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Structural polyprotein (p110) [Cleaved into: Capsid protein (Coat protein) (C); E2 envelope glycoprotein (Spike glycoprotein E2); E1 envelope glycoprotein (Spike glycoprotein E1)]

 POLS_RUBVV              Reviewed;        1063 AA.
P08564; Q4VDZ6; Q4VE00; Q4VE01; Q4VE02; Q4VE03; Q4VE04; Q4VE05;
Q4VE06; Q4VE07; Q4VE08; Q4VE09; Q4VE10; Q4VE11; Q88780; Q99IE4;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 3.
28-MAR-2018, entry version 83.
RecName: Full=Structural polyprotein;
AltName: Full=p110;
Contains:
RecName: Full=Capsid protein;
AltName: Full=Coat protein;
Short=C;
Contains:
RecName: Full=Spike glycoprotein E2;
AltName: Full=E2 envelope glycoprotein;
Contains:
RecName: Full=Spike glycoprotein E1;
AltName: Full=E1 envelope glycoprotein;
Rubella virus (strain TO-336) (RUBV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Rubivirus.
NCBI_TaxID=376264;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 470-994.
PubMed=3023358;
Nakhasi H.L., Meyer B.C., Liu T.Y.;
"Rubella virus cDNA. Sequence and expression of E1 envelope protein.";
J. Biol. Chem. 261:16616-16621(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11282189; DOI=10.1016/S0264-410X(01)00018-4;
Kakizawa J., Nitta Y., Yamashita T., Ushijima H., Katow S.;
"Mutation of rubella virus vaccine TO-336 strain occurred in the
attenuation process of wild progenitor virus.";
Vaccine 19:2793-2802(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate RVI/Anhui.CHN/00, Isolate RVI/CAL.USA/91,
Isolate RVI/CAL.USA/97, Isolate RVI/ISR/75, Isolate RVI/ISR/79,
Isolate RVI/ISR/88, Isolate RVI/MYS/01, Isolate RVI/PAN/99,
Isolate RVI/SAITAMA.JPN/94, Isolate RVI/SHANDONG.CHN/00,
Isolate RVI/SHANDONG.CHN/02, Isolate RVI/SLV/02, and
Isolate RVI/TOKOYO.JPN/90;
PubMed=15850226;
Icenogle J.P., Abernathy E.S.;
"Standardization of the nomenclature for genetic characteristics of
wild-type rubella viruses.";
Wkly. Epidemiol. Rec. 80:126-132(2005).
-!- FUNCTION: Capsid protein: Capsid protein interacts with genomic
RNA and assembles into icosahedric core particles. The resulting
nucleocapsid eventually associates with the cytoplasmic domain of
E2 at the cell membrane, leading to budding and formation of
mature virions. Phosphorylation negatively regulates RNA-binding
activity, possibly delaying virion assembly during the viral
replication phase. Capsid protein dimerizes and becomes disulfide-
linked in the virion, but this interaction seems not to be
important for its biological function. Modulates genomic RNA
replication. Modulates subgenomic RNA synthesis by interacting
with human C1QBP/SF2P32. Induces both perinuclear clustering of
mitochondria and the formation of electron-dense
intermitochondrial plaques, both hallmarks of rubella virus
infected cells. Induces apoptosis when expressed in transfected
cells. {ECO:0000250|UniProtKB:P08563}.
-!- FUNCTION: Spike glycoprotein E2: Responsible for viral attachment
to target host cell, by binding to the cell receptor. Its
transport to the plasma membrane depends on interaction with E1
protein. {ECO:0000250|UniProtKB:P08563}.
-!- FUNCTION: Spike glycoprotein E1: Class II viral fusion protein.
Fusion activity is inactive as long as E1 is bound to E2 in mature
virion. After virus attachment to target cell and clathrin-
mediated endocytosis, acidification of the endosome would induce
dissociation of E1/E2 heterodimer and concomitant trimerization of
the E1 subunits. This E1 homotrimer is fusion active, and promotes
release of viral nucleocapsid in cytoplasm after endosome and
viral membrane fusion (By similarity). E1 cytoplasmic tail
modulates virus release, and the tyrosines residues are critical
for this function. {ECO:0000250|UniProtKB:P08563}.
-!- SUBUNIT: Capsid protein: Homooligomer. Forms a dimer shortly after
synthesis, this dimer become disulfide-linked in the virion.
Interacts with human C1QBP. Spike glycoprotein E1: Heterodimer
with spike glycoprotein E2. Spike glycoprotein E2: Heterodimer
with spike glycoprotein E1. {ECO:0000250|UniProtKB:P08563}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000250}. Host mitochondrion {ECO:0000250}.
