ID CERS4_HUMAN Reviewed; 394 AA. AC Q9HA82; D6W665; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 27-MAR-2024, entry version 182. DE RecName: Full=Ceramide synthase 4 {ECO:0000303|PubMed:17977534}; DE Short=CerS4 {ECO:0000303|PubMed:17977534}; DE EC=2.3.1.- {ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:29632068}; DE AltName: Full=LAG1 longevity assurance homolog 4 {ECO:0000250|UniProtKB:Q9D6J1}; DE AltName: Full=Sphingosine N-acyltransferase CERS4 {ECO:0000305}; DE EC=2.3.1.24 {ECO:0000250|UniProtKB:Q9D6J1}; GN Name=CERS4 {ECO:0000303|PubMed:17977534, ECO:0000312|HGNC:HGNC:23747}; GN Synonyms=LASS4 {ECO:0000250|UniProtKB:Q9D6J1}; 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 [LARGE SCALE MRNA], AND VARIANTS VAL-353 AND GLN-379. RC TISSUE=Embryo; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-366. 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-353 AND GLN-379. RC TISSUE=Lung; 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 [5] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=17977534; DOI=10.1016/j.febslet.2007.10.018; RA Lahiri S., Lee H., Mesicek J., Fuks Z., Haimovitz-Friedman A., RA Kolesnick R.N., Futerman A.H.; RT "Kinetic characterization of mammalian ceramide synthases: determination of RT K(m) values towards sphinganine."; RL FEBS Lett. 581:5289-5294(2007). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=23530041; DOI=10.1074/jbc.m112.428185; RA Russo S.B., Tidhar R., Futerman A.H., Cowart L.A.; RT "Myristate-derived d16:0 sphingolipids constitute a cardiac sphingolipid RT pool with distinct synthetic routes and functional properties."; RL J. Biol. Chem. 288:13397-13409(2013). RN [7] 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 [8] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, PHOSPHORYLATION, GLYCOSYLATION, RP TOPOLOGY, AND MUTAGENESIS OF 342-SER--SER-350. RX PubMed=26887952; DOI=10.1074/jbc.m115.695858; RA Sassa T., Hirayama T., Kihara A.; RT "Enzyme activities of the ceramide synthases CERS2-6 are regulated by RT phosphorylation in the C-terminal region."; RL J. Biol. Chem. 291:7477-7487(2016). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, GLYCOSYLATION, AND MUTAGENESIS OF RP 291-GLU--GLY-301. RX PubMed=29632068; DOI=10.1074/jbc.ra118.001936; RA Tidhar R., Zelnik I.D., Volpert G., Ben-Dor S., Kelly S., Merrill A.H. Jr., RA Futerman A.H.; RT "Eleven residues determine the acyl chain specificity of ceramide RT synthases."; RL J. Biol. Chem. 293:9912-9921(2018). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=31916624; DOI=10.1096/fj.201902645r; RA Jojima K., Edagawa M., Sawai M., Ohno Y., Kihara A.; RT "Biosynthesis of the anti-lipid-microdomain sphingoid base 4,14- RT sphingadiene by the ceramide desaturase FADS3."; RL FASEB J. 34:3318-3335(2020). CC -!- FUNCTION: Ceramide synthase that catalyzes formation of ceramide from CC sphinganine and acyl-CoA substrates, with high selectivity toward long CC and very-long chains (C18:0-C22:0) as acyl donor. CC {ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:23530041, CC ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:29632068, CC ECO:0000269|PubMed:31916624}. CC -!