ID H2MJS5_ORYLA Unreviewed; 153 AA.
AC H2MJS5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 04-NOV-2026, entry version 69.
DE RecName: Full=ORM1-like protein {ECO:0000256|PIRNR:PIRNR018147};
GN Name=ormdl1 {ECO:0000313|Ensembl:ENSORLP00000018924.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000018924.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000018924.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018924.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000018924.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018924.2};
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_020568997.1; XM_020713338.3.
DR AlphaFoldDB; H2MJS5; -.
DR FunCoup; H2MJS5; 955.
DR STRING; 8090.ENSORLP00000018924; -.
DR Ensembl; ENSORLT00000018925.2; ENSORLP00000018924.2; ENSORLG00000015100.2.
DR GeneID; 101160518; -.
DR KEGG; ola:101160518; -.
DR CTD; 94101; -.
DR eggNOG; KOG2771; Eukaryota.
DR GeneTree; ENSGT00950000183178; -.
DR HOGENOM; CLU_013817_2_1_1; -.
DR InParanoid; H2MJS5; -.
DR OrthoDB; 1932233at2759; -.
DR Proteomes; UP000001038; Chromosome 21.
DR Bgee; ENSORLG00000015100; Expressed in animal zygote and 14 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0017059; C:serine palmitoyltransferase complex; IBA:GO_Central.
DR GO; GO:0006672; P:ceramide metabolic process; IBA:GO_Central.
DR GO; GO:0090156; P:intracellular sphingolipid homeostasis; IBA:GO_Central.
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:UP000001038};
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; 17377 MW; D0C4B65D85796588 CRC64;
MNVGVAHSEV NPNTRVMNSR GIWLTYALGV GVLHIVLLSI PFFSVPVVWT LTNVIHNFGM
YVFMHAVKGT PFETPDQGKA RLLTHWEQLD YGVQFTSSRK FFTISPIILY FLASFYTKYD
TTHFVINTAS LLSVLIPKLP QLHGVRIFGI NKY
//
