CERS5_HUMAN
ID CERS5_HUMAN Reviewed; 392 AA.
AC Q8N5B7; B4DV54;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ceramide synthase 5 {ECO:0000305};
DE Short=CerS5 {ECO:0000305};
DE AltName: Full=LAG1 longevity assurance homolog 5 {ECO:0000250|UniProtKB:Q9D6K9};
DE AltName: Full=Sphingoid base N-palmitoyltransferase CERS5 {ECO:0000305};
DE EC=2.3.1.291 {ECO:0000269|PubMed:16951403, ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:22144673, ECO:0000269|PubMed:22661289, ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:29632068};
DE AltName: Full=Sphingosine N-acyltransferase CERS5 {ECO:0000305};
DE EC=2.3.1.24 {ECO:0000250|UniProtKB:Q9D6K9};
GN Name=CERS5 {ECO:0000312|HGNC:HGNC:23749};
GN Synonyms=LASS5 {ECO:0000250|UniProtKB:Q9D6K9};
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] (ISOFORM 2).
RC TISSUE=Small intestine;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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, ACTIVITY REGULATION, PATHWAY, AND MUTAGENESIS
RP OF HIS-220; SER-231 AND LEU-254.
RX PubMed=16951403; DOI=10.1074/jbc.m608092200;
RA Spassieva S., Seo J.G., Jiang J.C., Bielawski J., Alvarez-Vasquez F.,
RA Jazwinski S.M., Hannun Y.A., Obeid L.M.;
RT "Necessary role for the Lag1p motif in (dihydro)ceramide synthase
RT activity.";
RL J. Biol. Chem. 281:33931-33938(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=18541923; DOI=10.1194/jlr.m800158-jlr200;
RA Mizutani Y., Kihara A., Chiba H., Tojo H., Igarashi Y.;
RT "2-Hydroxy-ceramide synthesis by ceramide synthase family: enzymatic basis
RT for the preference of FA chain length.";
RL J. Lipid Res. 49:2356-2364(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22144673; DOI=10.1074/jbc.m111.280271;
RA Tidhar R., Ben-Dor S., Wang E., Kelly S., Merrill A.H. Jr., Futerman A.H.;
RT "Acyl chain specificity of ceramide synthases is determined within a region
RT of 150 residues in the Tram-Lag-CLN8 (TLC) domain.";
RL J. Biol. Chem. 287:3197-3206(2012).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22661289; DOI=10.1194/jlr.d025627;
RA Kim H.J., Qiao Q., Toop H.D., Morris J.C., Don A.S.;
RT "A fluorescent assay for ceramide synthase activity.";
RL J. Lipid Res. 53:1701-1707(2012).
RN [9]
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, PHOSPHORYLATION, GLYCOSYLATION,
RP TOPOLOGY, AND MUTAGENESIS OF 350-SER--SER-356.
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TOPOLOGY, DOMAIN, GLYCOSYLATION AT
RP ASN-26, AND MUTAGENESIS OF ASN-26; 153-CYS--SER-165 AND 299-GLU--SER-309.
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 [12]
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 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:16951403,
CC PubMed:18541923, PubMed:22144673, PubMed:22661289, PubMed:23530041,
CC PubMed:26887952, PubMed:29632068, PubMed:31916624). Can use other acyl
CC donors, but with less efficiency (By similarity). N-acylates
CC sphinganine and sphingosine bases to form dihydroceramides and
CC ceramides in de novo synthesis and salvage pathways, respectively
CC (PubMed:31916624). Plays a role in de novo ceramide synthesis and
CC surfactant homeostasis in pulmonary epithelia (By similarity).
CC {ECO:0000250|UniProtKB:Q9D6K9, ECO:0000269|PubMed:16951403,
CC ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:22144673,
CC ECO:0000269|PubMed:22661289, ECO:0000269|PubMed:23530041,
CC ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:29632068,
CC ECO:0000269|PubMed:31916624}.
