ID M3XHN7_LATCH Unreviewed; 153 AA.
AC M3XHN7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 04-NOV-2026, entry version 60.
DE RecName: Full=ORM1-like protein {ECO:0000256|PIRNR:PIRNR018147};
GN Name=ORMDL1 {ECO:0000313|Ensembl:ENSLACP00000022243.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000022243.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Ensembl:ENSLACP00000022243.1}
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 EMBL; AFYH01074217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01074218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01074219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01074220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005996595.1; XM_005996533.3.
DR RefSeq; XP_005996596.1; XM_005996534.3.
DR AlphaFoldDB; M3XHN7; -.
DR Ensembl; ENSLACT00000026563.1; ENSLACP00000022243.1; ENSLACG00000014434.2.
DR GeneID; 102348582; -.
DR CTD; 94101; -.
DR GeneTree; ENSGT00950000183178; -.
DR HOGENOM; CLU_072117_3_0_1; -.
DR OrthoDB; 1932233at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000014434; Expressed in pelvic fin and 6 other cell types or tissues.
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:UP000008672};
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..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 153 AA; 17393 MW; 33D9D67665978B88 CRC64;
MNVGVAHSEV NPNTRVMNSR GIWLTYALGV GMLHIVLLSI PFFSVPVVWT LTNVIHNLGM
YVFLHAVKGT PFETPDQGKA RLLTHWEQLD YGVQFTSSRK FFTISPIILY FLTSFYTKYD
PTHFIINTTS LLSVLIPKLP QLHGVRILGI NKY
//
