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Genome polyprotein [Cleaved into: Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 3)] (Fragments)

 POLG_DEN2T              Reviewed;        1683 AA.
P27914;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
20-JUN-2018, entry version 140.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Non-structural protein 3;
Flags: Fragments;
Dengue virus type 2 (strain Tonga/EKB194/1974) (DENV-2).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=11067;
NCBI_TaxID=53540; Aedimorphus.
NCBI_TaxID=53539; Diceromyia.
NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=53541; Stegomyia.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-495.
PubMed=2216784; DOI=10.1093/nar/18.19.5889;
Chen W., Maguire T.;
"Nucleotide sequence of the envelope glycoprotein gene of a dengue-2
virus isolated during an epidemic of benign dengue fever in Tonga in
1974.";
Nucleic Acids Res. 18:5889-5889(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 496-1683.
Qu X., Chen W., Maguire T.;
Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
[3]
STRUCTURE BY ELECTRON MICROSCOPY (12.5 ANGSTROMS) OF 1-395, AND X-RAY
CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-395.
PubMed=15341726; DOI=10.1016/j.str.2004.06.019;
Zhang Y., Zhang W., Ogata S., Clements D., Strauss J.H., Baker T.S.,
Kuhn R.J., Rossmann M.G.;
"Conformational changes of the flavivirus E glycoprotein.";
Structure 12:1607-1618(2004).
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particle is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the
polyprotein, is targeted to three destinations: the viral
replication cycle, the plasma membrane and the extracellular
compartment. Essential for viral replication. Required for
formation of the replication complex and recruitment of other non-
structural proteins to the ER-derived membrane structures.
Excreted as a hexameric lipoparticle that plays a role against
host immune response. Antagonizing the complement function. Binds
to the host macrophages and dendritic cells. Inhibits signal
transduction originating from Toll-like receptor 3 (TLR3).
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Non-structural protein 1: Disrupts the host endothelial
glycocalyx layer of host pulmonary microvascular endothelial
cells, inducing degradation of sialic acid and shedding of heparan
sulfate proteoglycans. NS1 induces expression of sialidases,
heparanase, and activates cathepsin L, which activates heparanase
via enzymatic cleavage. These effects are probably linked to the
endothelial hyperpermeability observed in severe dengue disease.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: Serine protease NS3: Displays three enzymatic
activities: serine protease, NTPase and RNA helicase. NS3 serine
protease, in association with NS2B, performs its autocleavage and
cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
{ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
in which each of the Xaa can be either Arg or Lys and Yaa can be
either Ser or Ala.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
with host EXOC1 (via C-terminus); this interaction results in
EXOC1 degradation through the proteasome degradation pathway.
Protein prM: Forms heterodimers with envelope protein E in the
endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
the endoplasmic reticulum and Golgi. Interacts with protein prM.
Interacts with non-structural protein 1. Non-structural protein 1:
Homodimer; Homohexamer when secreted. Interacts with envelope
protein E. Non-structural protein 2A: Interacts (via N-terminus)
with serine protease NS3. Non-structural protein 2B: Forms a
heterodimer with serine protease NS3. May form homooligomers.
Serine protease NS3: Forms a heterodimer with NS2B. Interacts with
NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase
NS5; this interaction stimulates RNA-directed RNA polymerase NS5
guanylyltransferase activity. {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane; Peripheral membrane protein; Lumenal side
{ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
Peripheral membrane protein {ECO:0000255|PROSITE-
ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
ProRule:PRU00860}. Note=Remains non-covalently associated to
serine protease subunit NS2B. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M
and envelope protein E contain an endoplasmic reticulum retention
signal. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Cleavages in the lumen of endoplasmic
reticulum are performed by host signal peptidase, wereas cleavages
in the cytoplasmic side are performed by the Serine protease NS3.
Signal cleavage at the 2K-4B site requires a prior NS3 protease-
mediated cleavage at the 4A-2K site.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated. The excreted form
is glycosylated and this is required for efficient secretion of
the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Cleavages in the lumen of endoplasmic
reticulum are performed by host signal peptidase, wereas cleavages
in the cytoplasmic side are performed by serine protease NS3.
