CERS5_MOUSE
ID CERS5_MOUSE Reviewed; 414 AA.
AC Q9D6K9; Q3UL17; Q80YB2; Q8BPH6; Q921T8; Q924Z3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ceramide synthase 5 {ECO:0000305};
DE Short=CerS5 {ECO:0000305};
DE AltName: Full=LAG1 longevity assurance homolog 5 {ECO:0000303|PubMed:16100120};
DE AltName: Full=Sphingoid base N-palmitoyltransferase CERS5 {ECO:0000305};
DE EC=2.3.1.291 {ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15772421, ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:17977534};
DE AltName: Full=Sphingosine N-acyltransferase CERS5 {ECO:0000305};
DE EC=2.3.1.24 {ECO:0000269|PubMed:12912983};
DE AltName: Full=Translocating chain-associating membrane protein homolog 4 {ECO:0000303|PubMed:12912983};
DE Short=TRAM homolog 4 {ECO:0000303|PubMed:12912983};
GN Name=Cers5 {ECO:0000312|MGI:MGI:1919199};
GN Synonyms=Lass5 {ECO:0000303|PubMed:16100120},
GN Trh4 {ECO:0000303|PubMed:12912983};
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 [MRNA] (ISOFORM 1).
RA Hartmann E.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and 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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12912983; DOI=10.1074/jbc.m307104200;
RA Riebeling C., Allegood J.C., Wang E., Merrill A.H. Jr., Futerman A.H.;
RT "Two mammalian longevity assurance gene (LAG1) family members, trh1 and
RT trh4, regulate dihydroceramide synthesis using different fatty acyl-CoA
RT donors.";
RL J. Biol. Chem. 278:43452-43459(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, GLYCOSYLATION AT ASN-26, AND TISSUE
RP SPECIFICITY.
RX PubMed=15823095; DOI=10.1042/bj20050291;
RA Mizutani Y., Kihara A., Igarashi Y.;
RT "Mammalian Lass6 and its related family members regulate synthesis of
RT specific ceramides.";
RL Biochem. J. 390:263-271(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND ACTIVITY REGULATION.
RX PubMed=16100120; DOI=10.1074/jbc.m506485200;
RA Lahiri S., Futerman A.H.;
RT "LASS5 is a bona fide dihydroceramide synthase that selectively utilizes
RT palmitoyl-CoA as acyl donor.";
RL J. Biol. Chem. 280:33735-33738(2005).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15772421; DOI=10.1194/jlr.m500001-jlr200;
RA Xu Z., Zhou J., McCoy D.M., Mallampalli R.K.;
RT "LASS5 is the predominant ceramide synthase isoform involved in de novo
RT sphingolipid synthesis in lung epithelia.";
RL J. Lipid Res. 46:1229-1238(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [9]
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF 129-ARG--LYS-140; LYS-134; 136-PRO--LYS-140 AND LYS-140.
RX PubMed=17609214; DOI=10.1074/jbc.m703487200;
RA Mesika A., Ben-Dor S., Laviad E.L., Futerman A.H.;
RT "A new functional motif in Hox domain-containing ceramide synthases:
RT identification of a novel region flanking the Hox and TLC domains essential
RT for activity.";
RL J. Biol. Chem. 282:27366-27373(2007).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26853464; DOI=10.1074/jbc.m115.691212;
RA Gosejacob D., Jaeger P.S., Vom Dorp K., Frejno M., Carstensen A.C.,
RA Koehnke M., Degen J., Doermann P., Hoch M.;
RT "Ceramide Synthase 5 is essential to maintain C16:0-ceramide pools and
RT contributes to the development of diet-induced obesity.";
RL J. Biol. Chem. 291:6989-7003(2016).
RN [12]
RP CAUTION.
RX PubMed=31150623; DOI=10.1016/j.cell.2019.05.008;
RA Hammerschmidt P., Ostkotte D., Nolte H., Gerl M.J., Jais A., Brunner H.L.,
RA Sprenger H.G., Awazawa M., Nicholls H.T., Turpin-Nolan S.M., Langer T.,
RA Krueger M., Bruegger B., Bruening J.C.;
RT "CerS6-derived sphingolipids interact with Mff and promote mitochondrial
RT fragmentation in obesity.";
RL Cell 177:1536-1552(2019).
