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 POLG_BVDVC              Reviewed;        3907 AA.
Q96662;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 140.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=N-terminal protease;
Short=N-pro;
EC=3.4.22.-;
AltName: Full=Autoprotease p20;
Contains:
RecName: Full=Capsid protein C;
Contains:
RecName: Full=E(rns) glycoprotein;
AltName: Full=gp44/48;
Contains:
RecName: Full=Envelope glycoprotein E1;
AltName: Full=gp33;
Contains:
RecName: Full=Envelope glycoprotein E2;
AltName: Full=gp55;
Contains:
RecName: Full=p7;
Contains:
RecName: Full=Non-structural protein 2-3;
Contains:
RecName: Full=Cysteine protease NS2;
EC=3.4.22.-;
AltName: Full=Non-structural protein 2;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.113;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=Non-structural protein 5A;
Short=NS5A;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=NS5B;
Bovine viral diarrhea virus (strain CP7) (BVDV) (Mucosal disease
virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Pestivirus.
NCBI_TaxID=268305;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8970985;
Meyers G., Tautz N., Becher P., Thiel H., Kuemmerer B.M.;
"Recovery of cytopathogenic and noncytopathogenic bovine viral
diarrhea viruses from cDNA constructs.";
J. Virol. 70:8606-8613(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate CP7-5A;
PubMed=10933696; DOI=10.1128/JVI.74.17.7884-7894.2000;
Becher P., Orlich M., Thiel H.-J.;
"Mutations in the 5' nontranslated region of bovine viral diarrhea
virus result in altered growth characteristics.";
J. Virol. 74:7884-7894(2000).
[3]
PROTEIN SEQUENCE OF 1067-1083, AND PROTEOLYTIC PROCESSING OF
POLYPROTEIN.
PubMed=8648755;
Elbers K., Tautz N., Becher P., Stoll D., Ruemenapf T., Thiel H.-J.;
"Processing in the pestivirus E2-NS2 region: identification of
proteins p7 and E2p7.";
J. Virol. 70:4131-4135(1996).
[4]
PROTEIN SEQUENCE OF 2282-2289; 2693-2705 AND 3189-3202, AND
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=9188613;
Tautz N., Elbers K., Stoll D., Meyers G., Thiel H.-J.;
"Serine protease of pestiviruses: determination of cleavage sites.";
J. Virol. 71:5415-5422(1997).
[5]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=11000219; DOI=10.1128/JVI.74.20.9498-9506.2000;
Harada T., Tautz N., Thiel H.-J.;
"E2-p7 region of the bovine viral diarrhea virus polyprotein:
processing and functional studies.";
J. Virol. 74:9498-9506(2000).
[6]
CLEAVAGE BETWEEN NS2 AND NS3, AND ACTIVE SITES OF NS2 PROTEASE.
STRAIN=CP7, and NCP7;
PubMed=15367643; DOI=10.1128/JVI.78.19.10765-10775.2004;
Lackner T., Mueller A., Pankraz A., Becher P., Thiel H.-J.,
Gorbalenya A.E., Tautz N.;
"Temporal modulation of an autoprotease is crucial for replication and
pathogenicity of an RNA virus.";
J. Virol. 78:10765-10775(2004).
[7]
SUBCELLULAR LOCATION OF E(RNS) GLYCOPROTEIN, AND MUTAGENESIS OF
GLU-438; GLN-446; GLY-455; LEU-460; GLU-461; SER-462; GLN-465;
LYS-469; THR-471; TRP-473; ARG-476; LEU-478; LEU-481; GLU-486;
ASN-487; SER-489 AND TRP-492.
PubMed=17848558; DOI=10.1074/jbc.M706803200;
Tews B.A., Meyers G.;
"The pestivirus glycoprotein Erns is anchored in plane in the membrane
via an amphipathic helix.";
J. Biol. Chem. 282:32730-32741(2007).
-!- FUNCTION: Initial binding to target cell probably involves
interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are
responsible of cell attachment with CD46 and subsequent fusion
after internalization of the virion by endocytosis (By
similarity). {ECO:0000250}.
