SPTC2_CRIGR
ID SPTC2_CRIGR Reviewed; 560 AA.
AC O54694;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Serine palmitoyltransferase 2 {ECO:0000305};
DE EC=2.3.1.50 {ECO:0000250|UniProtKB:O15270};
DE AltName: Full=Long chain base biosynthesis protein 2;
DE Short=LCB 2;
DE AltName: Full=Long chain base biosynthesis protein 2a;
DE Short=LCB2a;
DE AltName: Full=Serine-palmitoyl-CoA transferase 2;
DE Short=SPT 2;
GN Name=SPTLC2; Synonyms=LCB2;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=9405408; DOI=10.1074/jbc.272.51.32108;
RA Hanada K., Hara T., Nishijima M., Kuge O., Dickson R.C., Nagiec M.M.;
RT "A mammalian homolog of the yeast LCB1 encodes a component of serine
RT palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid
RT synthesis.";
RL J. Biol. Chem. 272:32108-32114(1997).
CC -!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed
CC with LCB1/SPTLC1 constitutes the catalytic core. The composition of the
CC serine palmitoyltransferase (SPT) complex determines the substrate
CC preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference
CC for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays
CC a preference for C18-CoA substrate (By similarity). Plays an important
CC role in de novo sphyngolipid biosynthesis which is crucial for
CC adipogenesis (By similarity). {ECO:0000250|UniProtKB:O15270,
CC ECO:0000250|UniProtKB:P97363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 +
CC CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58299; EC=2.3.1.50;
CC Evidence={ECO:0000250|UniProtKB:O15270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC Evidence={ECO:0000250|UniProtKB:O15270};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine +
CC CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65073;
CC Evidence={ECO:0000250|UniProtKB:O15270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684;
CC Evidence={ECO:0000250|UniProtKB:O15270};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Heterodimer with SPTLC1. Component of the serine
CC palmitoyltransferase (SPT) complex, composed of LCB1/SPTLC1, LCB2
CC (SPTLC2 or SPTLC3) and ssPT (SPTSSA or SPTSSB) (By similarity).
CC {ECO:0000250|UniProtKB:O15270}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P97363}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P97363}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF004830; AAC53504.1; -; mRNA.
DR RefSeq; NP_001233609.1; NM_001246680.1.
DR AlphaFoldDB; O54694; -.
DR SMR; O54694; -.
DR STRING; 10029.NP_001233609.1; -.
DR Ensembl; ENSCGRT00001014323; ENSCGRP00001010103; ENSCGRG00001012086.
DR GeneID; 100689415; -.
DR KEGG; cge:100689415; -.
DR CTD; 9517; -.
DR eggNOG; KOG1357; Eukaryota.
DR GeneTree; ENSGT00940000155786; -.
DR OrthoDB; 438936at2759; -.
DR UniPathway; UPA00222; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0046513; P:ceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:1904504; P:positive regulation of lipophagy; IEA:Ensembl.
DR GO; GO:0046511; P:sphinganine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IEA:Ensembl.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IEA:Ensembl.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Pyridoxal phosphate; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..560
FT /note="Serine palmitoyltransferase 2"
FT /id="PRO_0000163857"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 377
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 560 AA; 62882 MW; C835A5E0244878E6 CRC64;
MRPEPGGCCC RRPLRANGCV KNGEVRNGYV RSSTATAAAA GQIHHVTENG GLYKRPFNEV
FEETPMLVAV LTYVGYGVLT LFGYLRDFLR HWRIEKCHHA TEREEQKDFV SLYQDFENFY
TRNLYMRIRD NWNRPICSVP GARVDIMERQ SHDYNWSFKY TGNIIKGVIN MGSYNYLGFA
RNTGSCQEAA AEVLKEYGAG VCSTRQEIGN LDKHEELEKL VARFLGVEAA MTYGMGFATN
SMNIPALVGK GCLILSDELN HASLVLGARL SGATIRIFKH NNMQSLEKLL KDAIVYGQPR
TRRPWKKILI LVEGIYSMEG SIVRLPEVIA LKKKYKAYLY LDEAHSIGAL GPSGRGVVDY
FGLDPEDVDV MMGTFTKSFG ASGGYIGGKK ALIDYLRTHS HSAVYATSMS PPVMEQIITS
MKCIMGQDGT SLGKECVQQL AENTKYFRRR LKEMGFIIYG NEDSPVVPLM LYMPAKIGAF
GREMLKRNVG VVVVGFPATP IIESRARFCL SAAHTKEILD TALKEIDEVG DLLQLKYSRR
RLVPLLDRPF DETTYEETED