- CATALYTIC ACTIVITY: CC Reaction=octadecanoyl-CoA + sphinganine = CoA + H(+) + N- CC (octadecanoyl)-sphinganine; Xref=Rhea:RHEA:36547, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57817, CC ChEBI:CHEBI:67033; Evidence={ECO:0000269|PubMed:17977534, CC ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:29632068, CC ECO:0000269|PubMed:31916624}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36548; CC Evidence={ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:23530041, CC ECO:0000269|PubMed:29632068, ECO:0000269|PubMed:31916624}; CC -!- CATALYTIC ACTIVITY: CC Reaction=eicosanoyl-CoA + sphinganine = CoA + H(+) + N- CC eicosanoylsphinganine; Xref=Rhea:RHEA:36555, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:57817, CC ChEBI:CHEBI:67027; Evidence={ECO:0000269|PubMed:17977534, CC ECO:0000269|PubMed:26887952}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36556; CC Evidence={ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:26887952}; CC -!- CATALYTIC ACTIVITY: CC Reaction=docosanoyl-CoA + sphinganine = CoA + H(+) + N- CC docosanoylsphinganine; Xref=Rhea:RHEA:36535, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, ChEBI:CHEBI:65059, CC ChEBI:CHEBI:67021; Evidence={ECO:0000250|UniProtKB:Q9D6J1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36536; CC Evidence={ECO:0000250|UniProtKB:Q9D6J1}; CC -!- CATALYTIC ACTIVITY: CC Reaction=sphinganine + tetracosanoyl-CoA = CoA + H(+) + N- CC tetracosanoylsphinganine; Xref=Rhea:RHEA:33591, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:52961, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, CC ChEBI:CHEBI:65052; Evidence={ECO:0000269|PubMed:31916624}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33592; CC Evidence={ECO:0000269|PubMed:31916624}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexacosanoyl-CoA + sphinganine = CoA + H(+) + N- CC hexacosanoylsphinganine; Xref=Rhea:RHEA:33351, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:52962, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, CC ChEBI:CHEBI:64868; Evidence={ECO:0000250|UniProtKB:Q9D6J1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33352; CC Evidence={ECO:0000250|UniProtKB:Q9D6J1}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acyl-CoA + sphing-4-enine = an N-acylsphing-4-enine + CC CoA + H(+); Xref=Rhea:RHEA:23768, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57287, ChEBI:CHEBI:57756, CC ChEBI:CHEBI:77636; EC=2.3.1.24; CC Evidence={ECO:0000250|UniProtKB:Q9D6J1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23769; CC Evidence={ECO:0000250|UniProtKB:Q9D6J1}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octadecanoyl-CoA + sphing-4-enine = CoA + H(+) + N- CC octadecanoylsphing-4-enine; Xref=Rhea:RHEA:36691, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57756, CC ChEBI:CHEBI:72961; Evidence={ECO:0000250|UniProtKB:Q9D6J1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36692; CC Evidence={ECO:0000250|UniProtKB:Q9D6J1}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecasphinganine + octadecanoyl-CoA = CoA + H(+) + N- CC octadecanoylhexadecasphinganine; Xref=Rhea:RHEA:43044, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, CC ChEBI:CHEBI:71009, ChEBI:CHEBI:82811; CC Evidence={ECO:0000269|PubMed:23530041}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43045; CC Evidence={ECO:0000269|PubMed:23530041}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.8 uM for sphinganine (with octadecanoyl-CoA as substrate) CC {ECO:0000269|PubMed:17977534}; CC KM=1.8 uM for sphinganine (with eicosanoyl-CoA as substrate) CC {ECO:0000269|PubMed:17977534}; CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC {ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:23530041, CC ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:29632068}. CC -!