RN [13]
RP STRUCTURE BY NMR OF 77-135.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-034, a homeodomain from mouse cDNA.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Ceramide synthase that catalyzes the transfer of the acyl
CC chain from acyl-CoA to a sphingoid base, with high selectivity toward
CC palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:12912983,
CC PubMed:15823095, PubMed:16100120, PubMed:17977534, PubMed:17609214,
CC PubMed:26853464). Can use other acyl donors, but with less efficiency
CC (PubMed:15823095). N-acylates sphinganine and sphingosine bases to form
CC dihydroceramides and ceramides in de novo synthesis and salvage
CC pathways, respectively (PubMed:12912983, PubMed:15823095,
CC PubMed:15772421, PubMed:17977534). Plays a role in de novo ceramide
CC synthesis and surfactant homeostasis in pulmonary epithelia
CC (PubMed:15772421). {ECO:0000269|PubMed:12912983,
CC ECO:0000269|PubMed:15772421, ECO:0000269|PubMed:15823095,
CC ECO:0000269|PubMed:16100120, ECO:0000269|PubMed:17609214,
CC ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:26853464}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingoid base + hexadecanoyl-CoA = an N-hexadecanoyl-
CC sphingoid base + CoA + H(+); Xref=Rhea:RHEA:61472, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:84410,
CC ChEBI:CHEBI:144703; EC=2.3.1.291;
CC Evidence={ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15772421,
CC ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:17977534};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61473;
CC Evidence={ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15772421,
CC ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:17977534};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphinganine = CoA + H(+) + N-
CC hexadecanoylsphinganine; Xref=Rhea:RHEA:36539, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67042; Evidence={ECO:0000269|PubMed:12912983,
CC ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:17977534};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36540;
CC Evidence={ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15823095,
CC ECO:0000269|PubMed:17977534};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + hexadecasphinganine = CoA + H(+) + N-
CC hexadecanoylhexadecasphinganine; Xref=Rhea:RHEA:43040,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:71009, ChEBI:CHEBI:82810;
CC Evidence={ECO:0000250|UniProtKB:Q8N5B7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43041;
CC Evidence={ECO:0000250|UniProtKB:Q8N5B7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphing-4-enine = CoA + H(+) + N-
CC hexadecanoylsphing-4-enine; Xref=Rhea:RHEA:36687, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:72959; Evidence={ECO:0000269|PubMed:12912983};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36688;
CC Evidence={ECO:0000269|PubMed:12912983};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyhexadecanoyl-CoA + sphinganine = CoA + H(+) + N-(2-
CC hydroxyhexadecanoyl)-sphinganine; Xref=Rhea:RHEA:36647,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67043, ChEBI:CHEBI:74115;
CC Evidence={ECO:0000250|UniProtKB:Q8N5B7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36648;
CC Evidence={ECO:0000250|UniProtKB:Q8N5B7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinganine + tetradecanoyl-CoA = CoA + H(+) + N-
CC (tetradecanoyl)-sphinganine; Xref=Rhea:RHEA:36571, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67045; Evidence={ECO:0000269|PubMed:15823095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36572;
CC Evidence={ECO:0000269|PubMed:15823095};
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:12912983,
CC ECO:0000269|PubMed:15823095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36548;
CC Evidence={ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15823095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sphinganine = CoA + H(+) + N-(9Z-
CC octadecenoyl)-sphinganine; Xref=Rhea:RHEA:36575, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:74100; Evidence={ECO:0000269|PubMed:15823095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36576;
CC Evidence={ECO:0000269|PubMed:15823095};
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:0000269|PubMed:12912983};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23769;
CC Evidence={ECO:0000269|PubMed:12912983};
CC -!- ACTIVITY REGULATION: Inhibited by fumonisin B1.
CC {ECO:0000269|PubMed:16100120}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for sphinganine {ECO:0000269|PubMed:17977534};
CC KM=3.6 uM for sphinganine {ECO:0000269|PubMed:17609214};
CC Vmax=215 pmol/min/mg enzyme with sphinganine as substrate
CC {ECO:0000269|PubMed:17609214};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15823095,
CC ECO:0000269|PubMed:16100120, ECO:0000269|PubMed:17609214,
CC ECO:0000269|PubMed:17977534}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12912983}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D6K9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D6K9-2; Sequence=VSP_011192, VSP_011193;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC testis and kidney (PubMed:12912983, PubMed:15823095). Expressed in
CC pulmonary epithelia (PubMed:15772421). {ECO:0000269|PubMed:12912983,
CC ECO:0000269|PubMed:15772421, ECO:0000269|PubMed:15823095}.
