed:16895911}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=CERTL {ECO:0000303|PubMed:14685229}; CC IsoId=Q9Y5P4-1; Sequence=Displayed; CC Name=2; Synonyms=Delta26, GPBPD26, CERT {ECO:0000303|PubMed:14685229}; CC IsoId=Q9Y5P4-2; Sequence=VSP_006276; CC Name=3; CC IsoId=Q9Y5P4-3; Sequence=VSP_041022; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DOMAIN: The START domain recognizes ceramides and diacylglycerol CC lipids, interacts with membranes, and mediates the intermembrane CC transfer of ceramides and diacylglycerol lipids. CC {ECO:0000269|PubMed:14685229}. CC -!- DOMAIN: The PH domain targets the Golgi apparatus. CC {ECO:0000269|PubMed:16895911}. CC -!- DOMAIN: The FFAT motif is required for interaction with VAPA, VAPB and CC MOSPD2. {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:29858488}. CC -!- PTM: Phosphorylation on Ser-132 decreases the affinity toward CC phosphatidylinositol 4-phosphate at Golgi membranes and reduces CC ceramide transfer activity. Inactivated by hyperphosphorylation of CC serine residues by CSNK1G2/CK1 that triggers dissociation from the CC Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide CC and sphingomyelin synthesis. {ECO:0000269|PubMed:17591919, CC ECO:0000269|PubMed:19005213}. CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 34 CC (MRD34) [MIM:616351]: A disorder characterized by significantly below CC average general intellectual functioning associated with impairments in CC adaptive behavior and manifested during the developmental period. CC {ECO:0000269|PubMed:25356899, ECO:0000269|PubMed:25533962}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- CAUTION: Was originally reported to have a protein kinase activity and CC to phosphorylate on Ser and Thr residues the Goodpasture autoantigen CC (in vitro). {ECO:0000305|PubMed:10212244}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF136450; AAD30288.1; -; mRNA. DR EMBL; AF232930; AAG42046.1; -; mRNA. DR EMBL; AF232935; AAG42051.1; -; Genomic_DNA. DR EMBL; AY453385; AAR26717.1; -; mRNA. DR EMBL; AY453386; AAR26718.1; -; mRNA. DR EMBL; AK091851; BAC03762.1; -; mRNA. DR EMBL; AK096854; BAG53379.1; -; mRNA. DR EMBL; AK292087; BAF84776.1; -; mRNA. DR EMBL; AC008897; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112183; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC116341; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471084; EAW95757.1; -; Genomic_DNA. DR EMBL; CH471084; EAW95760.1; -; Genomic_DNA. DR EMBL; BC000102; AAH00102.1; -; mRNA. DR EMBL; AB036934; BAB58974.1; -; Genomic_DNA. DR EMBL; AB036936; BAB58977.1; -; Genomic_DNA. DR CCDS; CCDS4028.1; -. [Q9Y5P4-1] DR CCDS; CCDS4029.1; -. [Q9Y5P4-2] DR CCDS; CCDS47235.1; -. [Q9Y5P4-3] DR RefSeq; NP_001123577.1; NM_001130105.1. [Q9Y5P4-3] DR RefSeq; NP_005704.1; NM_005713.2. [Q9Y5P4-1] DR RefSeq; NP_112729.1; NM_031361.2. [Q9Y5P4-2] DR RefSeq; XP_006714576.1; XM_006714513.2. DR RefSeq; XP_016864408.1; XM_017008919.1. DR PDB; 2E3M; X-ray; 2.20 A; A=347-624. DR PDB; 2E3N; X-ray; 1.40 A; A=347-624. DR PDB; 