ID LCB2C_ORYSJ Reviewed; 497 AA. AC Q8RYL0; A0A0P0VCB1; DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=Long chain base biosynthesis protein 2c; DE EC=2.3.1.50; GN OrderedLocusNames=Os01g0928700, LOC_Os01g70370; GN ORFNames=OsJ_04634, OSJNBa0052O12.13; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12447438; DOI=10.1038/nature01184; RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M., RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.; RT "The genome sequence and structure of rice chromosome 1."; RL Nature 420:312-316(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). CC -!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed CC with LCB1 constitutes the catalytic core (By similarity). CC {ECO:0000250}. 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 -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC -!- SUBUNIT: Heterodimer with LCB1. Component of the serine CC palmitoyltransferase (SPT) complex, composed of LCB1 and LCB2 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; CC Single-pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP004330; BAB90752.1; -; Genomic_DNA. DR EMBL; AP008207; BAF07192.1; -; Genomic_DNA. DR EMBL; AP014957; BAS76015.1; -; Genomic_DNA. DR EMBL; CM000138; EAZ14710.1; -; Genomic_DNA. DR RefSeq; XP_015613384.1; XM_015757898.1. DR AlphaFoldDB; Q8RYL0; -. DR SMR; Q8RYL0; -. DR STRING; 39947.Q8RYL0; -. DR PaxDb; 39947-Q8RYL0; -. DR EnsemblPlants; Os01t0928700-00; Os01t0928700-00; Os01g0928700. DR GeneID; 4326965; -. DR Gramene; Os01t0928700-00; Os01t0928700-00; Os01g0928700. DR KEGG; osa:4326965; -. DR eggNOG; KOG1357; Eukaryota. DR HOGENOM; CLU_015846_7_0_1; -. DR InParanoid; Q8RYL0; -. DR OMA; YAEPMSV; -. DR OrthoDB; 341090at2759; -. DR PlantReactome; R-OSA-1119325; Sphingolipid metabolism. DR PlantReactome; R-OSA-1119610; Biotin biosynthesis II. DR UniPathway; UPA00222; -. DR Proteomes; UP000000763; Chromosome 1. DR Proteomes; UP000007752; Chromosome 1. DR Proteomes; UP000059680; Chromosome 1. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IBA:GO_Central. DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central. DR GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central. DR CDD; cd06454; KBL_like; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1. DR PANTHER; PTHR13693:SF3; LD36009P; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. DR Genevisible; Q8RYL0; OS. PE 3: Inferred from homology; KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane; KW Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..497 FT /note="Long chain base biosynthesis protein 2c" FT /id="PRO_0000419152" FT TRANSMEM 4..24 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 319 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250" SQ SEQUENCE 497 AA; 54647 MW; 7EF5833AA6538DB5 CRC64; MVRVPFVTAV TTVFSYGVIF GFGHLRDWFR ALLRSLFSGH SPAAAGTNLK GYAPICGGQE DFYYRRFVRR VQDCFWRPIA SKPDAWFDVV ERYSNDSNKT LHRTTKTSRC LNLGSYNYLG FAAADEYCTP RVIESLKKYS ASTCSVRVDG GNTKLHVELE ELVARFVGKP AAILFGMGYV TNSAIIPALI GKGGLIISDS LNHNSIVNGA RGSGASVQVF QHNNPAHLEE VLREQIAGGQ PRTHRRWKKI IVIVEGIYSM EGELCKLPEI VAVCKKYKAY TYLDEAHSIG AVGKTGRGVC ELLGVDPADV DIMMGTFTKS FGSCGGYIAA SKEIIDHLKH ICPAHIYATS MSPPAVQQVI SAIEVILGED GSDRGAKKLA QIRENSNFFR SELEKMGFEV LGDNDSPVMP IMLYNPAKMP AFSRECLRQK VAIVTVSFPA TPLLLARARI CISASHSRED LIKGLEVISK VGDLVGIKYL PVEHEKTTSA EKLKKIQ //