ID A0A498MF57_LABRO Unreviewed; 215 AA.
AC A0A498MF57;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 04-NOV-2026, entry version 21.
DE SubName: Full=ORM1 2 {ECO:0000313|EMBL:RXN17992.1};
GN ORFNames=ROHU_007913 {ECO:0000313|EMBL:RXN17992.1};
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:RXN17992.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN17992.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN17992.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN17992.1};
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}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the ORM family. {ECO:0000256|ARBA:ARBA00007649}.
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:RXN17992.1}.
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DR EMBL; QBIY01012730; RXN17992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MF57; -.
DR STRING; 84645.A0A498MF57; -.
DR PaxDb; 84645-A0A498MF57; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR007203; ORMDL.
DR PANTHER; PTHR12665; ORMDL PROTEINS; 1.
DR Pfam; PF04061; ORMDL; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 215 AA; 24239 MW; 3E8B48EB96F420C0 CRC64;
MSSANGAPAR AADEVNFTEC KALSIKLNEM ARDLYNTVES PEFSSIIDDP PVSVRPIDIC
DPVSLYSNRE TCQSRIILAL KNYTRIFNKN GVFKNSACSK WRGQANKVAD VTGDLLRLLE
AMYLFLHTVK GTPFETPDQG KARLLTHWEQ MDYGVQFTAS RKFLTISPII LYILASFYTK
YDTTHFLVNT GSLLSVLLPK LPQFHGVRLF GINKY
//