2E3O; X-ray; 1.55 A; A=347-624. DR PDB; 2E3P; X-ray; 1.40 A; A/B=347-624. DR PDB; 2E3Q; X-ray; 2.08 A; A=347-624. DR PDB; 2E3R; X-ray; 1.65 A; A/B=347-624. DR PDB; 2E3S; X-ray; 1.94 A; A=347-624. DR PDB; 2RSG; NMR; -; A=24-117. DR PDB; 2Z9Y; X-ray; 1.80 A; A=347-624. DR PDB; 2Z9Z; X-ray; 1.74 A; A=347-624. DR PDB; 3H3Q; X-ray; 2.00 A; A/B=347-624. DR PDB; 3H3R; X-ray; 1.85 A; A/B=347-624. DR PDB; 3H3S; X-ray; 1.66 A; A/B=347-624. DR PDB; 3H3T; X-ray; 2.40 A; A/B=347-624. DR PDB; 4HHV; X-ray; 1.75 A; A/B=20-121. DR PDB; 5JJD; X-ray; 2.40 A; A=20-122, B=385-624. DR PDB; 5ZYG; X-ray; 1.80 A; A=390-624. DR PDB; 5ZYH; X-ray; 1.95 A; A=390-624. DR PDB; 5ZYI; X-ray; 1.90 A; A=390-624. DR PDB; 5ZYJ; X-ray; 1.90 A; A=390-624. DR PDB; 5ZYK; X-ray; 1.55 A; A=390-624. DR PDB; 5ZYL; X-ray; 1.80 A; A=390-624. DR PDB; 5ZYM; X-ray; 1.90 A; A=390-624. DR PDB; 6IEZ; X-ray; 1.90 A; A=390-624. DR PDB; 6IF0; X-ray; 1.80 A; A=390-624. DR PDB; 6J0O; X-ray; 1.80 A; A=390-624. DR PDB; 6J81; X-ray; 1.80 A; A=390-624. DR PDBsum; 2E3M; -. DR PDBsum; 2E3N; -. DR PDBsum; 2E3O; -. DR PDBsum; 2E3P; -. DR PDBsum; 2E3Q; -. DR PDBsum; 2E3R; -. DR PDBsum; 2E3S; -. DR PDBsum; 2RSG; -. DR PDBsum; 2Z9Y; -. DR PDBsum; 2Z9Z; -. DR PDBsum; 3H3Q; -. DR PDBsum; 3H3R; -. DR PDBsum; 3H3S; -. DR PDBsum; 3H3T; -. DR PDBsum; 4HHV; -. DR PDBsum; 5JJD; -. DR PDBsum; 5ZYG; -. DR PDBsum; 5ZYH; -. DR PDBsum; 5ZYI; -. DR PDBsum; 5ZYJ; -. DR PDBsum; 5ZYK; -. DR PDBsum; 5ZYL; -. DR PDBsum; 5ZYM; -. DR PDBsum; 6IEZ; -. DR PDBsum; 6IF0; -. DR PDBsum; 6J0O; -. DR PDBsum; 6J81; -. DR AlphaFoldDB; Q9Y5P4; -. DR BMRB; Q9Y5P4; -. DR SASBDB; Q9Y5P4; -. DR SMR; Q9Y5P4; -. DR BioGRID; 115396; 57. DR ELM; Q9Y5P4; -. DR IntAct; Q9Y5P4; 35. DR MINT; Q9Y5P4; -. DR STRING; 9606.ENSP00000383996; -. DR BindingDB; Q9Y5P4; -. DR ChEMBL; CHEMBL3399913; -. DR SwissLipids; SLP:000000407; -. DR TCDB; 2.D.1.1.10; the pi4p/ps counter transporter (p/p-ct) family. DR iPTMnet; Q9Y5P4; -. DR PhosphoSitePlus; Q9Y5P4; -. DR BioMuta; COL4A3BP; -. DR DMDM; 20978413; -. DR EPD; Q9Y5P4; -. DR jPOST; Q9Y5P4; -. DR MassIVE; Q9Y5P4; -. DR MaxQB; Q9Y5P4; -. DR PaxDb; 9606-ENSP00000369862; -. DR PeptideAtlas; Q9Y5P4; -. DR ProteomicsDB; 86463; -. [Q9Y5P4-1] DR ProteomicsDB; 86464; -. [Q9Y5P4-2] DR ProteomicsDB; 86465; -. [Q9Y5P4-3] DR Pumba; Q9Y5P4; -. DR Antibodypedia; 24390; 407 antibodies from 35 providers. DR DNASU; 10087; -. DR Ensembl; ENST00000261415.12; ENSP00000261415.8; ENSG00000113163.19. [Q9Y5P4-1] DR Ensembl; ENST00000405807.10; ENSP00000383996.4; ENSG00000113163.19. [Q9Y5P4-3] DR Ensembl; ENST00000643780.2; ENSP00000495760.1; ENSG00000113163.19. [Q9Y5P4-1] DR Ensembl; ENST00000644072.2; ENSP00000494110.2; ENSG00000113163.19. [Q9Y5P4-1] DR Ensembl; ENST00000644445.1; ENSP00000496243.1; ENSG00000113163.19. [Q9Y5P4-2] DR Ensembl; ENST00000645483.1; ENSP00000493563.1; ENSG00000113163.19. [Q9Y5P4-2] DR Ensembl; ENST00000646511.1; ENSP00000495446.1; ENSG00000113163.19. [Q9Y5P4-2] DR GeneID; 10087; -. DR KEGG; hsa:10087; -. DR MANE-Select; ENST00000643780.2; ENSP00000495760.1; NM_001379029.1; NP_001365958.1. DR