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Long chain base biosynthesis protein 2a (AtLCB2a) (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (AtLCB2)

 LCB2A_ARATH             Reviewed;         489 AA.
Q9LSZ9; B9DFX8; Q9LRB4;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
13-FEB-2019, entry version 131.
RecName: Full=Long chain base biosynthesis protein 2a;
Short=AtLCB2a;
EC=2.3.1.50;
AltName: Full=Long chain base biosynthesis protein 2;
Short=AtLCB2;
Name=LCB2a; Synonyms=LCB2; OrderedLocusNames=At5g23670;
ORFNames=MQM1.6;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=11171191; DOI=10.1042/bst0280745;
Tamura K., Nishiura H., Mori J., Imai H.;
"Cloning and characterization of a cDNA encoding serine
palmitoyltransferase in Arabidopsis thaliana.";
Biochem. Soc. Trans. 28:745-747(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=11726713; DOI=10.1093/pcp/pce165;
Tamura K., Mitsuhashi N., Hara-Nishimura I., Imai H.;
"Characterization of an Arabidopsis cDNA encoding a subunit of serine
palmitoyltransferase, the initial enzyme in sphingolipid
biosynthesis.";
Plant Cell Physiol. 42:1274-1281(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-489.
STRAIN=cv. Columbia; TISSUE=Rosette leaf;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[7]
SUBUNIT.
PubMed=17194770; DOI=10.1105/tpc.105.040774;
Chen M., Han G., Dietrich C.R., Dunn T.M., Cahoon E.B.;
"The essential nature of sphingolipids in plants as revealed by the
functional identification and characterization of the Arabidopsis LCB1
subunit of serine palmitoyltransferase.";
Plant Cell 18:3576-3593(2006).
[8]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND SUBUNIT.
PubMed=18208516; DOI=10.1111/j.1365-313X.2008.03420.x;
Dietrich C.R., Han G., Chen M., Berg R.H., Dunn T.M., Cahoon E.B.;
"Loss-of-function mutations and inducible RNAi suppression of
Arabidopsis LCB2 genes reveal the critical role of sphingolipids in
gametophytic and sporophytic cell viability.";
Plant J. 54:284-298(2008).
[9]
FUNCTION.
PubMed=21534970; DOI=10.1111/j.1469-8137.2011.03727.x;
Saucedo-Garcia M., Guevara-Garcia A., Gonzalez-Solis A.,
Cruz-Garcia F., Vazquez-Santana S., Markham J.E., Lozano-Rosas M.G.,
Dietrich C.R., Ramos-Vega M., Cahoon E.B., Gavilanes-Ruiz M.;
"MPK6, sphinganine and the LCB2a gene from serine palmitoyltransferase
are required in the signaling pathway that mediates cell death induced
by long chain bases in Arabidopsis.";
New Phytol. 191:943-957(2011).
-!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer
formed with LCB1 constitutes the catalytic core. Involved in the
regulation of the programmed cell death (PCD) signaling pathway.
Plays an important role during male gametogenesis and
embryogenesis. {ECO:0000269|PubMed:11726713,
ECO:0000269|PubMed:18208516, ECO:0000269|PubMed:21534970}.
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine +
CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50;
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
-!- SUBUNIT: Heterodimer with LCB1. Component of the serine
palmitoyltransferase (SPT) complex, composed of LCB1 and LCB2
(LCB2a or LCB2b). {ECO:0000269|PubMed:17194770,
ECO:0000269|PubMed:18208516}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:11726713}; Single-pass membrane protein
{ECO:0000269|PubMed:11726713}.
-!- TISSUE SPECIFICITY: Ubiquitous. Detected in leaves, roots, stems,
flowers and at a lower level in mature seeds.
{ECO:0000269|PubMed:11171191, ECO:0000269|PubMed:11726713,
ECO:0000269|PubMed:18208516}.
-!- DEVELOPMENTAL STAGE: Detected at high levels in the petiole,
sepals and petals in young flowers, but was not detected in the
anthers during the early stages of pollen development.
{ECO:0000269|PubMed:18208516}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Lcb2a and lcb2b double
mutant is not viable due to pollen lethality.
{ECO:0000269|PubMed:18208516}.
-!- MISCELLANEOUS: The lcb2a-1 mutant is incapable of initiating
programmed cell death (PCD) after induction by fumonisin B1 (FB1),
a specific inhibitor of ceramide synthase.
-!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB046384; BAB03231.1; -; mRNA.
EMBL; AB025633; BAA97234.1; -; Genomic_DNA.
EMBL; CP002688; AED93196.1; -; Genomic_DNA.
EMBL; CP002688; AED93197.1; -; Genomic_DNA.
EMBL; AY050829; AAK92764.1; -; mRNA.
EMBL; AY133827; AAM91761.1; -; mRNA.
EMBL; AK316942; BAH19645.1; -; mRNA.
RefSeq; NP_001031932.1; NM_001036855.1.
RefSeq; NP_197756.1; NM_122272.3.
UniGene; At.23395; -.
UniGene; At.49054; -.
ProteinModelPortal; Q9LSZ9; -.
SMR; Q9LSZ9; -.
BioGrid; 17707; 1.
STRING; 3702.AT5G23670.1; -.
PaxDb; Q9LSZ9; -.
EnsemblPlants; AT5G23670.1; AT5G23670.1; AT5G23670.
EnsemblPlants; AT5G23670.2; AT5G23670.2; AT5G23670.
GeneID; 832432; -.
Gramene; AT5G23670.1; AT5G23670.1; AT5G23670.
Gramene; AT5G23670.2; AT5G23670.2; AT5G23670.
KEGG; ath:AT5G23670; -.
Araport; AT5G23670; -.
TAIR; locus:2171731; AT5G23670.
eggNOG; KOG1357; Eukaryota.
eggNOG; COG0156; LUCA.
HOGENOM; HOG000206826; -.
InParanoid; Q9LSZ9; -.
KO; K00654; -.
OMA; ISQGQPK; -.
OrthoDB; 438936at2759; -.
PhylomeDB; Q9LSZ9; -.
BioCyc; ARA:AT5G23670-MONOMER; -.
BioCyc; MetaCyc:AT5G23670-MONOMER; -.
BRENDA; 2.3.1.50; 399.
UniPathway; UPA00222; -.
PRO; PR:Q9LSZ9; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q9LSZ9; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0004758; F:serine C-palmitoyltransferase activity; IDA:TAIR.
GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
GO; GO:0009555; P:pollen development; IMP:TAIR.
GO; GO:0043067; P:regulation of programmed cell death; IMP:UniProtKB.
GO; GO:0046512; P:sphingosine biosynthetic process; IDA:TAIR.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
1: Evidence at protein level;
Acyltransferase; Apoptosis; Complete proteome; Endoplasmic reticulum;
Lipid metabolism; Membrane; Pyridoxal phosphate; Reference proteome;
Sphingolipid metabolism; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 489 Long chain base biosynthesis protein 2a.
/FTId=PRO_0000419145.
TRANSMEM 2 22 Helical. {ECO:0000255}.
MOD_RES 311 311 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
CONFLICT 65 65 D -> N (in Ref. 1 and 2; BAB03231).
{ECO:0000305}.
SEQUENCE 489 AA; 54290 MW; 00B396BB47D2E048 CRC64;
MITIPYLTAV STYFSYGLLF AFGQLRDFFR RFIDWWFTSN LQGYAPICLG HEDFYIRRLY
HRIQDCFERP ISSAPDAWFD VVERYSNDNN KTLKRTTKTS RCLNLGSYNY LGFGSFDEYC
TPRVIESLKK FSASTCSSRV DAGTTSVHAE LEECVTRFVG KPAAVVFGMG YATNSAIIPV
LIGKGGLIIS DSLNHSSIVN GARGSGATIR VFQHNTPSHL ERVLREQIAE GQPRTHRPWK
KIIVVVEGIY SMEGEICHLP EVVAICKKYK AYVYLDEAHS IGAIGKTGKG ICELLGVDTA
DVDVMMGTFT KSFGSCGGYI AGSKELIQYL KHQCPAHLYA TSIPTPSAQQ IISAIKVILG
EDGSNRGAQK LARIRENSNF FRAELQKMGF EVLGDNDSPV MPIMLYNPAK IPAFSRECLR
QKVAVVVVGF PATPLLLARA RICISASHSR EDLIRALKVI SKVGDLSGIK YFPAEPKKIE
QSKNDIKLD


