SPTSB_MOUSE
ID SPTSB_MOUSE Reviewed; 76 AA.
AC Q925E8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 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 [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15777716; DOI=10.1016/j.gene.2004.12.047;
RA Singh J., Young L., Handelsman D.J., Dong Q.;
RT "Molecular cloning and characterization of a novel androgen repressible
RT gene expressed in the prostate epithelium.";
RL Gene 348:55-63(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
RN [4]
RP FUNCTION, MUTAGENESIS OF HIS-56, AND PATHWAY.
RX PubMed=26438849; DOI=10.1073/pnas.1516733112;
RA Zhao L., Spassieva S., Gable K., Gupta S.D., Shi L.Y., Wang J.,
RA Bielawski J., Hicks W.L., Krebs M.P., Naggert J., Hannun Y.A., Dunn T.M.,
RA Nishina P.M.;
RT "Elevation of 20-carbon long chain bases due to a mutation in serine
RT palmitoyltransferase small subunit b results in neurodegeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:12962-12967(2015).
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.
CC {ECO:0000269|PubMed:26438849}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:26438849}.
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 -!- TISSUE SPECIFICITY: Expression is strong in hypogonadal (hpg) mouse
CC prostate, weak in mature castrated mouse prostate and absent in normal
CC intact or androgen-replaced hpg mouse prostates.
CC {ECO:0000269|PubMed:15777716}.
CC -!- INDUCTION: While expression is androgen independent in the hpg mouse
CC prostate, it appears to be androgen-dependent in the kidney and brain
CC of normal intact mouse suggesting tissue specific regulation by
CC androgens. {ECO:0000269|PubMed:15777716}.
CC -!- SIMILARITY: Belongs to the SPTSS family. SPTSSB subfamily.
CC {ECO:0000305}.
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DR EMBL; AF365876; AAK53702.1; -; mRNA.
DR EMBL; AK010117; BAC25280.1; -; mRNA.
DR EMBL; AK009973; BAC25279.1; -; mRNA.
DR EMBL; AK004017; BAC25062.1; -; mRNA.
DR EMBL; BC022628; AAH22628.1; -; mRNA.
DR CCDS; CCDS38453.1; -.
DR RefSeq; NP_001157682.1; NM_001164210.2.
DR RefSeq; NP_598436.1; NM_133675.3.
DR AlphaFoldDB; Q925E8; -.
DR SMR; Q925E8; -.
DR STRING; 10090.ENSMUSP00000131241; -.
DR PhosphoSitePlus; Q925E8; -.
DR PaxDb; Q925E8; -.
DR PRIDE; Q925E8; -.
DR ProteomicsDB; 257062; -.
DR DNASU; 66183; -.
DR Ensembl; ENSMUST00000051239; ENSMUSP00000062794; ENSMUSG00000043461.
DR Ensembl; ENSMUST00000171529; ENSMUSP00000131241; ENSMUSG00000043461.
DR GeneID; 66183; -.
DR KEGG; mmu:66183; -.
DR UCSC; uc008pmn.3; mouse.
DR CTD; 165679; -.
DR MGI; MGI:1913433; Sptssb.
DR VEuPathDB; HostDB:ENSMUSG00000043461; -.
DR eggNOG; ENOG502S4Q9; Eukaryota.
DR GeneTree; ENSGT00390000002766; -.
DR HOGENOM; CLU_187811_0_0_1; -.
DR InParanoid; Q925E8; -.
DR OMA; WEFFSEI; -.
DR OrthoDB; 1627882at2759; -.
DR PhylomeDB; Q925E8; -.
DR TreeFam; TF328418; -.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 66183; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q925E8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q925E8; protein.
DR Bgee; ENSMUSG00000043461; Expressed in urinary bladder urothelium and 101 other tissues.
DR Genevisible; Q925E8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; IDA:MGI.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IDA:MGI.
DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:1904220; P:regulation of serine C-palmitoyltransferase activity; IMP:MGI.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:MGI.
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 1: Evidence at protein level;
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_0000239720"
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"
FT MUTAGEN 56
FT /note="H->L: Mutant mice develop early onset ataxia,
FT exhibit reduced body weight and usually die around 10 weeks
FT after birth. Increases SPT affininity toward C18-CoA
FT substrate by twofold and elevates C20 long chain base
FT production in the brain and eye. Produces neurodegenerative
FT effects such as aberrant membrane strucutres, accumulation
FT of ubiquitinated protein on membranes and axon
FT degeneration."
FT /evidence="ECO:0000269|PubMed:26438849"
SQ SEQUENCE 76 AA; 9108 MW; F9D17253A0E25CC3 CRC64;
MDFKRVKEYF AWLYYQYQII TCCAVMEPWE QSMLNTIILT IVAMVVYTAY VFIPIHIRLA
WEFFSKICGY DSSISN