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:16951403, ECO:0000269|PubMed:18541923,
CC ECO:0000269|PubMed:22144673, ECO:0000269|PubMed:22661289,
CC ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952,
CC ECO:0000269|PubMed:29632068, ECO:0000269|PubMed:31916624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61473;
CC Evidence={ECO:0000269|PubMed:16951403, ECO:0000269|PubMed:18541923,
CC ECO:0000269|PubMed:22144673, ECO:0000269|PubMed:22661289,
CC ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952,
CC ECO:0000269|PubMed:29632068, ECO:0000269|PubMed:31916624};
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:16951403,
CC ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:22144673,
CC ECO:0000269|PubMed:22661289, ECO:0000269|PubMed:23530041,
CC ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:29632068,
CC ECO:0000269|PubMed:31916624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36540;
CC Evidence={ECO:0000269|PubMed:16951403, ECO:0000269|PubMed:18541923,
CC ECO:0000269|PubMed:22144673, ECO:0000269|PubMed:22661289,
CC ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952,
CC ECO:0000269|PubMed:29632068, ECO:0000269|PubMed:31916624};
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:0000269|PubMed:23530041};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43041;
CC Evidence={ECO:0000269|PubMed:23530041};
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:31916624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36688;
CC Evidence={ECO:0000269|PubMed:31916624};
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:0000269|PubMed:22144673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36648;
CC Evidence={ECO:0000269|PubMed:22144673};
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:0000250|UniProtKB:Q9D6K9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36572;
CC Evidence={ECO:0000250|UniProtKB:Q9D6K9};
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:0000250|UniProtKB:Q9D6K9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36548;
CC Evidence={ECO:0000250|UniProtKB:Q9D6K9};
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:0000250|UniProtKB:Q9D6K9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36576;
CC Evidence={ECO:0000250|UniProtKB:Q9D6K9};
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:Q9D6K9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23769;
CC Evidence={ECO:0000250|UniProtKB:Q9D6K9};
CC -!- ACTIVITY REGULATION: Inhibited by fumonisin B1.
CC {ECO:0000269|PubMed:16951403}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:22144673,
CC ECO:0000269|PubMed:22661289, ECO:0000269|PubMed:23530041,
CC ECO:0000269|PubMed:26887952}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9D6K9}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N5B7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5B7-2; Sequence=VSP_054572;
CC -!- DOMAIN: The last loop motif confers selectivity toward palmitoyl-CoA
CC (hexadecanoyl-CoA; C16:0-CoA) as acyl donor.
CC {ECO:0000269|PubMed:29632068}.
CC -!- PTM: Phosphorylated at the C-terminus by CK2.
CC {ECO:0000269|PubMed:26887952}.
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}.
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DR EMBL; AK300937; BAG62566.1; -; mRNA.
DR EMBL; AC074032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58133.1; -; Genomic_DNA.
DR EMBL; BC032565; AAH32565.1; -; mRNA.
DR CCDS; CCDS61120.1; -. [Q8N5B7-2]
DR CCDS; CCDS8801.1; -. [Q8N5B7-1]
DR RefSeq; NP_001268660.1; NM_001281731.1. [Q8N5B7-2]
DR RefSeq; NP_671723.1; NM_147190.3. [Q8N5B7-1]
DR AlphaFoldDB; Q8N5B7; -.
DR SMR; Q8N5B7; -.
DR BioGRID; 124788; 31.
DR IntAct; Q8N5B7; 8.
DR STRING; 9606.ENSP00000325485; -.
DR SwissLipids; SLP:000000261; -.
DR GlyGen; Q8N5B7; 1 site.
DR iPTMnet; Q8N5B7; -.
DR PhosphoSitePlus; Q8N5B7; -.
DR SwissPalm; Q8N5B7; -.
DR BioMuta; CERS5; -.
DR DMDM; 51316484; -.
DR EPD; Q8N5B7; -.
DR jPOST; Q8N5B7; -.
DR MassIVE; Q8N5B7; -.
DR MaxQB; Q8N5B7; -.
DR PaxDb; Q8N5B7; -.
DR PeptideAtlas; Q8N5B7; -.
DR PRIDE; Q8N5B7; -.
DR ProteomicsDB; 5243; -.
DR ProteomicsDB; 72028; -. [Q8N5B7-1]
DR Antibodypedia; 14183; 219 antibodies from 30 providers.
DR DNASU; 91012; -.
DR Ensembl; ENST00000317551.12; ENSP00000325485.6; ENSG00000139624.14. [Q8N5B7-1]
DR Ensembl; ENST00000422340.6; ENSP00000389050.2; ENSG00000139624.14. [Q8N5B7-2]
DR GeneID; 91012; -.
DR KEGG; hsa:91012; -.
DR MANE-Select; ENST00000317551.12; ENSP00000325485.6; NM_147190.5; NP_671723.1.
DR UCSC; uc001rwd.6; human. [Q8N5B7-1]
DR CTD; 91012; -.
DR DisGeNET; 91012; -.
DR GeneCards; CERS5; -.
DR HGNC; HGNC:23749; CERS5.
DR HPA; ENSG00000139624; Low tissue specificity.