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Pathways :
WP1996: Linoleate Biosynthesis
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP2434: very-long-chain-fatty-acid-biosynthesis
WP1502: Mitochondrial biogenesis
WP1625: Base excision repair
WP1647: Fatty acid biosynthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation
WP1685: Peptidoglycan biosynthesis
WP1708: Terpenoid backbone biosynthesis
WP1002: Electron Transport Chain
WP102: Heme Biosynthesis
WP1020: Fatty Acid Biosynthesis
WP1024: Steroid Biosynthesis
WP103: Cholesterol Biosynthesis
WP1049: G Protein Signaling Pathways
WP1070: Cholesterol Biosynthesis
WP1086: Heme Biosynthesis
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP1139: Fatty Acid Biosynthesis
WP114: Core lipid-linked oligosaccharide biosynthesis
WP1143: Steroid Biosynthesis
WP1165: G Protein Signaling Pathways

Related Genes :
[LCB2a LCB2 At5g23670 MQM1.6] Long chain base biosynthesis protein 2a (AtLCB2a) (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (AtLCB2)
[LCB2b LCB2.2 SPT1 At3g48780 T21J18_50] Long chain base biosynthesis protein 2b (AtLCB2b) (EC 2.3.1.50) (Serine palmitoyltransferase 1) (AtSPT1)
[Sptlc2 Lcb2] 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)
[SPTLC2 KIAA0526 LCB2] 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)
[ACSM2A ACSM2 MACS2] Acyl-coenzyme A synthetase ACSM2A, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 2A) (Butyrate--CoA ligase 2A) (Butyryl-coenzyme A synthetase 2A) (Middle-chain acyl-CoA synthetase 2A)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[Acot3 Pte1a Pte2 Pte2a] Acyl-coenzyme A thioesterase 3 (Acyl-CoA thioesterase 3) (EC 3.1.2.2) (PTE-Ia) (Peroxisomal acyl-coenzyme A thioester hydrolase 2a) (Peroxisomal long-chain acyl-CoA thioesterase 2)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[SPTLC3 C20orf38 SPTLC2L] Serine palmitoyltransferase 3 (EC 2.3.1.50) (Long chain base biosynthesis protein 2b) (LCB2b) (Long chain base biosynthesis protein 3) (LCB 3) (Serine-palmitoyl-CoA transferase 3) (SPT 3)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[LCB1 EMB2779 FBR11 At4g36480 AP22 C7A10.880] Long chain base biosynthesis protein 1 (AtLCB1) (EC 2.3.1.50) (Protein EMBRYO DEFECTIVE 2779) (Protein FUMONISIN B1 RESISTANT 11)
[ospF mkaD CP0010 pWR501_0013 SFLP011] Phosphothreonine lyase OspF (EC 4.2.3.-) (Effector protein OspF)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

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