ID   SPTSA_BOVIN             Reviewed;          68 AA.
AC   Q5E978; A8E4L0;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Serine palmitoyltransferase small subunit A;
DE   AltName: Full=Small subunit of serine palmitoyltransferase A;
DE            Short=ssSPTa;
GN   Name=SPTSSA; Synonyms=SSSPTA;
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=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) 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. The SPTLC1-SPTLC2-SPTSSA complex
CC       shows a strong preference for C16-CoA substrate, while the SPTLC1-
CC       SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with
CC       a slight preference for C14-CoA. Plays a role in MBOAT7 location to
CC       mitochondria-associated membranes (MAMs), may me involved in fatty acid
CC       remodeling phosphatidylinositol (PI). {ECO:0000250|UniProtKB:Q969W0}.
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. Interacts with
CC       MBOAT7; the interaction facilitates MBOAT7 location to mitochondria-
CC       associated membranes (MAMs). {ECO:0000250|UniProtKB:Q969W0}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SPTSS family. SPTSSA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BT021042; AAX09059.1; -; mRNA.
DR   EMBL; BC134492; AAI34493.1; -; mRNA.
DR   RefSeq; NP_001181971.1; NM_001195042.1.
DR   AlphaFoldDB; Q5E978; -.
DR   SMR; Q5E978; -.
DR   STRING; 9913.ENSBTAP00000018578; -.
DR   PaxDb; Q5E978; -.
DR   Ensembl; ENSBTAT00000018578; ENSBTAP00000018578; ENSBTAG00000013981.
DR   GeneID; 615641; -.
DR   KEGG; bta:615641; -.
DR   CTD; 171546; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013981; -.
DR   VGNC; VGNC:35259; SPTSSA.
DR   eggNOG; ENOG502S4Q3; Eukaryota.
DR   GeneTree; ENSGT00390000002766; -.
DR   HOGENOM; CLU_187811_1_0_1; -.
DR   InParanoid; Q5E978; -.
DR   OMA; AWKQISW; -.
DR   OrthoDB; 1627882at2759; -.
DR   TreeFam; TF328418; -.
DR   Reactome; R-BTA-1660661; Sphingolipid de novo biosynthesis.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000013981; Expressed in adult mammalian kidney and 105 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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; IBA:GO_Central.
DR   GO; GO:0008104; P:protein localization; 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..68
FT                   /note="Serine palmitoyltransferase small subunit A"
FT                   /id="PRO_0000089948"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..31
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..68
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   68 AA;  8207 MW;  68DE7BB928FBDB72 CRC64;
     MALARAWKQM SWFYYQYLLV TALYMLEPWE RTVFNSMLVS IVGMALYTGY VFMPQHIMAI
     LHYFEIVQ