-!- FUNCTION: P7 forms a leader sequence to properly orient NS2 in the
membrane. {ECO:0000250}.
-!- FUNCTION: Uncleaved NS2-3 is required for production of infectious
virus.
-!- FUNCTION: NS2 protease seems to play a vital role in viral RNA
replication control and in the pathogenicity of the virus.
-!- FUNCTION: NS3 displays three enzymatic activities: serine
protease, NTPase and RNA helicase.
-!- FUNCTION: NS4A is a cofactor for the NS3 protease activity.
{ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase NS5 replicates the viral (+)
and (-) genome.
-!- CATALYTIC ACTIVITY: Leu is conserved at position P1 for all four
cleavage sites. Alanine is found at position P1' of the NS4A-NS4B
cleavage site, whereas serine is found at position P1' of the NS3-
NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: The E(rns) glycoprotein is found as a homodimer;
disulfide-linked. The E1 and E2 envelope glycoproteins form
disulfide-linked homodimers as well as heterodimers.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: E(rns) glycoprotein: Host membrane;
Peripheral membrane protein. Virion membrane; Peripheral membrane
protein {ECO:0000305}. Note=The C-terminus membrane anchor of Erns
represents an amphipathic helix embedded in plane into the
membrane. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Host cell surface
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cysteine protease NS2: Host membrane
{ECO:0000255|PROSITE-ProRule:PRU01029}; Multi-pass membrane
protein {ECO:0000255|PROSITE-ProRule:PRU01029}.
-!- PTM: The E(rns) glycoprotein is heavily glycosylated.
{ECO:0000250}.
-!- PTM: The viral RNA of pestiviruses is expressed as a single
polyprotein which undergoes post-translational proteolytic
processing resulting in the production of at least eleven
individual proteins. The N-terminal protease cleaves itself from
the nascent polyprotein autocatalytically and thereby generates
the N-terminus of the adjacent viral capsid protein C (By
similarity). {ECO:0000250}.
-!- PTM: Cleavage between E2 and p7 is partial.
-!- MISCELLANEOUS: BVDV is divided in two types: cytopathic and non-
cytopathic. Both types of viruses can be found in animals
suffering from mucosal disease, as a cytopathic BVDV can develop
from a non-cytopathic virus within the infected animal by
deletions, mutations or insertions. Both types express uncleaved
NS2-3, but cytopathic strains also express NS3.
-!- SIMILARITY: Belongs to the pestivirus polyprotein family.
{ECO:0000305}.
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EMBL; U63479; AAC55984.1; -; Genomic_RNA.
EMBL; AF220247; AAG00378.1; -; Genomic_RNA.
PDB; 2AJJ; NMR; -; A=2693-2720.
PDB; 2AJM; NMR; -; A=2693-2720.
PDB; 2AJN; NMR; -; A=2693-2720.
PDB; 2AJO; NMR; -; A=2693-2720.
PDB; 2CJQ; X-ray; 2.60 A; A=3189-3907.
PDB; 4DVK; X-ray; 2.21 A; A/B=271-435.
PDB; 4DVL; X-ray; 2.75 A; A/B=271-435.
PDB; 4DVN; X-ray; 2.38 A; A/B=271-435.
PDB; 4DW3; X-ray; 2.35 A; A/B=271-435.
PDB; 4DW4; X-ray; 2.23 A; A/B=271-435.
PDB; 4DW5; X-ray; 2.21 A; A/B=271-435.
PDB; 4DW7; X-ray; 3.08 A; A/B=271-435.
PDB; 4DWA; X-ray; 3.01 A; A/B=271-435.
PDB; 4DWC; X-ray; 2.89 A; A/B=271-435.
PDBsum; 2AJJ; -.
PDBsum; 2AJM; -.
PDBsum; 2AJN; -.
PDBsum; 2AJO; -.
PDBsum; 2CJQ; -.
PDBsum; 4DVK; -.
PDBsum; 4DVL; -.
PDBsum; 4DVN; -.
PDBsum; 4DW3; -.
PDBsum; 4DW4; -.
PDBsum; 4DW5; -.