Note=The capsid protein is concentrated around Golgi region.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E2: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host Golgi apparatus membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Note=E1 and E2 form heterodimer in
the endoplasmic reticulum before they are transported to and
retained in the Golgi complex, where virus assembly occurs. E1
possesses an endoplasmic reticulum retention signal, and
unassembled E2 and E1 subunits are retained in the endoplasmic
reticulum. Presumably, assembly of E2 and E1 would mask the
signal, thereby allowing transport of the heterodimer to the Golgi
complex (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E1: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host Golgi apparatus membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Note=E1 and E2 form heterodimer in
the endoplasmic reticulum before they are transported to and
retained in the Golgi complex, where virus assembly occurs. E1
possesses an endoplasmic reticulum retention signal, and
unassembled E2 and E1 subunits are retained in the endoplasmic
reticulum. Presumably, assembly of E2 and E1 would mask the
signal, thereby allowing transport of the heterodimer to the Golgi
complex (By similarity). {ECO:0000250}.
-!- DOMAIN: Structural polyprotein: Contains two internal signal
peptides that are necessary for directing translocation of the
glycoproteins into the lumen of the endoplasmic reticulum.
{ECO:0000250|UniProtKB:P08563}.
-!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Two signal peptidase-mediated cleavages
within the polyprotein produce the structural proteins capsid, E2,
and E1. The E2 signal peptide remains attached to the C-terminus
of the capsid protein after cleavage by the signal peptidase.
Another signal peptide at E2 C-terminus directs E1 to the ER, with
a similar mechanism. {ECO:0000250|UniProtKB:P08563}.
-!- MISCELLANEOUS: Structural polyprotein: Translated from a
subgenomic RNA synthesized during togaviruses replication.
{ECO:0000250|UniProtKB:Q6X2U3}.
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EMBL; J02620; AAA47423.1; ALT_SEQ; Genomic_RNA.
EMBL; AB047330; BAB32474.1; -; Genomic_RNA.
EMBL; AY968206; AAY34231.1; -; Genomic_RNA.
EMBL; AY968207; AAY34232.1; -; Genomic_RNA.
EMBL; AY968208; AAY34233.1; -; Genomic_RNA.
EMBL; AY968209; AAY34234.1; -; Genomic_RNA.
EMBL; AY968210; AAY34235.1; -; Genomic_RNA.
EMBL; AY968211; AAY34236.1; -; Genomic_RNA.
EMBL; AY968212; AAY34237.1; -; Genomic_RNA.
EMBL; AY968213; AAY34238.1; -; Genomic_RNA.
EMBL; AY968214; AAY34239.1; -; Genomic_RNA.
EMBL; AY968215; AAY34240.1; -; Genomic_RNA.
EMBL; AY968216; AAY34241.1; -; Genomic_RNA.
EMBL; AY968217; AAY34242.1; -; Genomic_RNA.
EMBL; AY968221; AAY34246.1; -; Genomic_RNA.
PIR; A25340; GNWVR1.
ProteinModelPortal; P08564; -.
SMR; P08564; -.
OrthoDB; VOG0900007P; -.
Proteomes; UP000008389; Genome.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; 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.
InterPro; IPR008819; Rubella_Capsid.
InterPro; IPR008820; Rubella_E1.
InterPro; IPR008821; Rubella_E2.
Pfam; PF05750; Rubella_Capsid; 1.
Pfam; PF05748; Rubella_E1; 1.
Pfam; PF05749; Rubella_E2; 1.
3: Inferred from homology;
Capsid protein; Clathrin-mediated endocytosis of virus by host;
Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cytoplasm; Host Golgi apparatus; Host membrane;
Host mitochondrion; Host-virus interaction; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; RNA-binding;
T=4 icosahedral capsid protein; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 300 Capsid protein.
/FTId=PRO_0000238999.
CHAIN 301 582 Spike glycoprotein E2.
/FTId=PRO_0000239000.
CHAIN 583 1063 Spike glycoprotein E1.
/FTId=PRO_0000239001.
TOPO_DOM 301 534 Extracellular. {ECO:0000255}.
TRANSMEM 535 555 Helical; Note=Golgi retention signal.
{ECO:0000255}.
TOPO_DOM 556 582 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 583 1028 Extracellular. {ECO:0000255}.
TRANSMEM 1029 1049 Helical; Note=Endoplasmic reticulum
retention signal. {ECO:0000255}.
TOPO_DOM 1050 1063 Extracellular. {ECO:0000255}.
REGION 30 69 Human C1QBP/SF2P32-binding.
{ECO:0000250}.
REGION 279 300 Functions as E2 signal peptide.
{ECO:0000250|UniProtKB:P08563}.
REGION 535 555 Golgi retention signal. {ECO:0000250}.
REGION 563 582 Functions as E1 signal peptide.
{ECO:0000250|UniProtKB:P08563}.
REGION 1029 1050 Endoplasmic reticulum retention signal.
{ECO:0000250}.
SITE 300 301 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 582 583 Cleavage; by host signal peptidase.
{ECO:0000255}.
MOD_RES 46 46 Phosphoserine; by host. {ECO:0000250}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 429 429 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 658 658 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 759 759 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 791 791 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 590 595 {ECO:0000250}.
DISULFID 619 824 {ECO:0000250}.
DISULFID 641 653 {ECO:0000250}.
DISULFID 699 712 {ECO:0000250}.