UCSC; uc003kds.4; human. [Q9Y5P4-1] DR AGR; HGNC:2205; -. DR CTD; 10087; -. DR DisGeNET; 10087; -. DR GeneCards; CERT1; -. DR HGNC; HGNC:2205; CERT1. DR HPA; ENSG00000113163; Low tissue specificity. DR MalaCards; CERT1; -. DR MIM; 604677; gene. DR MIM; 616351; phenotype. DR neXtProt; NX_Q9Y5P4; -. DR OpenTargets; ENSG00000113163; -. DR PharmGKB; PA26720; -. DR VEuPathDB; HostDB:ENSG00000113163; -. DR eggNOG; KOG1739; Eukaryota. DR GeneTree; ENSGT00940000155123; -. DR HOGENOM; CLU_017289_0_0_1; -. DR InParanoid; Q9Y5P4; -. DR OMA; SLFWSHM; -. DR OrthoDB; 5489052at2759; -. DR PhylomeDB; Q9Y5P4; -. DR TreeFam; TF106160; -. DR BRENDA; 2.7.11.9; 2681. DR PathwayCommons; Q9Y5P4; -. DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis. [Q9Y5P4-2] DR SignaLink; Q9Y5P4; -. DR SIGNOR; Q9Y5P4; -. DR BioGRID-ORCS; 10087; 34 hits in 1152 CRISPR screens. DR ChiTaRS; COL4A3BP; human. DR EvolutionaryTrace; Q9Y5P4; -. DR GeneWiki; COL4A3BP; -. DR GenomeRNAi; 10087; -. DR Pharos; Q9Y5P4; Tbio. DR PRO; PR:Q9Y5P4; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9Y5P4; Protein. DR Bgee; ENSG00000113163; Expressed in sperm and 213 other cell types or tissues. DR ExpressionAtlas; Q9Y5P4; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:1902387; F:ceramide 1-phosphate binding; IBA:GO_Central. DR GO; GO:1902388; F:ceramide 1-phosphate transfer activity; IBA:GO_Central. DR GO; GO:0097001; F:ceramide binding; IDA:UniProtKB. DR GO; GO:0120017; F:ceramide transfer activity; IDA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0016301; F:kinase activity; IEA:Ensembl. DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl. DR GO; GO:0006672; P:ceramide metabolic process; IEA:Ensembl. DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central. DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl. DR GO; GO:0035621; P:ER to Golgi ceramide transport; IMP:UniProtKB. DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central. DR GO; GO:0120012; P:intermembrane sphingolipid transfer; IDA:UniProtKB. DR GO; GO:0055088; P:lipid homeostasis; IEA:Ensembl. DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl. DR GO; GO:0006936; P:muscle contraction; IEA:Ensembl. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IEA:Ensembl. DR CDD; cd13283; PH_GPBP; 1. DR CDD; cd08872; START_STARD11-like; 1. DR Gene3D; 3.30.530.20; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR041952; STARD11_START. DR InterPro; IPR023393; START-like_dom_sf. DR InterPro; IPR002913; START_lipid-bd_dom. DR PANTHER; PTHR19308:SF53; CERAMIDE TRANSFER PROTEIN; 1. DR PANTHER; PTHR19308; PHOSPHATIDYLCHOLINE TRANSFER PROTEIN; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF01852; START; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00234; START; 1. DR SUPFAM; SSF55961; Bet v1-like; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50848; START; 1. DR Genevisible; Q9Y5P4; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; KW Disease variant; Endoplasmic reticulum; Golgi apparatus; KW Intellectual