ID   A0A498LVM1_LABRO        Unreviewed;       153 AA.
AC   A0A498LVM1;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   04-NOV-2026, entry version 23.
DE   RecName: Full=ORM1-like protein {ECO:0000256|PIRNR:PIRNR018147};
GN   ORFNames=ROHU_030122 {ECO:0000313|EMBL:RXN11176.1};
OS   Labeo rohita (Indian major carp) (Cyprinus rohita).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Labeoninae; Labeonini; Labeo.
OX   NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN11176.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN11176.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN11176.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN11176.1};
RA   Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA   Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA   Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA   Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA   Shah T.M., Rai A., Jena J.K.;
RT   "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL   Submitted (MAR-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RXN11176.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QBIY01013150; RXN11176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498LVM1; -.
DR   STRING; 84645.A0A498LVM1; -.
DR   PaxDb; 84645-A0A498LVM1; -.
DR   OrthoDB; 1932233at2759; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
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   1: Evidence at protein level;
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR018147};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018147};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A498LVM1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572};
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;  17609 MW;  C70E1774AD7D09B1 CRC64;
     MNVGTAHSEV NPNTRVMNSR GIWLSYVLGI GLLHIILLSI PFVSVPVVWT LTNLIHNLCM
     YIFLHTVKGT PFETPDQGKA RLLTHWEQMD YGVQFTASRK FLTITPIILY FLTSFYTKYD
     RVHFIINTIS LLTVLIPKLP QFHGVRLFGI NKY
//