ID H2VA90_TAKRU Unreviewed; 391 AA.
AC H2VA90;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Ceramide synthase 6 {ECO:0000313|Ensembl:ENSTRUP00000046130.3};
GN Name=CERS6 {ECO:0000313|Ensembl:ENSTRUP00000046130.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000046130.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000046130.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000046130.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Sequence-specific transcription factor which is part of a
CC developmental regulatory system that provides cells with specific
CC positional identities on the anterior-posterior axis.
CC {ECO:0000256|ARBA:ARBA00003263}.
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 AlphaFoldDB; H2VA90; -.
DR STRING; 31033.ENSTRUP00000066639; -.
DR Ensembl; ENSTRUT00000046285.3; ENSTRUP00000046130.3; ENSTRUG00000018001.3.
DR eggNOG; KOG1607; Eukaryota.
DR GeneTree; ENSGT01030000234515; -.
DR TreeFam; TF314319; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000005226; Chromosome 1.
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:InterPro.
DR GO; GO:0046513; P:ceramide biosynthetic process; IEA:InterPro.
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 Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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:UP000005226};
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 43..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..132
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 135..336
FT /note="TLC"
FT /evidence="ECO:0000259|PROSITE:PS50922"
FT DNA_BIND 90..133
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 342..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 45615 MW; 2F600C82BDD59428 CRC64;
LAEAEMAGIL AWFWNERFWL PHNVTWADLK NTDEATFPQA EDLYLACPLA FCIFMIRLIF
ERFIARPCAM GLKIQANGPQ KAQSNAILEK VFTAITKHPD EKRLEGLSKQ LDWDVRTIQR
WFRQRRNQEK PSTLARFCES MWKFTFYLYI FTYGVRFLKK TPWLWNTKEC WYNYPYQPLT
VDIHYYYVLE LSFYLSLLFS QFTDIRRKDF LIMFLHHVAA ISLITFSYVN NMARVGTLVM
CLHDAADVLI EAAKMANYAK CQILCNLLFA MFAILFISSR LGVYPVWILN TTLFESWEIV
GPYPSWWVFN LLLILLQLLH SFWSYLIVKT VCRAISKGKV SKDDRSDIES SSDEDDGPPP
SQKHHSSATN GTNKNHGTNG YLTGGSYPDE H
//