PDBsum; 4DW7; -.
PDBsum; 4DWA; -.
PDBsum; 4DWC; -.
ProteinModelPortal; Q96662; -.
SMR; Q96662; -.
IntAct; Q96662; 1.
BindingDB; Q96662; -.
ChEMBL; CHEMBL3937; -.
TCDB; 1.A.53.1.5; the hepatitis c virus p7 viroporin cation-selective channel (hcv-p7) family.
OrthoDB; VOG09000032; -.
EvolutionaryTrace; Q96662; -.
PMAP-CutDB; Q96662; -.
Proteomes; UP000007618; Genome.
Proteomes; UP000173611; Genome.
GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00079; HELICc; 1.
InterPro; IPR021824; Capsid-C_pestivirus.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR022120; NS2.
InterPro; IPR030399; NS2_C74.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008751; Peptidase_C53.
InterPro; IPR032521; Pestivirus_E2.
InterPro; IPR000280; Pestivirus_NS3_S31.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002166; RNA_pol_HCV.
InterPro; IPR036430; RNase_T2-like_sf.
InterPro; IPR033130; RNase_T2_His_AS_2.
Pfam; PF11889; DUF3409; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF05550; Peptidase_C53; 1.
Pfam; PF12387; Peptidase_C74; 1.
Pfam; PF05578; Peptidase_S31; 1.
Pfam; PF16329; Pestivirus_E2; 1.
Pfam; PF00998; RdRP_3; 1.
PRINTS; PR00729; CDVENDOPTASE.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55895; SSF55895; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS00531; RNASE_T2_2; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Direct protein sequencing; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host membrane; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host IRF3 by virus;
Inhibition of host RLR pathway by virus; Ion channel; Ion transport;
Membrane; Nucleotide-binding; Nucleotidyltransferase; Protease;
RNA-directed RNA polymerase; Serine protease; Thiol protease;
Transferase; Transmembrane; Transmembrane helix; Transport;
Viral attachment to host cell; Viral immunoevasion; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 168 N-terminal protease. {ECO:0000250}.
/FTId=PRO_0000038011.
CHAIN 169 270 Capsid protein C. {ECO:0000250}.
/FTId=PRO_0000038012.
CHAIN 271 497 E(rns) glycoprotein. {ECO:0000250}.
/FTId=PRO_0000038013.
CHAIN 498 659 Envelope glycoprotein E1. {ECO:0000250}.
/FTId=PRO_0000038014.
CHAIN 660 1066 Envelope glycoprotein E2. {ECO:0000250}.
/FTId=PRO_0000038015.
CHAIN 1067 1136 p7.
/FTId=PRO_0000038016.
CHAIN 1137 2281 Non-structural protein 2-3.
{ECO:0000250}.
/FTId=PRO_0000038017.
CHAIN 1137 1598 Cysteine protease NS2.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
/FTId=PRO_0000038018.
CHAIN 1599 2281 Serine protease NS3. {ECO:0000250}.
/FTId=PRO_0000038019.
CHAIN 2282 2345 Non-structural protein 4A.
/FTId=PRO_0000038020.
CHAIN 2346 2692 Non-structural protein 4B.
/FTId=PRO_0000038021.
CHAIN 2693 3188 Non-structural protein 5A.
/FTId=PRO_0000038022.
CHAIN 3189 3907 RNA-directed RNA polymerase.
/FTId=PRO_0000038023.
TRANSMEM 1144 1164 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1189 1209 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1217 1237 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1247 1267 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1281 1301 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1369 1389 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1577 1597 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
DOMAIN 1 168 Peptidase C53.
DOMAIN 1450 1598 Peptidase C74. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
DOMAIN 1599 1772 Peptidase S31. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
DOMAIN 1811 1969 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1987 2152 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 3527 3650 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
COMPBIAS 1432 1435 Poly-Glu.
COMPBIAS 3268 3271 Poly-Glu.
ACT_SITE 22 22 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046}.
ACT_SITE 49 49 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046}.
ACT_SITE 69 69 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046}.
ACT_SITE 1456 1456 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029,
ECO:0000269|PubMed:15367643}.