Signal cleavage at the 2K-4B site requires a prior NS3 protease-
mediated cleavage at the 4A-2K site.
{ECO:0000250|UniProtKB:P17763}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
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EMBL; X54319; CAA38217.1; -; Genomic_RNA.
EMBL; X57469; CAA40705.1; -; Genomic_RNA.
EMBL; X57468; CAA40704.1; -; Genomic_RNA.
PIR; PQ0507; PQ0507.
PIR; S11482; S11482.
PDB; 1TG8; X-ray; 2.61 A; A=1-395.
PDB; 1TGE; EM; 12.50 A; A/B/C=1-395.
PDBsum; 1TG8; -.
PDBsum; 1TGE; -.
ProteinModelPortal; P27914; -.
SMR; P27914; -.
DrugBank; DB04473; Alpha-L-Fucose.
PRIDE; P27914; -.
EvolutionaryTrace; P27914; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; 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:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 3.
Gene3D; 3.30.387.10; -; 2.
Gene3D; 3.30.67.10; -; 4.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF00949; Peptidase_S7; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Capsid protein;
Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host endoplasmic reticulum; Host membrane; Host-virus interaction;
Hydrolase; Membrane; Nucleotide-binding; Protease; Secreted;
Serine protease; Suppressor of RNA silencing; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral nucleoprotein;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
CHAIN <1 >1683 Genome polyprotein.
/FTId=PRO_0000405219.
CHAIN 1 495 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037980.
CHAIN 496 847 Non-structural protein 1.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037981.
CHAIN 848 1065 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000308290.
CHAIN 1066 1683 Serine protease NS3.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037983.
TOPO_DOM <1 445 Extracellular. {ECO:0000255}.
TRANSMEM 446 466 Helical. {ECO:0000255}.
TOPO_DOM 467 472 Cytoplasmic. {ECO:0000255}.
TRANSMEM 473 493 Helical. {ECO:0000255}.
TOPO_DOM 494 915 Extracellular. {ECO:0000255}.
TRANSMEM 916 940 Helical. {ECO:0000255}.
TOPO_DOM 941 946 Cytoplasmic. {ECO:0000255}.
TRANSMEM 947 965 Helical. {ECO:0000255}.
TOPO_DOM 966 989 Lumenal. {ECO:0000255}.
TRANSMEM 990 1010 Helical. {ECO:0000255}.
TOPO_DOM 1011 1011 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1012 1030 Helical. {ECO:0000255}.
TOPO_DOM 1031 1037 Lumenal. {ECO:0000255}.
TRANSMEM 1038 1058 Helical. {ECO:0000255}.
TOPO_DOM 1059 >1683 Cytoplasmic. {ECO:0000255}.
DOMAIN 1066 1243 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1245 1401 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1411 1582 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 1258 1265 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 98 111 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1249 1252 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1349 1352 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
ACT_SITE 1116 1116 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1140 1140 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1200 1200 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
SITE 495 496 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 847 848 Cleavage; by host.
{ECO:0000250|UniProtKB:P29990}.
SITE 1065 1066 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P29990}.
SITE 1522 1522 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1525 1525 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 702 702 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 3 30 {ECO:0000250|UniProtKB:P17763}.
DISULFID 60 121 {ECO:0000250|UniProtKB:P17763}.
DISULFID 74 105 {ECO:0000250|UniProtKB:P17763}.
DISULFID 92 116 {ECO:0000250|UniProtKB:P17763}.
DISULFID 185 285 {ECO:0000250|UniProtKB:P17763}.
DISULFID 302 333 {ECO:0000250|UniProtKB:P17763}.
DISULFID 499 510 {ECO:0000250|UniProtKB:P17763}.
DISULFID 550 638 {ECO:0000250|UniProtKB:P17763}.
DISULFID 674 718 {ECO:0000250|UniProtKB:P17763}.
DISULFID 775 824 {ECO:0000250|UniProtKB:P17763}.
DISULFID 786 808 {ECO:0000250|UniProtKB:P17763}.
