ID A0A3Q7R9Y7_VULVU Unreviewed; 380 AA.
AC A0A3Q7R9Y7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Ceramide synthase 2 {ECO:0000313|RefSeq:XP_025838899.1, ECO:0000313|RefSeq:XP_025838900.1};
GN Name=CERS2 {ECO:0000313|RefSeq:XP_025838899.1,
GN ECO:0000313|RefSeq:XP_025838900.1, ECO:0000313|RefSeq:XP_025838901.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025838901.1};
RN [1]
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025838899.1,
RC ECO:0000313|RefSeq:XP_025838900.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025838899.1,
RC ECO:0000313|RefSeq:XP_025838900.1};
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025838901.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025838901.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025838901.1};
RG RefSeq;
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 RefSeq; XP_025838899.1; XM_025983114.1.
DR RefSeq; XP_025838900.1; XM_025983115.1.
DR RefSeq; XP_025838901.1; XM_025983116.1.
DR STRING; 9627.ENSVVUP00000015871; -.
DR Ensembl; ENSVVUT00000020842; ENSVVUP00000015871; ENSVVUG00000011653.
DR KEGG; vvp:112907770; -.
DR OMA; KMFIHFV; -.
DR OrthoDB; 460400at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000286640; Unplaced.
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 GO; GO:0019216; P:regulation of lipid metabolic 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:SF7; CERAMIDE SYNTHASE 2; 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:UP000286640};
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 45..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..128
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 131..332
FT /note="TLC"
FT /evidence="ECO:0000259|PROSITE:PS50922"
FT DNA_BIND 69..129
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 338..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 380 AA; 44881 MW; 0888B59FF58C9FEB CRC64;
MFQTLYDYFW WERLWLPVNL TWADLEDRDG RVYAKASDLY ITLPLALLFL IVRYFFELYV
ATPLAALLNV KEKTRLRAPP NPTLEHFYLT SGKQPKQAEV ELLSRQSGLS GRQVERWFRR
RRNQDRPSLL KKFREASWRF TFYLIAFIAG MAVIVDKPWF YDMKKVWEGY PIQSTIPSQY
WYYMIELSFY WSLLFSIASD VKRKDFKEQI IHHVATIILI SFSWFANYIR AGTLIMALHD
SSDYLLESAK MFNYAGWKNT CNNIFIVFAI VFIITRLVIL PFWILHCTIV YPLELYPAFF
GYYFFNSMMG VLQLLHIFWA YLILRMAHKF ITGKLVEDER SDREETESSE GEEAGAVGGA
KSRPLANGHP VLSNNHRKND
//
