ID H3B3W6_LATCH Unreviewed; 153 AA.
AC H3B3W6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 04-NOV-2026, entry version 74.
DE RecName: Full=ORM1-like protein {ECO:0000256|PIRNR:PIRNR018147};
GN Name=LOC102363939 {ECO:0000313|Ensembl:ENSLACP00000016587.2};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000016587.2, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Ensembl:ENSLACP00000016587.2}
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 EMBL; AFYH01103225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01103226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01103227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01103228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01103229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005999582.1; XM_005999520.3.
DR RefSeq; XP_005999583.1; XM_005999521.3.
DR RefSeq; XP_005999584.1; XM_005999522.3.
DR RefSeq; XP_005999585.1; XM_005999523.2.
DR AlphaFoldDB; H3B3W6; -.
DR FunCoup; H3B3W6; 793.
DR STRING; 7897.ENSLACP00000016587; -.
DR Ensembl; ENSLACT00000016701.2; ENSLACP00000016587.2; ENSLACG00000014619.2.
DR GeneID; 102363939; -.
DR KEGG; lcm:102363939; -.
DR eggNOG; KOG3319; Eukaryota.
DR GeneTree; ENSGT00950000183178; -.
DR HOGENOM; CLU_072117_3_0_1; -.
DR InParanoid; H3B3W6; -.
DR OMA; AAWCFSQ; -.
DR OrthoDB; 1932233at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000014619; 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 23..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 153 AA; 17559 MW; 90B99FBF76EEAAB5 CRC64;
MNVGTAHSEV NPNTRVMNSR GIWLSYVLGI GLLHVVLLSI PFFSVPVVWT LTNIIHNMSM
YIFLHTVKGT PFETPDQGKA RLLTHWEQMD YGVQFTASRK FLTITPIILY FLTSFYTKYD
RIHFAINTVS LMSVLIPKLP QLHGVRIFGI NKY
//
