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)
1_MRPEP 6_ GGCCC 11_ RRTVR 16_ ANGCV 21_ ANGEV 26_ RNGYV 31_ RSSAA 36_ AAAAA 41_ AAGQI 46_ HHVTQ 51_ NGGLY 56_ KRPFN 61_ EAFEE 66_ TPMLV 71_ AVLTY 76_ VGYGV 81_ LTLFG 86_ YLRDF 91_ LRYWR 96_ IEKCH 101_ HATER 106_ EEQKD 111_ FVSLY 116_ QDFEN 121_ FYTRN 126_ LYMRI 131_ RDNWN 136_ RPICS 141_ VPGAR 146_ VDIME 151_ RQSHD 156_ YNWSF 161_ KYTGN 166_ IIKGV 171_ INMGS 176_ YNYLG 181_ FARNT 186_ GSCQE 191_ AAAKV 196_ LEEYG 201_ AGVCS 206_ TRQEI 211_ GNLDK 216_ HEELE 221_ ELVAR 226_ FLGVE 231_ AAMAY 236_ GMGFA 241_ TNSMN 246_ IPALV 251_ GKGCL 256_ ILSDE 261_ LNHAS 266_ LVLGA 271_ RLSGA 276_ TIRIF 281_ KHNNM 286_ QSLEK 291_ LLKDA 296_ IVYGQ 301_ PRTRR 306_ PWKKI 311_ LILVE 316_ GIYSM 321_ EGSIV 326_ RLPEV 331_ IALKK 336_ KYKAY 341_ LYLDE 346_ AHSIG 351_ ALGPT 356_ GRGVV 361_ EYFGL 366_ DPEDV 371_ DVMMG 376_ TFTKS 381_ FGASG 386_ GYIGG 391_ KKELI 396_ DYLRT 401_ HSHSA 406_ VYATS 411_ LSPPV 416_ VEQII 421_ TSMKC 426_ IMGQD 431_ GTSLG 436_ KECVQ 441_ QLAEN 446_ TRYFR 451_ RRLKE 456_ MGFII 461_ YGNED 466_ SPVVP 471_ LMLYM 476_ PAKIG 481_ AFGRE 486_ MLKRN 491_ IGVVV 496_ VGFPA 501_ TPIIE 506_ SRARF 511_ CLSAA 516_ HTKEI 521_ LDTAL 526_ KEIDE 531_ VGDLL 536_ QLKYS 541_ RHRLV 546_ PLLDR 551_ PFDET 556_TYEET
1: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases (PubMed:19416851, PubMed:19648650, PubMed:20504773, PubMed:20920666). The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core (PubMed:19416851). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (PubMed:19416851). The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA (PubMed:19416851, PubMed:19648650). The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (PubMed:19416851, PubMed:19648650). Crucial for adipogenesis (By similarity)