ID   SPTSB_BOVIN             Reviewed;          76 AA.
AC   Q0IIK4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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;
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].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-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, complexes with this subunit
CC       showing a clear preference for longer acyl-CoAs. The SPTLC1-SPTLC2-
CC       SPTSSB complex shows a strong preference for C18-CoA substrate, while
CC       the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader
CC       range of acyl-CoAs, without apparent 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, composed of SPTLC1,
CC       either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB (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; BC122600; AAI22601.1; -; mRNA.
DR   RefSeq; NP_001104244.1; NM_001110774.1.
DR   AlphaFoldDB; Q0IIK4; -.
DR   SMR; Q0IIK4; -.
DR   STRING; 9913.ENSBTAP00000055561; -.
DR   PaxDb; Q0IIK4; -.
DR   Ensembl; ENSBTAT00000085219; ENSBTAP00000068068; ENSBTAG00000049223.
DR   GeneID; 780785; -.
DR   KEGG; bta:780785; -.
DR   CTD; 165679; -.
DR   VEuPathDB; HostDB:ENSBTAG00000049223; -.
DR   VGNC; VGNC:35260; SPTSSB.
DR   eggNOG; ENOG502S4Q9; Eukaryota.
DR   GeneTree; ENSGT00390000002766; -.
DR   HOGENOM; CLU_187811_0_0_1; -.
DR   InParanoid; Q0IIK4; -.
DR   OMA; WEFFSEI; -.
DR   OrthoDB; 1627882at2759; -.
DR   TreeFam; TF328418; -.
DR   Reactome; R-BTA-1660661; Sphingolipid de novo biosynthesis.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000049223; Expressed in abomasum and 80 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:0004758; F:serine C-palmitoyltransferase activity; IEA:Ensembl.
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   GO; GO:0046512; P:sphingosine biosynthetic process; IEA:Ensembl.
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..76
FT                   /note="Serine palmitoyltransferase small subunit B"
FT                   /id="PRO_0000378916"
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..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   76 AA;  9180 MW;  7A8904819BC05227 CRC64;
     MDFKRVKDYL SWLYYQYQII SCCAVLEPWE QSMFNTIILT IFAMVVYTAY VFIPIHIRLA
     WEFFSKMCGY HSTISN