disability; Lipid transport; Lipid-binding; Phosphoprotein; KW Reference proteome; Transport. FT CHAIN 1..624 FT /note="Ceramide transfer protein" FT /id="PRO_0000220665" FT DOMAIN 23..117 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 389..618 FT /note="START" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 263..303 FT /evidence="ECO:0000255" FT MOTIF 321..327 FT /note="FFAT" FT /evidence="ECO:0000269|PubMed:16895911, FT ECO:0000269|PubMed:29858488" FT COMPBIAS 1..16 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 472 FT /ligand="an N-acylsphing-4-enine" FT /ligand_id="ChEBI:CHEBI:52639" FT /evidence="ECO:0000269|PubMed:18184806, FT ECO:0000269|PubMed:20036255" FT BINDING 493 FT /ligand="an N-acylsphing-4-enine" FT /ligand_id="ChEBI:CHEBI:52639" FT /evidence="ECO:0000269|PubMed:18184806, FT ECO:0000269|PubMed:20036255" FT BINDING 530 FT /ligand="an N-acylsphing-4-enine" FT /ligand_id="ChEBI:CHEBI:52639" FT /evidence="ECO:0000269|PubMed:18184806, FT ECO:0000269|PubMed:20036255" FT BINDING 579 FT /ligand="an N-acylsphing-4-enine" FT /ligand_id="ChEBI:CHEBI:52639" FT /evidence="ECO:0000269|PubMed:18184806, FT ECO:0000269|PubMed:20036255" FT MOD_RES 126 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 132 FT /note="Phosphoserine; by PKD" FT /evidence="ECO:0000269|PubMed:17591919" FT MOD_RES 135 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9EQG9" FT MOD_RES 315 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 372 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 373 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 377 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 380 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1 FT /note="M -> MQHSCIPTPPSPFSAPPAFLPVVTRESRRGLSSGGSAGRNAGVTATA FT AAADGWKGRLPSPLVLLPRSARCQARRRRGGRTSSLLLLPPTPERALFASPSPDPSPRG FT LGASSGAAEGAGAGLLLGCRASM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041022" FT VAR_SEQ 371..396 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11007769, FT ECO:0000303|PubMed:14685229, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_006276" FT VARIANT 132 FT /note="S -> L (in MRD34; dbSNP:rs1064794019)" FT /evidence="ECO:0000269|PubMed:25533962" FT /id="VAR_073721" FT VARIANT 138 FT /note="S -> C (found in a patient with intellectual FT disability)" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069403" FT VARIANT 243 FT /note="G -> R (in MRD34; associated with authism and FT epilepsy)" FT /evidence="ECO:0000269|PubMed:25356899" FT /id="VAR_078652" FT VARIANT 599 FT /note="K -> R (in dbSNP:rs55882089)" FT /id="VAR_061815" FT MUTAGEN 132 FT /note="S->A: Abolishes the phosphorylation. Strongly FT reduces the interaction with phosphatidylinositol FT 4-phosphate. Increases the ceramide transfer activity." FT /evidence="ECO:0000269|PubMed:17591919" FT MUTAGEN 324 FT /note="D->A: Impairs the endoplasmic reticulum-to-Golgi FT ceramide trafficking and abolishes the interaction with FT VAPA and MOSPD2." FT /evidence="ECO:0000269|PubMed:16895911, FT ECO:0000269|PubMed:29858488" FT MUTAGEN 