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Database: UniProt
Entry: A0AAD5AGE4_SILAS
LinkDB: A0AAD5AGE4_SILAS
Original site: A0AAD5AGE4_SILAS 
ID   A0AAD5AGE4_SILAS        Unreviewed;        96 AA.
AC   A0AAD5AGE4;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   02-SEP-2026, entry version 8.
DE   SubName: Full=ORM1-like protein 3 {ECO:0000313|EMBL:KAI5616038.1};
DE   Flags: Fragment;
GN   ORFNames=C0J50_8533 {ECO:0000313|EMBL:KAI5616038.1};
OS   Silurus asotus (Amur catfish) (Parasilurus asotus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Siluridae; Silurus.
OX   NCBI_TaxID=30991 {ECO:0000313|EMBL:KAI5616038.1, ECO:0000313|Proteomes:UP001205998};
RN   [1] {ECO:0000313|EMBL:KAI5616038.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Chongqing {ECO:0000313|EMBL:KAI5616038.1};
RA   Zhang Y., Wang D., Peng Z., Zheng S., Shao F., Tao W.;
RT   "Comparative genomics of catfishes provides insights into carnivory and
RT   benthic adaptation.";
RL   Submitted (JUL-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   -!- 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:KAI5616038.1}.
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DR   EMBL; MU552100; KAI5616038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD5AGE4; -.
DR   Proteomes; UP001205998; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro.
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:UP001205998};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KAI5616038.1"
FT   NON_TER         96
FT                   /evidence="ECO:0000313|EMBL:KAI5616038.1"
SQ   SEQUENCE   96 AA;  11313 MW;  E07328B6F507223A CRC64;
     QCMYLLLHTV KGTPFETPDQ GKARLLTHWE QMDYGVQFTA SRKFLTITPI ILYFLTSFYT
     KYDRIHFFIN TLSLLTVLIP KLPQLHGVRL FGINKY
//
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