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Serine palmitoyltransferase 2 (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (LCB 2) (Long chain base biosynthesis protein 2a) (LCB2a) (Serine-palmitoyl-CoA transferase 2) (SPT 2)

 SPTC2_CRIGR             Reviewed;         560 AA.
O54694;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 99.
RecName: Full=Serine palmitoyltransferase 2;
EC=2.3.1.50;
AltName: Full=Long chain base biosynthesis protein 2;
Short=LCB 2;
AltName: Full=Long chain base biosynthesis protein 2a;
Short=LCB2a;
AltName: Full=Serine-palmitoyl-CoA transferase 2;
Short=SPT 2;
Name=SPTLC2; Synonyms=LCB2;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=9405408; DOI=10.1074/jbc.272.51.32108;
Hanada K., Hara T., Nishijima M., Kuge O., Dickson R.C., Nagiec M.M.;
"A mammalian homolog of the yeast LCB1 encodes a component of serine
palmitoyltransferase, the enzyme catalyzing the first step in
sphingolipid synthesis.";
J. Biol. Chem. 272:32108-32114(1997).
-!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer
formed with LCB1/SPTLC1 constitutes the catalytic core. The
composition of the serine palmitoyltransferase (SPT) complex
determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA
complex shows a strong preference for C16-CoA substrate, while the
SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA
substrate (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-
sphinganine + CO(2).
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
-!- SUBUNIT: Heterodimer with SPTLC1. Component of the serine
palmitoyltransferase (SPT) complex, composed of LCB1/SPTLC1, LCB2
(SPTLC2 or SPTLC3) and ssPT (SPTSSA or SPTSSB) (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
-!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
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EMBL; AF004830; AAC53504.1; -; mRNA.
RefSeq; NP_001233609.1; NM_001246680.1.
ProteinModelPortal; O54694; -.
SMR; O54694; -.
PRIDE; O54694; -.
Ensembl; ENSCGRT00001014323; ENSCGRP00001010103; ENSCGRG00001012086.
GeneID; 100689415; -.
KEGG; cge:100689415; -.
CTD; 9517; -.
HOVERGEN; HBG002230; -.
KO; K00654; -.
UniPathway; UPA00222; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0017059; C:serine C-palmitoyltransferase complex; IEA:Ensembl.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0004758; F:serine C-palmitoyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046513; P:ceramide biosynthetic process; IEA:Ensembl.
GO; GO:1904504; P:positive regulation of lipophagy; IEA:Ensembl.
GO; GO:0046511; P:sphinganine biosynthetic process; IEA:Ensembl.
GO; GO:0006686; P:sphingomyelin biosynthetic process; IEA:Ensembl.
GO; GO:0046512; P:sphingosine biosynthetic process; IEA:Ensembl.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
2: Evidence at transcript level;
Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
Pyridoxal phosphate; Sphingolipid metabolism; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 560 Serine palmitoyltransferase 2.
/FTId=PRO_0000163857.
TRANSMEM 65 85 Helical. {ECO:0000255}.
MOD_RES 377 377 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
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


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