ID H2P7Q7_PONAB Unreviewed; 392 AA.
AC H2P7Q7; A0A2J8VQG3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=CERS6 isoform 2 {ECO:0000313|EMBL:PNJ59763.1};
DE SubName: Full=Ceramide synthase 6 {ECO:0000313|Ensembl:ENSPPYP00000014403.3};
GN Name=CERS6 {ECO:0000313|Ensembl:ENSPPYP00000014403.3};
GN ORFNames=CR201_G0017035 {ECO:0000313|EMBL:PNJ59763.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000014403.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000014403.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ59763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ59763.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000014403.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024546};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36548;
CC Evidence={ECO:0000256|ARBA:ARBA00024546};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus {ECO:0000256|PROSITE-
CC ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
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DR EMBL; NDHI03003413; PNJ59763.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000014403; -.
DR Ensembl; ENSPPYT00000014989.3; ENSPPYP00000014403.3; ENSPPYG00000012904.3.
DR eggNOG; KOG1607; Eukaryota.
DR GeneTree; ENSGT01030000234515; -.
DR HOGENOM; CLU_028277_1_2_1; -.
DR OMA; YLIGAPY; -.
DR TreeFam; TF314319; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000001595; Chromosome 2B.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0046513; P:ceramide biosynthetic process; IEA:Ensembl.
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:SF43; CERAMIDE SYNTHASE 6; 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; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS50922; TLC; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Homeobox {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00205};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00205};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..127
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 130..331
FT /note="TLC"
FT /evidence="ECO:0000259|PROSITE:PS50922"
FT DNA_BIND 85..128
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 344..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 45794 MW; 8977CEFEEA561DE4 CRC64;
MAGILAWFWN ERFWLPHNVT WADLKNTEEA TFPQAEDLYL AFPLAFCIFM VRLIFERFVA
KPCAIALNIQ ANGPQIAPPN AILEKVFTAI TKHPDEKRLE GLSKQLDWDV RSIQRWFRQR
RNQEKPSTLT RFCESMWRFS FYLYVFTYGV RFLKKTPWLW NTRHCWYNYP YQPLTTDLHY
YYILELSFYW SLMFSQFTDI KRKDFGIMFL HHLVSIFLIT FSYVNNMARV GTLVLCLHDS
ADALLEAAKM ANYAKFQKMC DLLFVMFAVV FITTRLGIFP LWVLNTTLFE SWEIVGPYPS
WWVFNLLLLL VQGLNCFWSY LIVKIACKAV SRGKAGKWNP LHVSKDDRSD IESSSDEEDS
EPPGKNPHTA TTTNGTSGTN GYLLTGSCSM DD
//