472 FT /note="E->A: Reduces ceramide transfer." FT /evidence="ECO:0000269|PubMed:18184806" FT MUTAGEN 493 FT /note="Q->A: No effect on ceramide transfer activity." FT /evidence="ECO:0000269|PubMed:18184806" FT MUTAGEN 499 FT /note="W->A: Reduces affinity for membranes. Abolishes FT ceramide transfer; when associated with A-588." FT /evidence="ECO:0000269|PubMed:20036255" FT MUTAGEN 530 FT /note="N->A: Reduces ceramide transfer." FT /evidence="ECO:0000269|PubMed:18184806" FT MUTAGEN 588 FT /note="W->A: Abolishes ceramide transfer; when associated FT with A-499." FT STRAND 26..33 FT /evidence="ECO:0007829|PDB:4HHV" FT TURN 36..38 FT /evidence="ECO:0007829|PDB:4HHV" FT STRAND 40..48 FT /evidence="ECO:0007829|PDB:4HHV" FT STRAND 51..56 FT /evidence="ECO:0007829|PDB:4HHV" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:4HHV" FT STRAND 64..71 FT /evidence="ECO:0007829|PDB:4HHV" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:4HHV" FT STRAND 85..90 FT /evidence="ECO:0007829|PDB:4HHV" FT STRAND 93..98 FT /evidence="ECO:0007829|PDB:4HHV" FT HELIX 102..119 FT /evidence="ECO:0007829|PDB:4HHV" FT HELIX 397..407 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:2E3M" FT STRAND 418..424 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 427..432 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 444..451 FT /evidence="ECO:0007829|PDB:2E3N" FT HELIX 455..463 FT /evidence="ECO:0007829|PDB:2E3N" FT HELIX 465..467 FT /evidence="ECO:0007829|PDB:2E3N" FT HELIX 468..471 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 474..485 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 488..495 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 499..502 FT /evidence="ECO:0007829|PDB:3H3S" FT STRAND 504..515 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 518..522 FT /evidence="ECO:0007829|PDB:2E3O" FT STRAND 525..532 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 542..546 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 548..559 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 563..565 FT /evidence="ECO:0007829|PDB:3H3S" FT HELIX 570..572 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 573..584 FT /evidence="ECO:0007829|PDB:2E3N" FT HELIX 591..617 FT /evidence="ECO:0007829|PDB:2E3N" FT STRAND 618..620 FT /evidence="ECO:0007829|PDB:2E3Q" SQ SEQUENCE 624 AA; 70835 MW; A125162492AC5A0E CRC64; MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN ALSYYKSEDE TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ DPDHRQQWID AIEQHKTESG YGSESSLRRH GSMVSLVSGA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK YFDACADAVS KDELQRDKVV EDDEDDFPTT RSDGDFLHST NGNKEKLFPH VTPKGINGID FKGEAITFKA TTAGILATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP TSLPSGDAFS SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM VQNHMTYSLQ DVGGDANWQL VVEEGEMKVY RREVEENGIV LDPLKATHAV KGVTGHEVCN YFWNVDVRND WETTIENFHV VETLADNAII IYQTHKRVWP ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL NNRCVRAKIN VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR EYPKFLKRFT SYVQEKTAGK PILF //