ID G3NHZ1_GASAC Unreviewed; 153 AA.
AC G3NHZ1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 04-NOV-2026, entry version 68.
DE RecName: Full=ORM1-like protein {ECO:0000256|PIRNR:PIRNR018147};
OS Gasterosteus aculeatus aculeatus (three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=481459 {ECO:0000313|Ensembl:ENSGACP00000004951.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000004951.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Benthic {ECO:0000313|Ensembl:ENSGACP00000004951.1,
RC ECO:0000313|Proteomes:UP000007635};
RX PubMed=33598708;
RA Nath S., Shaw D.E., White M.A.;
RT "Improved contiguity of the threespine stickleback genome using long-read
RT sequencing.";
RL G3 (Bethesda) 11:0-0(2021).
RN [2] {ECO:0000313|Ensembl:ENSGACP00000004951.1}
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 AlphaFoldDB; G3NHZ1; -.
DR FunCoup; G3NHZ1; 1303.
DR STRING; 69293.ENSGACP00000004951; -.
DR Ensembl; ENSGACT00000004965.2; ENSGACP00000004951.1; ENSGACG00000003772.2.
DR KEGG; gat:120819565; -.
DR eggNOG; KOG3319; Eukaryota.
DR GeneTree; ENSGT00950000183178; -.
DR InParanoid; G3NHZ1; -.
DR OMA; AAWCFSQ; -.
DR OrthoDB; 1932233at2759; -.
DR Proteomes; UP000007635; Chromosome V.
DR Bgee; ENSGACG00000003772; Expressed in heart and 11 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:UP000007635};
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; 17399 MW; 66E2CCFE1C383843 CRC64;
MNVGTAHSEV NPNTRVMNSR GMWLSYILGI GLLHVILLSV PFASVPAVWT LTNLIHNLCM
YLLLHAVKGT PFETPDQGKA RLMTYWEQMD YGVQFTASRK FLTITPIVLY ILTSFYTKYD
RAHFVVNTLS LLTVLIPKLP QLHGVRIFGI NKY
//
