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Rhesus theta defensin-1/3 subunit A (RTD-1 subunit A) (RTD-1a) (Demidefensin-2) (RTD-3)

 RTD1A_MACMU             Reviewed;          76 AA.
P82270; Q9TU01;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
16-JAN-2019, entry version 77.
RecName: Full=Rhesus theta defensin-1/3 subunit A;
Short=RTD-1 subunit A;
Short=RTD-1a;
AltName: Full=Demidefensin-2;
AltName: Full=RTD-3;
Flags: Precursor;
Name=RTD1A;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 65-73,
SYNTHESIS OF 65-73, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
DISULFIDE BONDS.
TISSUE=Bone marrow {ECO:0000269|PubMed:10521339}, and
Leukocyte {ECO:0000269|PubMed:10521339};
PubMed=10521339; DOI=10.1126/science.286.5439.498;
Tang Y.-Q., Yuan J., Oesapay G., Oesapay K., Tran D., Miller C.J.,
Ouellette A.J., Selsted M.E.;
"A cyclic antimicrobial peptide produced in primate leukocytes by the
ligation of two truncated alpha-defensins.";
Science 286:498-502(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF RTD-1 AND RTD-3, AND MASS
SPECTROMETRY.
TISSUE=Bone marrow;
PubMed=11527997;
Leonova L., Kokryakov V.N., Aleshina G., Hong T., Nguyen T., Zhao C.,
Waring A.J., Lehrer R.I.;
"Circular minidefensins and posttranslational generation of molecular
diversity.";
J. Leukoc. Biol. 70:461-464(2001).
[3]
PROTEIN SEQUENCE OF 65-73, SYNTHESIS OF RTD-3, FUNCTION OF RTD-1 AND
RTD-3, AND MASS SPECTROMETRY.
TISSUE=Leukocyte;
PubMed=11675394; DOI=10.1074/jbc.M109117200;
Tran D., Tran P.A., Tang Y.-Q., Yuan J., Cole T., Selsted M.E.;
"Homodimeric theta-defensins from rhesus macaque leukocytes:
isolation, synthesis, antimicrobial activities, and bacterial binding
properties of the cyclic peptides.";
J. Biol. Chem. 277:3079-3084(2002).
[4]
STRUCTURE BY NMR OF 65-73, DISULFIDE BOND, SYNTHESIS OF RTD-1, AND
SUBUNIT.
PubMed=23148585; DOI=10.1021/bi301363a;
Conibear A.C., Rosengren K.J., Harvey P.J., Craik D.J.;
"Structural characterization of the cyclic cystine ladder motif of
theta-defensins.";
Biochemistry 51:9718-9726(2012).
-!- FUNCTION: RTD-1 and RTD-3 have similar antimicrobial activities
against the Gram-positive bacteria S.aureus 502A and
L.monocytogenes, the Gram-negative bacteria S.typhimurium and
E.coli ML35, and the fungi C.albicans 16820 and C.neoformans 271A.
{ECO:0000269|PubMed:11675394}.
-!- SUBUNIT: RTD-1 is a cyclic heterodimer composed of subunits A and
B; disulfide-linked (PubMed:23148585). RTD-3 is a cyclic homodimer
composed of two subunits A; disulfide-linked.
{ECO:0000269|PubMed:10521339, ECO:0000269|PubMed:23148585}.
-!- TISSUE SPECIFICITY: RTD-1 is expressed in bone marrow. Detected in
promyelocytes, myelocytes and mature neutrophils and monocytes.
{ECO:0000269|PubMed:10521339}.
-!- DEVELOPMENTAL STAGE: RTD-1 expression begins early during
granulocyte myelopoiesis. {ECO:0000269|PubMed:10521339}.
-!- PTM: Forms a cyclic peptide with subunit A (RTD-3) or with subunit
B (RTD-1). An additional intersubunit disulfide bond is formed.
-!- MASS SPECTROMETRY: Mass=2083.0; Method=MALDI; Range=65-73;
Note=RTD-1, heterodimer, cyclized and oxidized.;
Evidence={ECO:0000269|PubMed:11675394};
-!- MASS SPECTROMETRY: Mass=2076.0; Method=MALDI; Range=65-73;
Note=RTD-3, homodimer, cyclized and oxidized.;
Evidence={ECO:0000269|PubMed:11675394};
-!- MASS SPECTROMETRY: Mass=2087.70; Method=MALDI; Range=65-73;
Note=RTD-1, heterodimer and reduced.;
Evidence={ECO:0000269|PubMed:11527997};
-!- MASS SPECTROMETRY: Mass=2080.48; Method=MALDI; Range=65-73;
Note=RTD-3, homodimer and reduced.;
Evidence={ECO:0000269|PubMed:11527997};
-!- MISCELLANEOUS: RTD-1 is 10-fold more present in cells than RTD-3.
-!- SIMILARITY: Belongs to the alpha-defensin family. Theta subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF191100; AAF04389.1; -; mRNA.
EMBL; AF191102; AAF04391.1; -; Genomic_DNA.
EMBL; AF184157; AAF07924.1; -; mRNA.
PIR; A59089; A59089.
RefSeq; NP_001027989.1; NM_001032817.2.
UniGene; Mmu.3480; -.
PDB; 2LYF; NMR; -; A=65-73.
PDBsum; 2LYF; -.
STRING; 9544.ENSMMUP00000023400; -.
TCDB; 1.C.19.1.6; the defensin (defensin) family.
PRIDE; P82270; -.
GeneID; 574122; -.
KEGG; mcc:574122; -.
CTD; 574122; -.
HOGENOM; HOG000233351; -.
HOVERGEN; HBG079156; -.
InParanoid; P82270; -.
KO; K05230; -.
OrthoDB; 1634035at2759; -.
Proteomes; UP000006718; Unplaced.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
GO; GO:0051673; P:membrane disruption in other organism; IBA:GO_Central.
InterPro; IPR016327; Alpha-defensin_pro.
InterPro; IPR002366; Defensin_propep.
PANTHER; PTHR11876; PTHR11876; 1.
Pfam; PF00879; Defensin_propep; 1.
PIRSF; PIRSF001875; Alpha-defensin; 1.
1: Evidence at protein level;
3D-structure; Antibiotic; Antimicrobial; Complete proteome; Defensin;
Direct protein sequencing; Disulfide bond; Fungicide;
Reference proteome; Signal.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 64 {ECO:0000255,
ECO:0000269|PubMed:10521339}.
/FTId=PRO_0000006871.
PEPTIDE 65 73 Rhesus theta defensin-1/3 subunit A.
/FTId=PRO_0000006872.
PROPEP 74 76 {ECO:0000269|PubMed:10521339}.
/FTId=PRO_0000006873.
DISULFID 66 66 Interchain (with C-66 in subunit A); in
form RTD-3. {ECO:0000269|PubMed:10521339,
ECO:0000269|PubMed:23148585}.
DISULFID 66 66 Interchain (with C-66 in subunit B); in
form RTD-1.
{ECO:0000269|PubMed:10521339}.
DISULFID 68 73 {ECO:0000269|PubMed:10521339,
ECO:0000269|PubMed:23148585}.
CROSSLNK 65 65 Cyclopeptide (Arg-Cys) (interchain with
C-73 in subunit A); in form RTD-3.
CROSSLNK 65 65 Cyclopeptide (Arg-Cys) (interchain with
C-73 in subunit B); in form RTD-1.
CROSSLNK 73 73 Cyclopeptide (Cys-Arg) (interchain with
R-65 in subunit A); in form RTD-3.
CROSSLNK 73 73 Cyclopeptide (Cys-Arg) (interchain with
R-65 in subunit B); in form RTD-1.
CONFLICT 38 38 T -> A (in Ref. 2; AAF07924).
{ECO:0000305}.
CONFLICT 49 49 W -> R (in Ref. 2; published sequence).
{ECO:0000305}.
SEQUENCE 76 AA; 8242 MW; BEA207932A030590 CRC64;
MRTFALLTAM LLLVALHAQA EARQARADEA AAQQQPGTDD QGMAHSFTWP ENAALPLSES
AKGLRCICTR GFCRLL


