ID ORML2_BOVIN Reviewed; 153 AA.
AC Q5E972; Q32KP3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 02-SEP-2026, entry version 103.
DE RecName: Full=ORM1-like protein 2;
GN Name=ORMDL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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 (By
CC similarity). When complexed to SPT, the binding of ceramides to its N-
CC terminus stabilizes a conformation that block SPT substrate entry,
CC hence preventing SPT catalytic activity. Through this mechanism,
CC maintains ceramide levels at sufficient concentrations for the
CC production of complex sphingolipids, but which prevents the
CC accumulation of ceramides to levels that trigger apoptosis (By
CC similarity). {ECO:0000250|UniProtKB:Q53FV1,
CC ECO:0000250|UniProtKB:Q8N138}.
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:0000250|UniProtKB:Q53FV1}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q53FV1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53FV1}.
CC -!- DOMAIN: Ceramides bind to ORMDL3 N-terminus and stabilize it in a
CC conformation that physically restricts the accessibility of the
CC substrates to their binding sites in the serine palmitoyltransferase
CC (SPT) complex, hence inhibiting SPT catalytic activity. In the absence
CC of ceramides, the N-terminus is flexible and permits substrate binding,
CC thus liberating SPT from inhibition. {ECO:0000250|UniProtKB:Q8N138}.
CC -!- SIMILARITY: Belongs to the ORM family. {ECO:0000305}.
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DR EMBL; BT021048; AAX09065.1; -; mRNA.
DR EMBL; BC109992; AAI09993.1; -; mRNA.
DR RefSeq; NP_001014931.1; NM_001014931.1.
DR RefSeq; XP_005206638.1; XM_005206581.4.
DR RefSeq; XP_005206639.1; XM_005206582.5.
DR AlphaFoldDB; Q5E972; -.
DR SMR; Q5E972; -.
DR FunCoup; Q5E972; 2977.
DR STRING; 9913.ENSBTAP00000027540; -.
DR PaxDb; 9913-ENSBTAP00000027540; -.
DR Ensembl; ENSBTAT00000027540.4; ENSBTAP00000027540.3; ENSBTAG00000020663.4.
DR Ensembl; ENSBTAT00085024988; ENSBTAP00085017660; ENSBTAG00085028787.
DR Ensembl; ENSBTAT00090012621; ENSBTAP00090005859; ENSBTAG00090006939.
DR GeneID; 515878; -.
DR KEGG; bta:515878; -.
DR CTD; 29095; -.
DR VEuPathDB; HostDB:ENSBTAG00000020663; -.
DR VGNC; VGNC:32453; ORMDL2.
DR eggNOG; KOG3319; Eukaryota.
DR GeneTree; ENSGT00950000183178; -.
DR HOGENOM; CLU_072117_3_0_1; -.
DR InParanoid; Q5E972; -.
DR OMA; STHYTHF; -.
DR OrthoDB; 1932233at2759; -.
DR Reactome; R-BTA-1660661; Sphingolipid de novo biosynthesis.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000020663; Expressed in oviduct epithelium and 102 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0017059; C:serine palmitoyltransferase complex; IBA:GO_Central.
DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
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; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..153
FT /note="ORM1-like protein 2"
FT /id="PRO_0000215635"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 153 AA; 17404 MW; 3387D6A2CA860AEE CRC64;
MNVGVAHSEV NPNTRVMNSR GIWLAYIILV GLLHVVLLSI PFFSIPVVWT LTNVIHNLVM
YVFLHTVKGT PFETPDQGKA RLLTHWEQMD YGLQFTSSRK FLSISPIVLY LLASFYTKYD
AAHFLINTAS LLSVLLPKLP QFHGVRLFGI NKY
//