DISULFID 807 811 {ECO:0000250|UniProtKB:P17763}.
NON_CONS 1065 1066 {ECO:0000305}.
NON_TER 1 1
NON_TER 1683 1683
TURN 2 5 {ECO:0000244|PDB:1TG8}.
STRAND 7 13 {ECO:0000244|PDB:1TG8}.
STRAND 20 24 {ECO:0000244|PDB:1TG8}.
STRAND 30 34 {ECO:0000244|PDB:1TG8}.
STRAND 36 38 {ECO:0000244|PDB:1TG8}.
STRAND 41 50 {ECO:0000244|PDB:1TG8}.
STRAND 55 72 {ECO:0000244|PDB:1TG8}.
STRAND 75 77 {ECO:0000244|PDB:1TG8}.
HELIX 83 85 {ECO:0000244|PDB:1TG8}.
STRAND 90 100 {ECO:0000244|PDB:1TG8}.
HELIX 101 103 {ECO:0000244|PDB:1TG8}.
STRAND 109 128 {ECO:0000244|PDB:1TG8}.
STRAND 135 143 {ECO:0000244|PDB:1TG8}.
TURN 148 152 {ECO:0000244|PDB:1TG8}.
STRAND 159 164 {ECO:0000244|PDB:1TG8}.
STRAND 171 175 {ECO:0000244|PDB:1TG8}.
TURN 176 178 {ECO:0000244|PDB:1TG8}.
STRAND 179 186 {ECO:0000244|PDB:1TG8}.
HELIX 193 195 {ECO:0000244|PDB:1TG8}.
STRAND 196 201 {ECO:0000244|PDB:1TG8}.
STRAND 204 209 {ECO:0000244|PDB:1TG8}.
HELIX 210 214 {ECO:0000244|PDB:1TG8}.
STRAND 220 222 {ECO:0000244|PDB:1TG8}.
HELIX 234 237 {ECO:0000244|PDB:1TG8}.
STRAND 238 241 {ECO:0000244|PDB:1TG8}.
STRAND 249 252 {ECO:0000244|PDB:1TG8}.
HELIX 257 263 {ECO:0000244|PDB:1TG8}.
TURN 264 266 {ECO:0000244|PDB:1TG8}.
STRAND 273 276 {ECO:0000244|PDB:1TG8}.
STRAND 284 288 {ECO:0000244|PDB:1TG8}.
STRAND 306 310 {ECO:0000244|PDB:1TG8}.
STRAND 320 326 {ECO:0000244|PDB:1TG8}.
STRAND 332 334 {ECO:0000244|PDB:1TG8}.
STRAND 337 340 {ECO:0000244|PDB:1TG8}.
STRAND 346 353 {ECO:0000244|PDB:1TG8}.
STRAND 365 370 {ECO:0000244|PDB:1TG8}.
STRAND 373 381 {ECO:0000244|PDB:1TG8}.
STRAND 383 385 {ECO:0000244|PDB:1TG8}.
STRAND 387 393 {ECO:0000244|PDB:1TG8}.
