ID   U6CPN5_NEOVI            Unreviewed;       153 AA.
AC   U6CPN5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   04-NOV-2026, entry version 43.
DE   RecName: Full=ORM1-like protein {ECO:0000256|PIRNR:PIRNR018147};
GN   Name=ORML1 {ECO:0000313|EMBL:CCP72411.1};
OS   Neogale vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Neogale.
OX   NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP72411.1};
RN   [1] {ECO:0000313|EMBL:CCP72411.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pool of brain {ECO:0000313|EMBL:CCP72411.1};
RA   Anistoroaei R., Christensen K.;
RT   "An American mink transcriptome.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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; HAAF01000585; CCP72411.1; -; mRNA.
DR   AlphaFoldDB; U6CPN5; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR018147};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018147};
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..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;  17371 MW;  14CE86484640D27D CRC64;
     MNVGVAHSEV NPNTRVMNSR GMWLTYALGV GLLHIVLLSI PFFSVPVAWT LTNVIHNLGM
     YVFLHAVKGT PFETPDQGKA RLLTHWEQLD YGVQFTSSRK FFTISPIILY FLASFYTKYD
     PTHFILNTAS LLTVLIPKMP QLHGVRIFGI NKY
//