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Lactotransferrin (Lactoferrin) (EC 3.4.21.-)

 TRFL_CAPHI              Reviewed;         708 AA.
Q29477; Q29479;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
16-JAN-2019, entry version 101.
RecName: Full=Lactotransferrin;
Short=Lactoferrin;
EC=3.4.21.-;
Flags: Precursor;
Name=LTF;
Capra hircus (Goat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Capra.
NCBI_TaxID=9925;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=8093048; DOI=10.1006/bbrc.1994.2327;
le Provost F., Nocart M., Guerin G., Martin P.;
"Characterization of the goat lactoferrin cDNA. Assignment of the
relevant locus to bovine U12 synteny group.";
Biochem. Biophys. Res. Commun. 203:1324-1332(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], ANTIBACTERIAL ACTIVITY, AND DEVELOPMENTAL
STAGE.
STRAIN=Korean Native; TISSUE=Mammary gland;
PubMed=9363601; DOI=10.1111/j.1365-2052.1997.00154.x;
Lee T.H., Shimazaki K., Yu S.L., Nam M.S., Kim S.J., Lee K.K.,
Yu D.Y.;
"Polymorphic sequence of Korean Native goat lactoferrin exhibiting
greater antibacterial activity.";
Anim. Genet. 28:367-369(1997).
[3]
X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 20-708 IN COMPLEX WITH IRON.
PubMed=22896884;
Kumar P., Yadav S., Singh T.P.;
"Crystallization and structure determination of goat lactoferrin at
4.0A resolution: A new form of packing in lactoferrins with a high
solvent content in crystals.";
Indian J. Biochem. Biophys. 39:16-21(2002).
-!- FUNCTION: Transferrins are iron binding transport proteins which
can bind two Fe(3+) ions in association with the binding of an
anion, usually bicarbonate.
-!- FUNCTION: Lactotransferrin is a major iron-binding and
multifunctional protein found in exocrine fluids such as breast
milk and mucosal secretions. Has antimicrobial activity.
Antimicrobial properties may include bacteriostasis, which is
related to its ability to sequester free iron and thus inhibit
microbial growth, as well as direct bactericidal properties
leading to the release of lipopolysaccharides from the bacterial
outer membrane. The most effective inhibitory activity is seen
against E.coli and P.aeruginosa. Has anabolic, differentiating and
anti-apoptotic effects on osteoblasts and can also inhibit
osteoclastogenesis, possibly playing a role in the regulation of
bone growth. Interferes with the lipopolysaccharide (LPS)-
stimulated TLR4 signaling, but cannot directly stimulate the TLR4
signaling pathway and subsequent NF-kappa-B activation (By
similarity). {ECO:0000250}.
-!- FUNCTION: The lactotransferrin transferrin-like domain 1 functions
as a serine protease of the peptidase S60 family that cuts
arginine rich regions. This function contributes to the
antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-
Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-
aminomethylcoumarin sites. {ECO:0000250}.
-!- SUBUNIT: Monomer. Found in a complex with LTF, CLU, EPPIN and
SEMG1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}.
Note=Secreted into most exocrine fluids by various endothelial
cells. Stored in the secondary granules of neutrophils (By
similarity). {ECO:0000250}.
-!- DEVELOPMENTAL STAGE: Expressed in mammary glands at various stages
of development, with weak expression detected in virgin goats and
during pregnancy and lactation and high expression detected at the
stage of involution. {ECO:0000269|PubMed:9363601}.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X78902; CAA55517.1; -; mRNA.
EMBL; U53857; AAA97958.1; -; mRNA.
PIR; JC2323; JC2323.
RefSeq; NP_001272477.1; NM_001285548.1.
UniGene; Chi.6573; -.
PDB; 1JW1; X-ray; 4.00 A; A=20-708.
PDBsum; 1JW1; -.
ProteinModelPortal; Q29477; -.
SMR; Q29477; -.
MEROPS; S60.001; -.
PRIDE; Q29477; -.
GeneID; 100861194; -.
KEGG; chx:100861194; -.
CTD; 4057; -.
HOVERGEN; HBG000055; -.
KO; K17283; -.
OrthoDB; 232859at2759; -.
EvolutionaryTrace; Q29477; -.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0042581; C:specific granule; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0019731; P:antibacterial humoral response; ISS:UniProtKB.
GO; GO:0019732; P:antifungal humoral response; ISS:UniProtKB.
GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
GO; GO:0002227; P:innate immune response in mucosa; ISS:UniProtKB.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:2001205; P:negative regulation of osteoclast development; ISS:UniProtKB.
GO; GO:1900229; P:negative regulation of single-species biofilm formation in or on host organism; ISS:UniProtKB.
GO; GO:2000308; P:negative regulation of tumor necrosis factor (ligand) superfamily member 11 production; ISS:UniProtKB.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; ISS:UniProtKB.
GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISS:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISS:UniProtKB.
GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
InterPro; IPR030684; Lactotransferrin.
InterPro; IPR016357; Transferrin.
InterPro; IPR001156; Transferrin-like_dom.
InterPro; IPR018195; Transferrin_Fe_BS.
PANTHER; PTHR11485:SF33; PTHR11485:SF33; 1.
Pfam; PF00405; Transferrin; 2.
PIRSF; PIRSF002549; Transferrin; 1.
PRINTS; PR00422; TRANSFERRIN.
SMART; SM00094; TR_FER; 2.
PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
1: Evidence at protein level;
3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Immunity;
Ion transport; Iron; Iron transport; Metal-binding; Osteogenesis;
Protease; Repeat; Secreted; Serine protease; Signal; Transport.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 708 Lactotransferrin.
/FTId=PRO_0000035730.
DOMAIN 25 352 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 364 693 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
ACT_SITE 92 92 {ECO:0000255|PROSITE-ProRule:PRU00741}.
ACT_SITE 278 278 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 79 79 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 111 111 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 211 211 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 272 272 Iron 1; via tele nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 414 414 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 452 452 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 545 545 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
METAL 614 614 Iron 2; via tele nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:22896884}.
BINDING 140 140 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 142 142 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 143 143 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 478 478 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 482 482 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 484 484 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 485 485 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 495 495 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 564 564 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 64
DISULFID 38 55
DISULFID 134 217
DISULFID 176 192
DISULFID 179 202
DISULFID 189 200
DISULFID 250 264
DISULFID 367 399
DISULFID 377 390
DISULFID 424 703
DISULFID 444 666
DISULFID 476 551
DISULFID 500 694
DISULFID 510 524
DISULFID 521 534
DISULFID 592 606
DISULFID 644 649
CONFLICT 56 56 I -> V (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 88 88 L -> R (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 124 124 Q -> K (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 154 154 F -> P (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 304 304 S -> R (in Ref. 1; CAA55517).
{ECO:0000305}.
CONFLICT 414 414 D -> G (in Ref. 1; CAA55517).
{ECO:0000305}.
SEQUENCE 708 AA; 77358 MW; F2EDA3C83539960D CRC64;
MKLFVPALLS LGALGLCLAA PRKNVRWCAI SLPEWSKCYQ WQRRMRKLGA PSITCIRRTS
ALECIRAIAG KNADAVTLDS GMVFEAGLDP YKLRPVAAEI YGTEKSPQTH YYAVAVVKKG
SNFQLDQLQG QKSCHMGLGR SAGWNIPVGI LRPFLSWTES AEPLQGAVAR FFSASCVPCV
DGKAYPNLCQ LCKGVGENKC ACSSQEPYFG YSGAFKCLQD GAGDVAFVKE TTVFENLPEK
ADRDQYELLC LNNTRAPVDA FKECHLAQVP SHAVVARSVD GKENLIWELL RKAQEKFGKN
KSQSFQLFGS PEGRRDLLFK DSALGFVRIP SKVDSALYLG SRYLTALKNL RETAEELKAR
CTRVVWCAVG PEEQSKCQQW SEQSGQNVTC ATASTTDDCI ALVLKGEADA LSLDGGYIYT
AGKCGLVPVM AENRKSSKYS SLDCVLRPTE GYLAVAVVKK ANEGLTWNSL KGKKSCHTAV
DRTAGWNIPM GLIANQTGSC AFDEFFSQSC APGADPKSSL CALCAGDDQG LDKCVPNSKE
KYYGYTGAFR CLAEDVGDVA FVKNDTVWEN TNGESSADWA KNLNREDFRL LCLDGTTKPV
TEAQSCYLAV APNHAVVSRS DRAAHVEQVL LHQQALFGKN GKNCPDQFCL FKSETKNLLF
NDNTECLAKL GGRPTYEKYL GTEYVTAIAN LKKCSTSPLL EACAFLTR


