ID I3KPD2_ORENI Unreviewed; 153 AA.
AC I3KPD2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 04-NOV-2026, entry version 71.
DE RecName: Full=ORM1-like protein {ECO:0000256|PIRNR:PIRNR018147};
GN Name=ormdl1 {ECO:0000313|Ensembl:ENSONIP00000022977.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000022977.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000022977.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2026) to UniProtKB.
CC -!- FUNCTION: Plays an essential role in the homeostatic regulation of
CC sphingolipid de novo biosynthesis by modulating the activity of the
CC serine palmitoyltransferase (SPT) in response to ceramide levels. When
CC complexed to SPT, the binding of ceramides to its N-terminus stabilizes
CC a conformation that block SPT substrate entry, hence preventing SPT
CC catalytic activity. Through this mechanism, maintains ceramide levels
CC at sufficient concentrations for the production of complex
CC sphingolipids, but which prevents the accumulation of ceramides to
CC levels that trigger apoptosis. {ECO:0000256|ARBA:ARBA00045896}.
CC -!- SUBUNIT: Ceramide-sensitive subunit of the serine palmitoyltransferase
CC (SPT) complex, which is also composed of SPTLC1, SPTLC2/3 and SPTSSA/B.
CC {ECO:0000256|ARBA:ARBA00038646}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ORM family. {ECO:0000256|ARBA:ARBA00007649,
CC ECO:0000256|PIRNR:PIRNR018147}.
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DR RefSeq; XP_003458882.1; XM_003458834.5.
DR AlphaFoldDB; I3KPD2; -.
DR FunCoup; I3KPD2; 979.
DR STRING; 8128.ENSONIP00000073428; -.
DR Ensembl; ENSONIT00000022997.2; ENSONIP00000022977.2; ENSONIG00000018245.2.
DR GeneID; 100712327; -.
DR KEGG; onl:100712327; -.
DR CTD; 94101; -.
DR eggNOG; KOG3319; Eukaryota.
DR GeneTree; ENSGT00950000183178; -.
DR HOGENOM; CLU_072117_3_0_1; -.
DR InParanoid; I3KPD2; -.
DR OMA; AFHWVKG; -.
DR OrthoDB; 1932233at2759; -.
DR Proteomes; UP000005207; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0006672; P:ceramide metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:2000303; P:regulation of ceramide biosynthetic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR007203; ORMDL.
DR PANTHER; PTHR12665; ORMDL PROTEINS; 1.
DR Pfam; PF04061; ORMDL; 1.
DR PIRSF; PIRSF018147; ORMDL; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR018147};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018147};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 153 AA; 17309 MW; 302AB8BD6B776582 CRC64;
MNVGVAHSEV NPNTRVMNSR GIWLTYALGV GVLHIVLLSI PFFSVPVVWT LTNVIHNLGM
YVFMHAVKGT PFETPDQGKA RLLTHWEQLD YGVQFTSSRK FFTISPIILY FLASFYTKYD
TTHFVINTAS LLSVLIPKLP QLHGVRILGI NKY
//