CC -!- DEVELOPMENTAL STAGE: Expressed in lungs of 15 days old fetuses followed
CC by a modest peak at day 17, thereafter decreasing in adult lungs.
CC {ECO:0000269|PubMed:15772421}.
CC -!- DOMAIN: The last loop motif confers selectivity toward palmitoyl-CoA
CC (hexadecanoyl-CoA; C16:0-CoA) as acyl donor.
CC {ECO:0000250|UniProtKB:Q8N5B7}.
CC -!- PTM: Phosphorylated at the C-terminus by CK2.
CC {ECO:0000250|UniProtKB:Q8N5B7}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and show no apparent
CC morphological alterations in normal conditions (PubMed:26853464).
CC Decreased palmitoyl (C16:0) ceramide pools (PubMed:26853464).
CC {ECO:0000269|PubMed:26853464}.
CC -!- CAUTION: According to a report, deletion of Cers5 protects from
CC obesity: knockout mice are associated with reduced weight gain and
CC improved systemic health after high fat diet challenge
CC (PubMed:26853464). This result was however not confirmed by another
CC study, which did not observe any protection from diet-induced obesity
CC in knockout mice (PubMed:31150623). Effects observed in the first study
CC might be indirect and caused by a large deletion that affects
CC neighboring genes and/or deletes non-coding RNAs (PubMed:26853464,
CC PubMed:31150623). {ECO:0000269|PubMed:26853464,
CC ECO:0000269|PubMed:31150623}.
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 Moreover, the protein localizes in the endoplasmic reticulum and not in
CC the nucleus, strongly suggesting that it does not constitute a
CC canonical homeobox domain (PubMed:12912983). {ECO:0000255,
CC ECO:0000269|PubMed:12912983}.
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DR EMBL; AY029533; AAK40301.1; -; mRNA.
DR EMBL; AK010241; BAB26792.1; -; mRNA.
DR EMBL; AK075694; BAC35894.1; -; mRNA.
DR EMBL; AK145589; BAE26527.1; -; mRNA.
DR EMBL; AK145762; BAE26634.1; -; mRNA.
DR EMBL; BC010670; AAH10670.1; -; mRNA.
DR EMBL; BC043059; AAH43059.1; -; mRNA.
DR EMBL; BC046797; AAH46797.1; -; mRNA.
DR CCDS; CCDS27830.1; -. [Q9D6K9-1]
DR RefSeq; NP_082291.1; NM_028015.2. [Q9D6K9-1]
DR PDB; 2CQX; NMR; -; A=77-135.
DR PDB; 5E8N; X-ray; 2.25 A; C/F/I/L=379-387.
DR PDB; 5E8O; X-ray; 1.98 A; C/F=379-387.
DR PDB; 5E8P; X-ray; 2.00 A; C/F=379-387.
DR PDBsum; 2CQX; -.
DR PDBsum; 5E8N; -.
DR PDBsum; 5E8O; -.
DR PDBsum; 5E8P; -.
DR AlphaFoldDB; Q9D6K9; -.
DR SMR; Q9D6K9; -.
DR BioGRID; 215049; 5.
DR IntAct; Q9D6K9; 3.
DR STRING; 10090.ENSMUSP00000023762; -.
DR SwissLipids; SLP:000000118; -.
DR GlyGen; Q9D6K9; 1 site.
DR iPTMnet; Q9D6K9; -.
DR PhosphoSitePlus; Q9D6K9; -.
DR SwissPalm; Q9D6K9; -.
DR EPD; Q9D6K9; -.
DR MaxQB; Q9D6K9; -.
DR PaxDb; Q9D6K9; -.
DR PeptideAtlas; Q9D6K9; -.
DR PRIDE; Q9D6K9; -.
DR ProteomicsDB; 281590; -. [Q9D6K9-1]
DR ProteomicsDB; 281591; -. [Q9D6K9-2]
DR Antibodypedia; 14183; 219 antibodies from 30 providers.
DR DNASU; 71949; -.
DR Ensembl; ENSMUST00000023762; ENSMUSP00000023762; ENSMUSG00000023021. [Q9D6K9-1]
DR Ensembl; ENSMUST00000109035; ENSMUSP00000104663; ENSMUSG00000023021. [Q9D6K9-2]
DR GeneID; 71949; -.
DR KEGG; mmu:71949; -.
