CERS4_BOVIN
ID CERS4_BOVIN Reviewed; 393 AA.
AC Q5E9R6; Q0V884;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ceramide synthase 4 {ECO:0000250|UniProtKB:Q9HA82};
DE Short=CerS4 {ECO:0000250|UniProtKB:Q9HA82};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9HA82};
DE AltName: Full=LAG1 longevity assurance homolog 4 {ECO:0000250|UniProtKB:Q9HA82};
DE AltName: Full=Sphingosine N-acyltransferase CERS4 {ECO:0000305};
DE EC=2.3.1.24 {ECO:0000250|UniProtKB:Q9HA82};
GN Name=CERS4 {ECO:0000250|UniProtKB:Q9HA82};
GN Synonyms=LASS4 {ECO:0000250|UniProtKB:Q9HA82};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9HA82}.
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:Q9HA82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36548;
CC Evidence={ECO:0000250|UniProtKB:Q9HA82};
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:0000250|UniProtKB:Q9HA82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36556;
CC Evidence={ECO:0000250|UniProtKB:Q9HA82};
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:0000250|UniProtKB:Q9D6J1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33592;
CC Evidence={ECO:0000250|UniProtKB:Q9D6J1};
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:0000250|UniProtKB:Q9HA82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43045;
CC Evidence={ECO:0000250|UniProtKB:Q9HA82};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q9HA82}.
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:0000250|UniProtKB:Q9HA82}.
CC -!- PTM: Phosphorylated at the C-terminus by CK2.
CC {ECO:0000250|UniProtKB:Q9HA82}.
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; BT020828; AAX08845.1; -; mRNA.
DR EMBL; BT020854; AAX08871.1; -; mRNA.
DR EMBL; BT026335; ABG81491.1; -; mRNA.
DR EMBL; BC120450; AAI20451.1; -; mRNA.
DR RefSeq; NP_001015520.1; NM_001015520.1.
DR RefSeq; XP_005208907.1; XM_005208850.2.
DR RefSeq; XP_010805210.1; XM_010806908.2.
DR AlphaFoldDB; Q5E9R6; -.
DR STRING; 9913.ENSBTAP00000004459; -.
DR PaxDb; Q5E9R6; -.
DR PRIDE; Q5E9R6; -.
DR Ensembl; ENSBTAT00000004459; ENSBTAP00000004459; ENSBTAG00000003434.
DR GeneID; 505233; -.
DR KEGG; bta:505233; -.
DR CTD; 79603; -.
DR VEuPathDB; HostDB:ENSBTAG00000003434; -.
DR VGNC; VGNC:27226; CERS4.
DR eggNOG; KOG1607; Eukaryota.
DR GeneTree; ENSGT01030000234515; -.
DR HOGENOM; CLU_028277_1_1_1; -.
DR InParanoid; Q5E9R6; -.
DR OMA; DQGGDCY; -.
DR OrthoDB; 987268at2759; -.
DR TreeFam; TF314319; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000003434; Expressed in retina and 100 other tissues.
DR ExpressionAtlas; Q5E9R6; baseline.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..393
FT /note="Ceramide synthase 4"
FT /id="PRO_0000240447"
FT TOPO_DOM 1..31
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9HA82"
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..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9HA82"
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 346..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 291..301
FT /note="Last loop motif"
FT /evidence="ECO:0000250|UniProtKB:Q9HA82"
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"
SQ SEQUENCE 393 AA; 46363 MW; 3F443D400F9CF8B5 CRC64;
MWSSLNDWLW NERLWLPANI SWAQLEDHDG LVFPHPQDTL MAVPLALALV VVRFTFERFV
ALPLSRWLGV RNQIRRPADP NATLEKHYLM KGREPTESQM NLLATQCGLT LRQTQCWFRR
RRNQDRPCLT KKFCESSWKF VFYLCCFVCG TMVLYHESWL WTPVKCWENY PHQPLKPGLY
HWYLLELSFY ISLLMTLPFD TKRKDFKEQV IHHFVTIILI SFSYSLNLLR IGSLVLLLHD
SADYLLEASK LFNYMHWRRM CDTLFIIFSL VFFYTRLVLF PTRILYTTFF ESIGNFSPFF
GYYFLNILLV ILQLLHVFWS WLILCMIYSF IKKGQMEKDV RSDVEELDSS DGEAAEECPQ
MKNGAAQRPG AAPTDGPRSR AAGRMVNRHT PAT