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Related Genes :
[LTF GIG12 LF] Lactotransferrin (Lactoferrin) (EC 3.4.21.-) (Growth-inhibiting protein 12) (Talalactoferrin) [Cleaved into: Lactoferricin-H (Lfcin-H); Kaliocin-1; Lactoferroxin-A; Lactoferroxin-B; Lactoferroxin-C]
[LTF] Lactotransferrin (Lactoferrin) (EC 3.4.21.-) [Cleaved into: Lactoferricin-B (Lfcin-B)]
[LTF] Lactotransferrin (Lactoferrin) (EC 3.4.21.-) (Fragment)
[LTF] Lactotransferrin (Lactoferrin) (EC 3.4.21.-)
[LTF] Lactotransferrin (Lactoferrin) (EC 3.4.21.-)
[LTF] Lactotransferrin (Lactoferrin) (EC 3.4.21.-)
[LTF] Lactotransferrin (Lactoferrin) (EC 3.4.21.-)
[Ltf] Lactotransferrin (Lactoferrin) (EC 3.4.21.-)
[] 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); 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); 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); 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); 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); 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)]
[Or22b AN12 DOR22A.2 dor67 Or22A.2 CG4231] Odorant receptor 22b
[] 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); 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: 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)]
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[Or22a AN11 DOR22A.1 dor53 Or22A.1 CG12193] Odorant receptor 22a
[] 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); 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: 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)]
[LTF] Lactoferrin (Lactotransferrin)
[pol] 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); 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: Peptide 2k; 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); 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); 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) (NS5)]
[] 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)]
[] 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); 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: 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); 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: 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); 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: 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); 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)]

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