- INTERACTION: CC Q9HA82; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-2622997, EBI-12062109; CC Q9HA82; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-2622997, EBI-10271156; CC Q9HA82; Q8NC01: CLEC1A; NbExp=3; IntAct=EBI-2622997, EBI-11996768; CC Q9HA82; P29400-2: COL4A5; NbExp=3; IntAct=EBI-2622997, EBI-12211159; CC Q9HA82; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-2622997, EBI-12019274; CC Q9HA82; P00387: CYB5R3; NbExp=3; IntAct=EBI-2622997, EBI-1046040; CC Q9HA82; P50402: EMD; NbExp=3; IntAct=EBI-2622997, EBI-489887; CC Q9HA82; Q969F0: FATE1; NbExp=3; IntAct=EBI-2622997, EBI-743099; CC Q9HA82; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-2622997, EBI-713304; CC Q9HA82; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-2622997, EBI-11955647; CC Q9HA82; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-2622997, EBI-725665; CC Q9HA82; P24593: IGFBP5; NbExp=3; IntAct=EBI-2622997, EBI-720480; CC Q9HA82; P11215: ITGAM; NbExp=3; IntAct=EBI-2622997, EBI-2568251; CC Q9HA82; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2622997, EBI-10266796; CC Q9HA82; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-2622997, EBI-2820517; CC Q9HA82; P11836: MS4A1; NbExp=3; IntAct=EBI-2622997, EBI-2808234; CC Q9HA82; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-2622997, EBI-2863634; CC Q9HA82; Q99519: NEU1; NbExp=3; IntAct=EBI-2622997, EBI-721517; CC Q9HA82; Q04941: PLP2; NbExp=3; IntAct=EBI-2622997, EBI-608347; CC Q9HA82; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-2622997, EBI-8652812; CC Q9HA82; P43378: PTPN9; NbExp=3; IntAct=EBI-2622997, EBI-742898; CC Q9HA82; Q8TAC9: SCAMP5; NbExp=3; IntAct=EBI-2622997, EBI-2695784; CC Q9HA82; O00767: SCD; NbExp=3; IntAct=EBI-2622997, EBI-2684237; CC Q9HA82; O75920: SERF1B; NbExp=3; IntAct=EBI-2622997, EBI-2115181; CC Q9HA82; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-2622997, EBI-749270; CC Q9HA82; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-2622997, EBI-12808018; CC Q9HA82; P78382: SLC35A1; NbExp=3; IntAct=EBI-2622997, EBI-12870360; CC Q9HA82; Q8N357: SLC35F6; NbExp=3; IntAct=EBI-2622997, EBI-713484; CC Q9HA82; P30825: SLC7A1; NbExp=3; IntAct=EBI-2622997, EBI-4289564; CC Q9HA82; P58511: SMIM11; NbExp=3; IntAct=EBI-2622997, EBI-1051936; CC Q9HA82; O15400: STX7; NbExp=3; IntAct=EBI-2622997, EBI-3221827; CC Q9HA82; Q9UNK0: STX8; NbExp=3; IntAct=EBI-2622997, EBI-727240; CC Q9HA82; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-2622997, EBI-10329860; CC Q9HA82; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-2622997, EBI-2800645; CC Q9HA82; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-2622997, EBI-11956809; CC Q9HA82; A0PK05: TMEM72; NbExp=3; IntAct=EBI-2622997, EBI-12878352; CC Q9HA82; Q96B49: TOMM6; NbExp=3; IntAct=EBI-2622997, EBI-10826510; CC Q9HA82; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-2622997, EBI-12195249; CC Q9HA82; O75841: UPK1B; NbExp=3; IntAct=EBI-2622997, EBI-12237619; CC Q9HA82; P63027: VAMP2; NbExp=3; IntAct=EBI-2622997, EBI-520113; CC Q9HA82; Q96FB2; NbExp=3; IntAct=EBI-2622997, EBI-2857623; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9D6J1}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- DOMAIN: The last loop motif confers selectivity toward stearoyl-CoA CC (octadecanoyl-CoA; C18:0-CoA) to behenoyl-CoA (docosanoyl-CoA; C22:0- CC CoA) as acyl donors. {ECO:0000269|PubMed:29632068}. CC -!