DR UCSC; uc007xqf.1; mouse. [Q9D6K9-1]
DR UCSC; uc007xqg.1; mouse. [Q9D6K9-2]
DR CTD; 91012; -.
DR MGI; MGI:1919199; Cers5.
DR VEuPathDB; HostDB:ENSMUSG00000023021; -.
DR eggNOG; KOG1607; Eukaryota.
DR GeneTree; ENSGT01030000234515; -.
DR HOGENOM; CLU_028277_1_1_1; -.
DR InParanoid; Q9D6K9; -.
DR OMA; TDMTERQ; -.
DR OrthoDB; 987268at2759; -.
DR PhylomeDB; Q9D6K9; -.
DR TreeFam; TF314319; -.
DR BRENDA; 2.3.1.24; 3474.
DR BRENDA; 2.3.1.291; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 71949; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Cers5; mouse.
DR EvolutionaryTrace; Q9D6K9; -.
DR PRO; PR:Q9D6K9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D6K9; protein.
DR Bgee; ENSMUSG00000023021; Expressed in tail skin and 261 other tissues.
DR ExpressionAtlas; Q9D6K9; baseline and differential.
DR Genevisible; Q9D6K9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
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; IDA:MGI.
DR CDD; cd00086; homeodomain; 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; PTHR12560; 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; SSF46689; 1.
DR PROSITE; PS50922; TLC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..414
FT /note="Ceramide synthase 5"
FT /id="PRO_0000185515"
FT TOPO_DOM 1..43
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:15823095"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8N5B7"
FT DOMAIN 139..340
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 75..136
FT /note="Homeobox-like"
FT /evidence="ECO:0000305"
FT REGION 347..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 299..309
FT /note="Last loop motif"
FT /evidence="ECO:0000250|UniProtKB:Q8N5B7"
FT COMPBIAS 347..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15823095"
FT VAR_SEQ 345..387
FT /note="SKDDRSDVESSSEEEDETTHKNNLSGSSSSNGANCMNGYMGGS -> LSQEG
FT LDPGSVPSALSHLLPLFSAWWQLDSSILCMCLRMTAVM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011192"
FT VAR_SEQ 388..414
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011193"
FT MUTAGEN 129..140
FT /note="Missing: Abolished ceramide synthase activity."
FT /evidence="ECO:0000269|PubMed:17609214"
FT MUTAGEN 134
FT /note="K->A: Abolished ceramide synthase activity."
FT /evidence="ECO:0000269|PubMed:17609214"
FT MUTAGEN 134
FT /note="K->R: Does not affect ceramide synthase activity."
FT /evidence="ECO:0000269|PubMed:17609214"
FT MUTAGEN 136..140
FT /note="Missing: Abolished ceramide synthase activity."
FT /evidence="ECO:0000269|PubMed:17609214"
FT MUTAGEN 140
FT /note="K->A: Abolished ceramide synthase activity."
FT /evidence="ECO:0000269|PubMed:17609214"
FT MUTAGEN 140
FT /note="K->R: Does not affect ceramide synthase activity."
FT /evidence="ECO:0000269|PubMed:17609214"
FT CONFLICT 82
FT /note="P -> A (in Ref. 1; AAK40301)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="W -> R (in Ref. 2; BAC35894)"
FT /evidence="ECO:0000305"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:2CQX"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:2CQX"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:2CQX"
SQ SEQUENCE 414 AA; 48167 MW; E3536F344A459D49 CRC64;
MATAAAETLG LLWGWLWSES FWLPQNVSWA DLEGPGDGYG YPRAQHVLSV FPLAVCIFSV
RMLFERFIAK PCALRVGIKD SPVNKVEPND TLEKVFVSVT KYPDEKRLKG LSKQLDWSVR
KIQCWFRHRR NQDKPPTLTK FCESMWRFTY YLCIFCYGIR FLWSMPWFWD TRQCWYNYPY
QPLSRELYYY YITQLAFYWS LMFSQFIDVK RKDFLMMFIH HMIGIMLTTF SYVNNMVRVG
ALIFCLHDFA DPLLEAAKMA NYARRERLCT TLFVIFGAAF IVSRLAIFPL WILNTTLFES
WEIIGPYPSW WLFNALLLIL QVLHAIWSYL IVQTASKALS RGKVSKDDRS DVESSSEEED
ETTHKNNLSG SSSSNGANCM NGYMGGSHLA EEQGTCKATG NLHFRASPHL HSCD
