SPTSA_MOUSE
ID SPTSA_MOUSE Reviewed; 71 AA.
AC Q8R207; Q8BHT2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine palmitoyltransferase small subunit A {ECO:0000305};
DE AltName: Full=Small subunit of serine palmitoyltransferase A;
DE Short=ssSPTa;
GN Name=Sptssa {ECO:0000312|MGI:MGI:1913399}; Synonyms=Ssspta;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22674.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25023.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25026.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25233.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25555.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK003171; BAC25023.1; ALT_INIT; mRNA.
DR EMBL; AK003275; BAC25026.1; ALT_INIT; mRNA.
DR EMBL; AK008904; BAC25233.1; ALT_INIT; mRNA.
DR EMBL; AK018380; BAC25555.1; ALT_INIT; mRNA.
DR EMBL; BC022674; AAH22674.1; ALT_INIT; mRNA.
DR CCDS; CCDS36445.1; -.
DR RefSeq; NP_598815.2; NM_134054.2.
DR AlphaFoldDB; Q8R207; -.
DR SMR; Q8R207; -.
DR BioGRID; 222685; 1.
DR STRING; 10090.ENSMUSP00000053671; -.
DR PaxDb; Q8R207; -.
DR PRIDE; Q8R207; -.
DR DNASU; 104725; -.
DR Ensembl; ENSMUST00000056228; ENSMUSP00000053671; ENSMUSG00000044408.
DR GeneID; 104725; -.
DR KEGG; mmu:104725; -.
DR UCSC; uc007nnt.1; mouse.
DR CTD; 171546; -.
DR MGI; MGI:1913399; Sptssa.
DR VEuPathDB; HostDB:ENSMUSG00000044408; -.
DR eggNOG; ENOG502S4Q3; Eukaryota.
DR GeneTree; ENSGT00390000002766; -.
DR HOGENOM; CLU_187811_1_0_1; -.
DR InParanoid; Q8R207; -.
DR OMA; AWKQISW; -.
DR OrthoDB; 1627882at2759; -.
DR PhylomeDB; Q8R207; -.
DR TreeFam; TF328418; -.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 104725; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Sptssa; mouse.
DR PRO; PR:Q8R207; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8R207; protein.
DR Bgee; ENSMUSG00000044408; Expressed in lip and 64 other tissues.
DR ExpressionAtlas; Q8R207; baseline and differential.
DR Genevisible; Q8R207; MM.
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; ISO:MGI.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic process; ISO:MGI.
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..71
FT /note="Serine palmitoyltransferase small subunit A"
FT /id="PRO_0000089950"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..34
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="A -> S (in Ref. 1; BAC25026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 71 AA; 8452 MW; ED4F189EB101703C CRC64;
MAGMALARAW KQMSWFYYQY LLVTALYMLE PWERTVFNSM LVSVVGMALY TGYVFMPQHI
MAILHYFEIV Q