ACT_SITE 1470 1470 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029,
ECO:0000269|PubMed:15367643}.
ACT_SITE 1521 1521 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029,
ECO:0000269|PubMed:15367643}.
ACT_SITE 1667 1667 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
ACT_SITE 1704 1704 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
ACT_SITE 1761 1761 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
SITE 168 169 Cleavage; by autolysis. {ECO:0000250}.
SITE 270 271 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 497 498 Cleavage. {ECO:0000250}.
SITE 659 660 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1066 1067 Cleavage; by host signal peptidase;
partial.
SITE 1136 1137 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1598 1599 Cleavage; by NS2; in cytopathic strains.
{ECO:0000250}.
SITE 2281 2282 Cleavage; by serine protease NS3.
SITE 2345 2346 Cleavage; by serine protease NS3.
SITE 2692 2693 Cleavage; by serine protease NS3.
SITE 3188 3189 Cleavage; by serine protease NS3.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 487 487 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 597 597 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 809 809 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 878 878 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 922 922 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 990 990 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1366 1366 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1428 1428 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1460 1460 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1722 1722 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2143 2143 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2226 2226 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2503 2503 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2691 2691 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2900 2900 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3697 3697 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3802 3802 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
MUTAGEN 438 438 E->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 446 446 Q->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 455 455 G->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 460 460 L->A: Reduced membrane association of
E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 461 461 E->A: Greatly reduced membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 462 462 S->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 465 465 Q->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 469 469 K->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 471 471 T->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 473 473 W->A: Reduced membrane association of
E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 476 476 R->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 478 478 L->A: Reduced membrane association of
E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 481 481 L->A: Reduced membrane association of
E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 486 486 E->A: Greatly reduced membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 487 487 N->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 489 489 S->A: Almost no effect on membrane
association of E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
MUTAGEN 492 492 W->A: Reduced membrane association of
E(rns) glycoprotein.
{ECO:0000269|PubMed:17848558}.
STRAND 273 278 {ECO:0000244|PDB:4DVK}.
HELIX 286 293 {ECO:0000244|PDB:4DVK}.
STRAND 297 303 {ECO:0000244|PDB:4DVK}.
HELIX 318 322 {ECO:0000244|PDB:4DVK}.
HELIX 332 334 {ECO:0000244|PDB:4DVK}.
HELIX 340 349 {ECO:0000244|PDB:4DVK}.
HELIX 351 354 {ECO:0000244|PDB:4DVK}.
HELIX 357 373 {ECO:0000244|PDB:4DVK}.
STRAND 377 387 {ECO:0000244|PDB:4DVK}.
TURN 388 391 {ECO:0000244|PDB:4DVK}.
STRAND 392 401 {ECO:0000244|PDB:4DVK}.
STRAND 413 416 {ECO:0000244|PDB:4DVK}.
STRAND 419 426 {ECO:0000244|PDB:4DVK}.
HELIX 2697 2718 {ECO:0000244|PDB:2AJJ}.
HELIX 3283 3291 {ECO:0000244|PDB:2CJQ}.
STRAND 3301 3308 {ECO:0000244|PDB:2CJQ}.
HELIX 3325 3334 {ECO:0000244|PDB:2CJQ}.
TURN 3338 3340 {ECO:0000244|PDB:2CJQ}.
TURN 3350 3352 {ECO:0000244|PDB:2CJQ}.
HELIX 3353 3360 {ECO:0000244|PDB:2CJQ}.
HELIX 3372 3380 {ECO:0000244|PDB:2CJQ}.
TURN 3381 3383 {ECO:0000244|PDB:2CJQ}.
HELIX 3386 3388 {ECO:0000244|PDB:2CJQ}.
HELIX 3397 3401 {ECO:0000244|PDB:2CJQ}.
HELIX 3418 3424 {ECO:0000244|PDB:2CJQ}.
HELIX 3426 3438 {ECO:0000244|PDB:2CJQ}.
STRAND 3446 3450 {ECO:0000244|PDB:2CJQ}.
STRAND 3474 3478 {ECO:0000244|PDB:2CJQ}.