- PTM: Phosphorylated at the C-terminus by CK2. CC {ECO:0000269|PubMed:26887952}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:26887952, CC ECO:0000269|PubMed:29632068}. CC -!- CAUTION: Some prediction bioinformatics tools predict the presence of a CC homeobox domain (By similarity). However, the domain is degenerate and CC residues that are important for DNA-binding are absent (By similarity). CC {ECO:0000255}. 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; AK022151; BAB13972.1; -; mRNA. DR EMBL; AC022146; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471139; EAW68940.1; -; Genomic_DNA. DR EMBL; CH471139; EAW68941.1; -; Genomic_DNA. DR EMBL; CH471139; EAW68942.1; -; Genomic_DNA. DR EMBL; CH471139; EAW68945.1; -; Genomic_DNA. DR EMBL; BC009828; AAH09828.1; -; mRNA. DR CCDS; CCDS12197.1; -. DR RefSeq; NP_078828.2; NM_024552.2. DR RefSeq; XP_011526592.1; XM_011528290.2. DR RefSeq; XP_011526593.1; XM_011528291.2. DR RefSeq; XP_011526594.1; XM_011528292.2. DR RefSeq; XP_011526595.1; XM_011528293.2. DR RefSeq; XP_011526596.1; XM_011528294.2. DR RefSeq; XP_011526597.1; XM_011528295.2. DR RefSeq; XP_016882792.1; XM_017027303.1. DR RefSeq; XP_016882793.1; XM_017027304.1. DR RefSeq; XP_016882794.1; XM_017027305.1. DR AlphaFoldDB; Q9HA82; -. DR SMR; Q9HA82; -. DR BioGRID; 122740; 73. DR IntAct; Q9HA82; 45. DR STRING; 9606.ENSP00000251363; -. DR SwissLipids; SLP:000000699; -. DR GlyConnect; 1106; 3 N-Linked glycans (1 site). DR GlyCosmos; Q9HA82; 1 site, 3 glycans. DR GlyGen; Q9HA82; 1 site, 3 N-linked glycans (1 site). DR iPTMnet; Q9HA82; -. DR PhosphoSitePlus; Q9HA82; -. DR SwissPalm; Q9HA82; -. DR BioMuta; CERS4; -. DR DMDM; 296434561; -. DR EPD; Q9HA82; -. DR jPOST; Q9HA82; -. DR MassIVE; Q9HA82; -. DR MaxQB; Q9HA82; -. DR PaxDb; 9606-ENSP00000251363; -. DR PeptideAtlas; Q9HA82; -. DR ProteomicsDB; 81384; -. DR Pumba; Q9HA82; -. DR Antibodypedia; 24821; 325 antibodies from 30 providers. DR DNASU; 79603; -. DR Ensembl; ENST00000251363.10; ENSP00000251363.5; ENSG00000090661.12. DR Ensembl; ENST00000559450.5; ENSP00000453509.1; ENSG00000090661.12. DR GeneID; 79603; -. DR KEGG; hsa:79603; -. DR MANE-Select; ENST00000251363.10; ENSP00000251363.5; NM_024552.3; NP_078828.2. DR UCSC; uc002mjg.4; human. DR AGR; HGNC:23747; -. DR CTD; 79603; -. DR DisGeNET; 79603; -. DR GeneCards; CERS4; -. DR HGNC; HGNC:23747; CERS4. DR HPA; ENSG00000090661; Low tissue specificity. DR MIM; 615334; gene. DR neXtProt; NX_Q9HA82; -. DR OpenTargets; ENSG00000090661; -. DR PharmGKB; PA134915173; -. DR VEuPathDB; HostDB:ENSG00000090661; -. DR eggNOG; KOG1607; Eukaryota. DR GeneTree; ENSGT01030000234515; -. DR InParanoid; Q9HA82; -. DR OMA; MYWWYLL; -. DR OrthoDB; 460400at2759; -. DR PhylomeDB; Q9HA82; -. DR TreeFam; TF314319; -. DR BioCyc; MetaCyc:ENSG00000090661-MONOMER; -. DR BRENDA; 2.3.1.24; 2681. DR BRENDA; 2.3.1.291; 2681. DR BRENDA; 2.3.1.297; 2681. DR PathwayCommons; Q9HA82; -. DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis. DR SignaLink; Q9HA82; -. DR UniPathway; UPA00222; -. DR BioGRID-ORCS; 79603; 31 hits in 1173 CRISPR screens. DR ChiTaRS; CERS4; human. DR GenomeRNAi; 79603; -. DR Pharos; Q9HA82; Tbio. DR PRO; PR:Q9HA82; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9HA82; Protein. DR