DR MIM; 615335; gene.
DR neXtProt; NX_Q8N5B7; -.
DR OpenTargets; ENSG00000139624; -.
DR PharmGKB; PA134882694; -.
DR VEuPathDB; HostDB:ENSG00000139624; -.
DR eggNOG; KOG1607; Eukaryota.
DR GeneTree; ENSGT01030000234515; -.
DR HOGENOM; CLU_028277_1_2_1; -.
DR InParanoid; Q8N5B7; -.
DR OMA; TDMTERQ; -.
DR OrthoDB; 987268at2759; -.
DR PhylomeDB; Q8N5B7; -.
DR TreeFam; TF314319; -.
DR BioCyc; MetaCyc:ENSG00000139624-MON; -.
DR BRENDA; 2.3.1.24; 2681.
DR BRENDA; 2.3.1.291; 2681.
DR PathwayCommons; Q8N5B7; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; Q8N5B7; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 91012; 28 hits in 1104 CRISPR screens.
DR ChiTaRS; CERS5; human.
DR GenomeRNAi; 91012; -.
DR Pharos; Q8N5B7; Tbio.
DR PRO; PR:Q8N5B7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8N5B7; protein.
DR Bgee; ENSG00000139624; Expressed in cerebellar hemisphere and 175 other tissues.
DR ExpressionAtlas; Q8N5B7; baseline and differential.
DR Genevisible; Q8N5B7; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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; TAS:Reactome.
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 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..392
FT /note="Ceramide synthase 5"
FT /id="PRO_0000185514"
FT TOPO_DOM 1..46
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29632068"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
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 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26887952"
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 349..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 299..309
FT /note="Last loop motif"
FT /evidence="ECO:0000269|PubMed:29632068"
FT COMPBIAS 365..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29632068"
FT VAR_SEQ 1..65
FT /note="MATAAQGPLSLLWGWLWSERFWLPENVSWADLEGPADGYGYPRGRHILSVFP
FT LAAGIFFVRLLFE -> MMKPRPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054572"
FT VARIANT 75
FT /note="C -> R (in dbSNP:rs7302981)"
FT /id="VAR_019558"
FT MUTAGEN 26
FT /note="N->Q: Reduced N-glycosylation."
FT /evidence="ECO:0000269|PubMed:29632068"
FT MUTAGEN 153..165
FT /note="CIFCYGIRFLWSS->IAGMAVIVD: Does not affect
FT specificity toward acyl donor."
FT /evidence="ECO:0000269|PubMed:29632068"
FT MUTAGEN 220
FT /note="H->D: Strongly decreased ceramide synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16951403"
FT MUTAGEN 231
FT /note="S->A: Does not affect ceramide synthase activity."
FT /evidence="ECO:0000269|PubMed:16951403"
FT MUTAGEN 254
FT /note="L->E: Strongly decreased ceramide synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16951403"
FT MUTAGEN 254
FT /note="L->M: Does not affect ceramide synthase activity."
FT /evidence="ECO:0000269|PubMed:16951403"
FT MUTAGEN 299..309
FT /note="ESWEIIGPYAS->YPLELYPAFFG: Altered specificity toward
FT acyl donor; generates C22-C24 ceramides instead of C16-
FT ceramide."
FT /evidence="ECO:0000269|PubMed:29632068"
FT MUTAGEN 350..356
FT /note="SDVESSS->ADVEAAA: Decreased phosphorylation."
FT /evidence="ECO:0000269|PubMed:26887952"
SQ SEQUENCE 392 AA; 45752 MW; E95658B20CE114B5 CRC64;
MATAAQGPLS LLWGWLWSER FWLPENVSWA DLEGPADGYG YPRGRHILSV FPLAAGIFFV
RLLFERFIAK PCALCIGIED SGPYQAQPNA ILEKVFISIT KYPDKKRLEG LSKQLDWNVR
KIQCWFRHRR NQDKPPTLTK FCESMWRFTF YLCIFCYGIR FLWSSPWFWD IRQCWHNYPF
QPLSSGLYHY YIMELAFYWS LMFSQFTDIK RKDFLIMFVH HLVTIGLISF SYINNMVRVG
TLIMCLHDVS DFLLEAAKLA NYAKYQRLCD TLFVIFSAVF MVTRLGIYPF WILNTTLFES
WEIIGPYASW WLLNGLLLTL QLLHVIWSYL IARIALKALI RGKVSKDDRS DVESSSEEED
VTTCTKSPCD SSSSNGANRV NGHMGGSYWA EE