HELIX 3480 3494 {ECO:0000244|PDB:2CJQ}.
TURN 3510 3512 {ECO:0000244|PDB:2CJQ}.
HELIX 3513 3521 {ECO:0000244|PDB:2CJQ}.
STRAND 3524 3532 {ECO:0000244|PDB:2CJQ}.
STRAND 3534 3536 {ECO:0000244|PDB:2CJQ}.
HELIX 3537 3540 {ECO:0000244|PDB:2CJQ}.
HELIX 3543 3556 {ECO:0000244|PDB:2CJQ}.
HELIX 3559 3561 {ECO:0000244|PDB:2CJQ}.
HELIX 3562 3572 {ECO:0000244|PDB:2CJQ}.
STRAND 3574 3579 {ECO:0000244|PDB:2CJQ}.
STRAND 3582 3589 {ECO:0000244|PDB:2CJQ}.
HELIX 3598 3618 {ECO:0000244|PDB:2CJQ}.
STRAND 3627 3634 {ECO:0000244|PDB:2CJQ}.
STRAND 3637 3643 {ECO:0000244|PDB:2CJQ}.
HELIX 3644 3661 {ECO:0000244|PDB:2CJQ}.
HELIX 3669 3671 {ECO:0000244|PDB:2CJQ}.
STRAND 3675 3678 {ECO:0000244|PDB:2CJQ}.
HELIX 3679 3681 {ECO:0000244|PDB:2CJQ}.
STRAND 3687 3694 {ECO:0000244|PDB:2CJQ}.
STRAND 3699 3704 {ECO:0000244|PDB:2CJQ}.
HELIX 3707 3715 {ECO:0000244|PDB:2CJQ}.
HELIX 3727 3741 {ECO:0000244|PDB:2CJQ}.
HELIX 3745 3754 {ECO:0000244|PDB:2CJQ}.
STRAND 3765 3773 {ECO:0000244|PDB:2CJQ}.
HELIX 3775 3783 {ECO:0000244|PDB:2CJQ}.
HELIX 3787 3789 {ECO:0000244|PDB:2CJQ}.
STRAND 3790 3793 {ECO:0000244|PDB:2CJQ}.
HELIX 3795 3801 {ECO:0000244|PDB:2CJQ}.
HELIX 3803 3807 {ECO:0000244|PDB:2CJQ}.
HELIX 3815 3828 {ECO:0000244|PDB:2CJQ}.
STRAND 3829 3831 {ECO:0000244|PDB:2CJQ}.
HELIX 3834 3837 {ECO:0000244|PDB:2CJQ}.
HELIX 3839 3845 {ECO:0000244|PDB:2CJQ}.
STRAND 3854 3858 {ECO:0000244|PDB:2CJQ}.
SEQUENCE 3907 AA; 439104 MW; 9E4B019FF8042410 CRC64;
MELITNELLY KTYKQKPAGV EEPVYDQAGN PLFGERGVIH PQSTLKLPHK RGEREVPTNL
ASLPKRGDCR SGNSKGPVSG IYLKPGPLFY QDYKGPVYHR APLEFFEEAS MCETTKRIGR
VTGSDSRLYH IYVCIDGCII VKSATKDRQK VLKWVHNKLN CPLWVSSCSD TKDEGVVRKK
QQKPDRLEKG RMKITPKESE KDSKTKPPDA TIVVDGVKYQ VKKKGKVKSK NTQDGLYHNK
NKPQESRKKL EKALLAWAII ALVFFQVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH
GIWPEKICTG VPSHLATDTE LKAIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW
ILLMNKTQAN LTEGQPLREC AVTCRYDRDS DLNVVTQARD SPTPLTGCKK GKNFSFAGIL