SEQUENCE 1683 AA; 187440 MW; 3B0438D96196BFC8 CRC64;
MRCIGISNRD FVEGVSGGSW VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC
IEAKLTNTTT DSRCPTQGEP TLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT
CKKNMEGKIV QPENLEYTVV ITPHSGEEHA VGNDTGKHGK EVKITPQSSI TEAELTGYGT
VTMECSPRTG LDFNEMVLLQ MEDKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF
KNPHAKKQDV VVLGSQEGAM HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS
MCTGKFKIVK EIAETQHGTI VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE
KDSPVNIEAE PPFGDSYIII GVEPGQLKLD WFKKGSSIGQ MFETTMRGAK RMAILGDTAW
DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV
LVGIVTLYLG VMVQADSGCV VSWKNKELKC GSGIFVTDNV HTWTEQYKFQ PESPSKLASA
IQKAHEEGIC GIRSVTRLEN LMWKQITSEL NHILSENEVK LTIMTGDIKG IMQVGKRSLR
PQPTELRYSW KTWGKAKMLS TELHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT
NIWLRLREKQ DVFCDSKLMS AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW
PKSHTLWSNG VLESEMVIPK NFAGPVSQHN NRPGYYTQTA GPWHLGKLEM DFDFCEGTTV
VVTEDCGNRG PSLRTTTASG KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL
VSSLVTAGHG QIDNFSLGIL GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL
GRVMVMVGAT MTDDIGMGVT YLALLAAFRV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ
SSIPETILEL TDALALGMMV LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA
VVSVSPLLLT SSQQKADWIP LALTIKGLNP TAIFLTTLSR TSKKRAGVLW DVPSPPPVGK
AELEDGAYRI KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD
LISYGGGWKL EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FRTNTGTIGA VSLDFSPGTS
GSPIVDKKGK VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP
GAGKTKRYLP AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE
IVDLMCHATF TMRLLSPIRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT
ATPPGSRDPF PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KTGNDIAACL
RKNGKRVIQL SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT
DGEERVILAG PMPVTHSSAA QRRGRIGRNP RNENDQYIYM GEPLENDEDC AHWKEAKMLL
DNINTPEGII PSIFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYKVAAEGI
NYADRRWCFD GTRNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA
GRK


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10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 0.5 mg
MCA4688 MOUSE ANTI INFLUENZA A NON STRUCTURAL PROTEIN , Product Type Monoclonal Antibody, Specificity INFLUENZA A NON STRUCTURAL PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2 0.2 mg
SCH-MCA4688 MOUSE ANTI INFLUENZA A NON STRUCTURAL PROTEIN , Product Type Monoclonal Antibody, Specificity INFLUENZA A NON STRUCTURAL PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2 0.2 mg
OBT1772 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human; WB 0.1 mg.
OBT1773 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB 0.1 mg.
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
20-272-190412 Filensin - Mouse monoclonal [FIL - 7B10] to Filensin; Beaded filament structural protein 1; Lens fiber cell beaded-filament structural protein CP 115; CP115; Lens intermediate filament-like heavy; LIF 0.1 ml
25-030 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. This gene encodes a protein that contains a tetr 0.05 mg
EIAAB38762 Cape,Chromosome-associated protein E,FGF-inducible protein 16,Fin16,Mouse,Mus musculus,SMC protein 2,Smc2,SMC-2,Smc2l1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
27-617 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. 0.1 mg
EIAAB38761 CAPE,Chromosome-associated protein E,hCAP-E,Homo sapiens,Human,PRO0324,SMC protein 2,SMC2,SMC-2,SMC2L1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
EIAAB38770 Kiaa0594,MLZ-453,Mouse,mSMC5,Mus musculus,Protein expressed in male leptotene and zygotene spermatocytes 453,SMC protein 5,Smc5,SMC-5,Smc5l1,Structural maintenance of chromosomes protein 5
EIAAB12958 Envelope polyprotein,EnvK2 protein,ERVK6,HERV-K(C7) envelope protein,HERV-K(HML-2.HOM) envelope protein,HERV-K_7p22.1 provirus ancestral Env polyprotein,HERV-K108 envelope protein,Homo sapiens,Human
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 1 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.1 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.5 mg
EIAAB38758 Mouse,Mus musculus,SMC protein 1B,Smc1b,SMC-1B,SMC-1-beta,Smc1l2,Structural maintenance of chromosomes protein 1B
EIAAB38757 Rat,Rattus norvegicus,SMC protein 1A,Smc1,Smc1a,SMC-1A,Smc1l1,Structural maintenance of chromosomes protein 1A
EIAAB38754 Bos taurus,Bovine,SMC protein 1A,SMC1,SMC1A,SMC-1A,SMC1L1,Structural maintenance of chromosomes protein 1A
orb81767 Measles Virus Non-Structural C-Protein (1-51) protein Proteins 100
EIAAB38755 Chromosome segregation protein SmcB,Mouse,Mus musculus,Sb1.8,Sb1.8,SMC protein 1A,Smc1,Smc1a,SMC-1A,SMC-1-alpha,Smc1l1,Smcb,Structural maintenance of chromosomes protein 1A


 

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