SPTSB_DANRE
ID SPTSB_DANRE Reviewed; 80 AA.
AC Q1RLT2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Serine palmitoyltransferase small subunit B;
DE AltName: Full=Protein ADMP;
DE AltName: Full=Small subunit of serine palmitoyltransferase B;
DE Short=ssSPTb;
GN Name=sptssb; Synonyms=admp, sssptb; ORFNames=zgc:136867;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT).
CC The composition of the serine palmitoyltransferase (SPT) complex
CC determines the substrate preference (By similarity).
CC {ECO:0000250|UniProtKB:Q8NFR3}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Interacts with sptlc1; the interaction is direct. Component of
CC the serine palmitoyltransferase (SPT) complex (By similarity).
CC {ECO:0000250|UniProtKB:Q8NFR3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SPTSS family. SPTSSB subfamily.
CC {ECO:0000305}.
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DR EMBL; BC115298; AAI15299.1; -; mRNA.
DR RefSeq; NP_001153305.1; NM_001159833.1.
DR RefSeq; NP_001289737.1; NM_001302808.1.
DR AlphaFoldDB; Q1RLT2; -.
DR SMR; Q1RLT2; -.
DR STRING; 7955.ENSDARP00000127984; -.
DR PaxDb; Q1RLT2; -.
DR Ensembl; ENSDART00000155579; ENSDARP00000127984; ENSDARG00000091658.
DR Ensembl; ENSDART00000181382; ENSDARP00000154838; ENSDARG00000091658.
DR GeneID; 678546; -.
DR KEGG; dre:678546; -.
DR CTD; 165679; -.
DR ZFIN; ZDB-GENE-060421-6887; sptssb.
DR eggNOG; ENOG502S4Q9; Eukaryota.
DR GeneTree; ENSGT00390000002766; -.
DR HOGENOM; CLU_187811_0_0_1; -.
DR InParanoid; Q1RLT2; -.
DR OMA; MNFKNFR; -.
DR OrthoDB; 1627882at2759; -.
DR PhylomeDB; Q1RLT2; -.
DR Reactome; R-DRE-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q1RLT2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 15.
DR Bgee; ENSDARG00000091658; Expressed in intestine and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; ISS:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:1904220; P:regulation of serine C-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR024512; Ser_palmitoyltrfase_ssu-like.
DR Pfam; PF11779; SPT_ssu-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Reference proteome;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..80
FT /note="Serine palmitoyltransferase small subunit B"
FT /id="PRO_0000378917"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..36
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 80 AA; 9477 MW; 83167A726295B8E2 CRC64;
MDMKNMREYM SWLYYQYLLI TGIYVLEPWE QSIFNTVLFT MVAMVIYTSY VFVPIHVRLA
LEFFCELVGG QPESTVALMT