VQGPCNFEIA VSDVLFKEHD CTSVIQDTAH YLVDGMTNSL ESARQGTAKL TTWLGRQLGI
LGKKLENKSK TWFGAYAASP YCEVERKLGY IWYTKNCTPA CLPRNTKIIG PGRFDTNAED
GKILHEMGGH LSEVLLLSVV VLSDFAPETA SVIYLILHFS IPQGHTDIQD CDKNQLNLTV
ELTTAEVIPG SVWNLGKYVC VRPDWWPYET ATVLVIEEVG QVIKVVLRAL KDLTRIWTAA
TTTAFLVCLV KVVRGQVLQG ILWLMLITGA QGYPDCKPGF SYAIAKNDEI GPLGATGLTT
QWYEYSDGMR LQDSVVEVWC KNGEIKYLIR CGREARYLAV LHTRALPTSV VFEKIFDGKE
QEDIVEMDDN FEFGLCPCDA RPLIRGKFNT TLLNGPAFQM VCPIGWTGTV SCTLANKDTL
ATIVVRTYKR VRPFPYRQDC VTQKTIGEDL YDCALGGNWT CVPGDALRYV AGPVESCEWC
GYKFLKSEGL PHFPIGKCRL KNESGYRQVD ETSCNRNGVA IVPSGTVKCK IGDTVVQVIA
MDDKLGPMPC KPHEIISSEG PVEKTACTFN YTRTLKNKYF EPRDNYFQQY MLKGEYQYWF
DLEITDHHRD YFAESLLVIV VALLGGRYVL WLLVTYMILS EQMASGVQYG AGEIVMMGNL
LTHDSVEVVT YFLLLYLLLR EENTKKWVIL IYHIIVMHPL KSVTVILLMV GGMAKAEPGA
QGYLEQVDLS FTMITIIVIG LVIARRDPTV VPLVTIVAAL KITGLGFGPG VDAAMAVLTL
TLLMTSYVTD YFRYKRWIQC ILSLVAGVFL IRTLKHLGEL KTPELTIPNW RPLTFILLYL
TSATVVTRWK IDIAGIFLQG APILLMIATL WADFLTLVLI LPTYELAKLY YLKNVKTDVE
KSWGVPYPDP QTLGGLDYRT IDSVYDVDES GEGVYLFPSR QKKNKNISIL LPLIRATLIS
CISSKWQMVY MAYLTLDFMY YMHRKVIEEI SGSTNVMSRV IAALIELNWS MEEEESKGLK
KFFILSGRLR NLIIKHKVRN QTVASWYGEE EVYGMPKVVT IIRACTLNKN KHCIICTVCE
ARKWKGGNCP KCGRHGKPII CGMTLADFEE RHYKRIFIRE GNFEGPFRQE YNGFVQYTAR
GQLFLRNLPI LATKVKMIMV GNLGEEIGDL EHLGWILRGP AVCKKITEHE KCHVNILDKL
TAFFGVMPRG TTPRAPVRFP TALLKVRRGL ETGWAYTHQG GISSVDHVTA GKDLLVCDSM
GRTRVVCQSN NKLTDETEYG VKTDSGCPDG ARCYVLNPEA VNISGSKGAV VHLQKTGGEF
TCVTASGTPA FFDLKNLKGW SGLPIFEASS GRVVGRVKVG KNEESKPTKL MSGIQTVSKN
TADLTEMVKK ITSMNRGDFR QITLATGAGK TTELPKAVIE EIGRHKRVLV LIPLRAAAES
VYQYMRLKHP SISFNLRIGD MKEGDMATGI TYASYGYFCQ MPQPKLRAAM IEYSYIFLDE
YHCATPEQLA VIGKIHRFSE SIRVVAMTAT PAGSVTTTGQ KHPIEEFIAP EVMKGEDLGS
QFLDIAGLKI PVEEMKGNML VFVPTRNMAV EVAKKLKAKG YNSGYYYSGE DPANLRVVTS
QSPYVVVATN AIESGVTLPD LDTVVDTGLK CEKRVRVSSK IPFIVTGLKR MAVTVGEQAQ
RRGRVGRVKP GRYYRSQETA TGSKDYHYDL LQAQRYGIED GINVTKSFRE MNYDWSLYEE
DSLLITQLEI LNNLLISEDL PAAVKNIMAR TDHPEPIQLA YNSYEVQVPV LFPKIRNGEV