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Kits Elisa; taq POLYMERASE

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Pathways :
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1644: DNA replication
WP1655: Geraniol degradation
WP1663: Homologous recombination
WP1671: Methane metabolism
WP1672: Mismatch repair
WP1680: Oxidative phosphorylation
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP1711: Trinitrotoluene degradation
WP1718: Vitamin B6 metabolism
WP2272: Pathogenic Escherichia coli infection
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Related Genes :
[RTD1A] Rhesus theta defensin-1/3 subunit A (RTD-1 subunit A) (RTD-1a) (Demidefensin-2) (RTD-3)
[RTD1B] Rhesus theta defensin-1/2 subunit B (RTD-1 subunit B) (RTD-1b) (Demidefensin-1) (RTD-2)
[] 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); 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); 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); 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)]
[] 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); Viroporin 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)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[VMA1 CLS8 TFP1 YDL185W D1286] V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (Vacuolar proton pump subunit A) [Cleaved into: Endonuclease PI-SceI (EC 3.1.-.-) (Sce VMA intein) (VMA1-derived endonuclease) (VDE)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[] 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)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[Cacna1a Caca1a Cach4 Cacn3 Cacnl1a4 Ccha1a] Voltage-dependent P/Q-type calcium channel subunit alpha-1A (Brain calcium channel I) (BI) (Calcium channel, L type, alpha-1 polypeptide isoform 4) (Voltage-gated calcium channel subunit alpha Cav2.1)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[SULT1A3 STM] Sulfotransferase 1A3 (ST1A3) (EC 2.8.2.1) (Aryl sulfotransferase 1A3/1A4) (Catecholamine-sulfating phenol sulfotransferase) (HAST3) (M-PST) (Monoamine-sulfating phenol sulfotransferase) (Placental estrogen sulfotransferase) (Sulfotransferase 1A3/1A4) (Sulfotransferase, monoamine-preferring) (Thermolabile phenol sulfotransferase) (TL-PST)

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