Bgee; ENSG00000090661; Expressed in lower esophagus mucosa and 117 other cell types or tissues. DR ExpressionAtlas; Q9HA82; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IDA:UniProtKB. DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB. DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome. DR CDD; cd00086; homeodomain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR016439; Lag1/Lac1-like. DR InterPro; IPR006634; TLC-dom. DR PANTHER; PTHR12560:SF6; CERAMIDE SYNTHASE 4; 1. DR PANTHER; PTHR12560; LONGEVITY ASSURANCE FACTOR 1 LAG1; 1. DR Pfam; PF00046; Homeodomain; 1. DR Pfam; PF03798; TRAM_LAG1_CLN8; 1. DR PIRSF; PIRSF005225; LAG1_LAC1; 1. DR SMART; SM00724; TLC; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS50922; TLC; 1. DR Genevisible; Q9HA82; HS. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism; KW Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..394 FT /note="Ceramide synthase 4" FT /id="PRO_0000185512" FT TOPO_DOM 1..31 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:29632068" FT TRANSMEM 32..52 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 140..160 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 179..199 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 209..229 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 260..280 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 304..324 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 325..394 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:26887952" FT DOMAIN 131..332 FT /note="TLC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205" FT REGION 67..128 FT /note="Homeobox-like" FT /evidence="ECO:0000305" FT REGION 341..394 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 291..301 FT /note="Last loop motif" FT /evidence="ECO:0000269|PubMed:29632068" FT MOD_RES 342 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D6J1" FT MOD_RES 349 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D6J1" FT MOD_RES 350 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D6J1" FT CARBOHYD 19 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 119 FT /note="R -> Q (in dbSNP:rs17159388)" FT /id="VAR_034065" FT VARIANT 301 FT /note="G -> S (in dbSNP:rs2288413)" FT /id="VAR_019556" FT VARIANT 353 FT /note="A -> V (in dbSNP:rs17160348)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_060263" FT VARIANT 366 FT /note="A -> T (in dbSNP:rs36259)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_019557" FT VARIANT 379 FT /note="R -> Q (in dbSNP:rs17160349)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_060264" FT MUTAGEN 291..298 FT /note="ESISNRGP->YPLELYPA: Altered specificity toward acyl FT donor; generates C24 ceramides instead of FT C18-C22-ceramides." FT /evidence="ECO:0000269|PubMed:29632068" FT MUTAGEN 342..350 FT /note="SDVEESDSS->ADVEEADAA: Decreased phosphorylation." FT /evidence="ECO:0000269|PubMed:26887952" SQ SEQUENCE 394 AA; 46399 MW; DAA12AA386ED2802 CRC64; MLSSFNEWFW QDRFWLPPNV TWTELEDRDG RVYPHPQDLL AALPLALVLL AMRLAFERFI GLPLSRWLGV RDQTRRQVKP NATLEKHFLT EGHRPKEPQL SLLAAQCGLT LQQTQRWFRR RRNQDRPQLT KKFCEASWRF LFYLSSFVGG LSVLYHESWL WAPVMCWDRY PNQTLKPSLY WWYLLELGFY LSLLIRLPFD VKRKDFKEQV IHHFVAVILM TFSYSANLLR IGSLVLLLHD SSDYLLEACK MVNYMQYQQV CDALFLIFSF VFFYTRLVLF PTQILYTTYY ESISNRGPFF GYYFFNGLLM LLQLLHVFWS CLILRMLYSF MKKGQMEKDI RSDVEESDSS EEAAAAQEPL QLKNGAAGGP RPAPTDGPRS RVAGRLTNRH TTAT //