TDTYENYSFL NARKLGEDVP VYVYATEDED LAVDLLGLDW PDPGNQQVVE TGKALKQVVG
LSSAENALLI ALFGYVGYQA LSKRHVPMIT DIYTIEDQRL EDTTHLQYAP NAIRTEGKET
ELKELAVGDL DKIMGSISDY ASEGLNFVRS QAEKMRSAPA FKENVEAAKG YVQKFIDSLI
ENKETIIRYG LWGTHTALYK SIAARLGHET AFATLVIKWL AFGGESVSDH MRQAAVDLVV
YYVINKPSFP GDSETQQEGR RFVASLFISA LATYTYKTWN YNNLSKVVEP ALAYLPYATN
ALKMFTPTRL ESVVILSTTI YKTYLSIRKG KSDGLLGTGI SAAMEILSQN PVSVGISVML
GVGAIAAHNA IESSEQKRTL LMKVFVKNFL DQAATDELVK ENPEKIIMAL FEAVQTIGNP
LRLIYHLYGV YYKGWEAKEL SERTAGRNLF TLIMFEAFEL LGMDSEGKIR NLSGNYVLDL
IYSLHKQINR GLKKIVLGWA PAPFSCDWTP SDERIRLPTN NYLRVETKCP CGYEMKALRN
VGGSLTKVEE KGPFLCRNRL GRGPVNYRVT KYYDDNLKEI KPVAKLEGFV DHYYKGVTAR
IDYGRGKMLL ATDKWEVEHG VVTRLAKRYT GVGFKGAYLG DEPNHRDLVE RDCATITKNT
VQFLKMKKGC AFTYDLTLSN LTRLIELVHK NNLEEKDIPA ATVTTWLAYT FVNEDIGTIK
PVLGERVVTD PVVDVNLQPE VQVDTSEVGI TLVGRAALMT TGTTPVVEKT EPNADGGPSS
IKIGLDEGRY PGPGLQDRTL TDEIHSRDER PFVLVLGSKN SMSNRAKTAR NINLYKGNNP
REIRDLMAQG RMLVVALKDF NPELSELVDF KGTFLDREAL EALSLGRPKS KQVTTATVRE
LLEQEVQVEI PSWFGAGDPV FLEVTLKGDR YHLVGDVDRV KDQAKELGAT DQTRIVKEVG
ARTYTMKLSS WFLQATNKQM SLTPLFEELL LRCPPKIKSN KGHMASAYQL AQGNWEPLDC
GVHLGTIPAR RVKIHPYEAY LKLKDLLEEE EKKPKCRDTV IREHNKWILK KVRHQGNLNT
KKILNPGKLS EQLDREGHKR NIYNNQIGTI MTEAGSRLEK LPVVRAQTDT KSFHEAIRDK
IDKNENQQSP GLHDKLLEIF HTIAQPSLRH TYSDVTWEQL EAGVNRKGAA GFLEKKNVGE
VLDSEKHLVE QLIRDLKTGR KIRYYETAIP KNEKRDVSDD WQSGDLVDEK KPRVIQYPEA
KTRLAITKVM YNWVKQQPVV IPGYEGKTPL FNIFNKVRKE WDLFNEPVAV SFDTKAWDTQ
VTSRDLRLIG EIQKYYYRKE WHKFIDTITD HMVEVPVITA DGEVYIRNGQ RGSGQPDTSA
GNSMLNVLTM MYAFCESTGV PYKSFNRVAR IHVCGDDGFL ITEKGLGLKF ANNGMQILHE
AGKPQKITEG ERMKVAYRFE DIEFCSHTPV PVRWSDNTSS YMAGRDTAVI LSKMATRLDS
SGERGTIAYE KAVAFSFLLM YSWNPLVRRI CLLVLSQQPE TTPSTQTTYY YKGDPIGAYK
DVIGKNLCEL KRTGFEKLAN LNLSLSTLGI WSKHTSKRII QDCVTIGKEE GNWLVNADRL
ISSKTGHLYI PDKGYTLQGK HYEQLQLQAR TSPVTGVGTE RYKLGPIVNL LLRRLRVLLM
AAVGASS


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