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Database: UniProt
Entry: A0A099YS92_TINGU
LinkDB: A0A099YS92_TINGU
Original site: A0A099YS92_TINGU 
ID   A0A099YS92_TINGU        Unreviewed;       331 AA.
AC   A0A099YS92;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Ceramide synthase 6 {ECO:0000313|EMBL:KGL73139.1};
DE   Flags: Fragment;
GN   ORFNames=N309_07947 {ECO:0000313|EMBL:KGL73139.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL73139.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL73139.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL73139.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; KL885612; KGL73139.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099YS92; -.
DR   STRING; 94827.A0A099YS92; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000053641; Unassembled WGS sequence.
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   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:UP000053641};
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        149..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..71
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000259|PROSITE:PS50071"
FT   DOMAIN          74..275
FT                   /note="TLC"
FT                   /evidence="ECO:0000259|PROSITE:PS50922"
FT   DNA_BIND        29..72
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT   REGION          285..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL73139.1"
FT   NON_TER         331
FT                   /evidence="ECO:0000313|EMBL:KGL73139.1"
SQ   SEQUENCE   331 AA;  38214 MW;  7EFA454BFBCB3010 CRC64;
     RFIAKPCALG LKVQANGPQK AQPNAILEKV FTAITKHPDE KRLEGLSKQL DWDVRSIQRW
     FRQRRNQEKP STLTKFCESM WRFTFYLYIF TYGVRFLKKT PWLWNTRQCW SGYPNQPLSP
     DLHYYYLVEL SFYWSLMFSQ FVDVRRKDFV IMFTHHVVAV ILITFSYITN LTRVGTLTLC
     LHDMADIILE AAKMANYCKC QKLSDLLFLS FAIVFIVSRL GIYPLWILNT TLFELYEALG
     NFPAWWVLNI LLALLQVLHC FWSYLIIKAA YKAISKGKVA KDDRSDIESS SDEEDTGSRS
     KTPHSTITTN GTGGANGTNG YLSGGTCSEE H
//
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