DISULFID 758 767 {ECO:0000250}.
DISULFID 807 817 {ECO:0000250}.
DISULFID 931 934 {ECO:0000250}.
DISULFID 950 983 {ECO:0000250}.
VARIANT 26 26 E -> G (in strain: Isolate RVI/ISR/79).
VARIANT 32 32 S -> A (in strain: Isolate RVI/CAL.USA/
91, Isolate RVI/PAN/99 and Isolate RVI/
SLV/02).
VARIANT 34 34 S -> P (in strain: Isolate RVI/CAL.USA/
91).
VARIANT 34 34 S -> T (in strain: Isolate RVI/CAL.USA/
97, Isolate RVI/MYS/01, Isolate RVI/
SAITAMA.JPN/94, Isolate RVI/SHANDONG.CHN/
02 and Isolate RVI/TOKOYO.JPN/90).
VARIANT 42 42 Q -> P (in strain: Isolate RVI/
SAITAMA.JPN/94).
VARIANT 71 71 L -> R (in strain: Isolate RVI/Anhui.CHN/
00, Isolate RVI/CAL.USA/91, Isolate RVI/
CAL.USA/97, Isolate RVI/ISR/75, Isolate
RVI/ISR/79, Isolate RVI/ISR/88, Isolate
RVI/MYS/01, Isolate RVI/PAN/99, Isolate
RVI/SAITAMA.JPN/94, Isolate RVI/
SHANDONG.CHN/00, Isolate RVI/
SHANDONG.CHN/02, Isolate RVI/SLV/02 and
Isolate RVI/TOKOYO.JPN/90).
VARIANT 84 84 R -> Q (in strain: Isolate RVI/
SHANDONG.CHN/02).
VARIANT 87 87 S -> G (in strain: Isolate RVI/CAL.USA/
91).
VARIANT 89 89 S -> P (in strain: Isolate RVI/SLV/02).
VARIANT 94 94 P -> S (in strain: Isolate RVI/SLV/02).
VARIANT 97 97 S -> A (in strain: Isolate RVI/ISR/88 and
Isolate RVI/SLV/02).
VARIANT 97 97 S -> P (in strain: Isolate RVI/MYS/01 and
Isolate RVI/SHANDONG.CHN/02).
VARIANT 100 100 P -> L (in strain: Isolate RVI/ISR/88).
VARIANT 101 101 P -> T (in strain: Isolate RVI/CAL.USA/
91, Isolate RVI/PAN/99 and Isolate RVI/
SLV/02).
VARIANT 148 148 A -> V (in strain: Isolate RVI/MYS/01).
VARIANT 245 245 M -> I (in strain: Isolate RVI/
SAITAMA.JPN/94).
VARIANT 269 269 S -> A (in strain: Isolate RVI/
TOKOYO.JPN/90).
VARIANT 283 283 A -> V (in strain: Isolate RVI/PAN/99 and
Isolate RVI/SLV/02).
VARIANT 307 307 D -> E (in strain: Isolate RVI/CAL.USA/
97).
VARIANT 312 312 P -> L (in strain: Isolate RVI/
SAITAMA.JPN/94 and Isolate RVI/
TOKOYO.JPN/90).
VARIANT 312 312 P -> S (in strain: Isolate RVI/
SHANDONG.CHN/00).
VARIANT 313 313 T -> A (in strain: Isolate RVI/MYS/01,
Isolate RVI/SAITAMA.JPN/94, Isolate RVI/
SHANDONG.CHN/02 and Isolate RVI/
TOKOYO.JPN/90).
VARIANT 313 313 T -> M (in strain: Isolate RVI/Anhui.CHN/
00 and Isolate RVI/SHANDONG.CHN/00).
VARIANT 313 313 T -> V (in strain: Isolate RVI/CAL.USA/
97).
VARIANT 314 314 L -> P (in strain: Isolate RVI/Anhui.CHN/
00, Isolate RVI/CAL.USA/91, Isolate RVI/
CAL.USA/97, Isolate RVI/MYS/01, Isolate
RVI/PAN/99, Isolate RVI/SAITAMA.JPN/94,
Isolate RVI/SHANDONG.CHN/00, Isolate RVI/
SHANDONG.CHN/02, Isolate RVI/SLV/02 and
Isolate RVI/TOKOYO.JPN/90).
VARIANT 325 325 Y -> H (in strain: Isolate RVI/ISR/79).
VARIANT 377 377 Q -> L (in strain: Isolate RVI/ISR/75).
VARIANT 398 400 PPA -> SPP (in strain: Isolate RVI/ISR/
79).
VARIANT 405 405 F -> L (in strain: Isolate RVI/Anhui.CHN/
00, Isolate RVI/CAL.USA/91, Isolate RVI/
CAL.USA/97, Isolate RVI/ISR/75, Isolate
RVI/ISR/79, Isolate RVI/ISR/88, Isolate
RVI/MYS/01, Isolate RVI/PAN/99, Isolate
RVI/SAITAMA.JPN/94, Isolate RVI/
SHANDONG.CHN/00, Isolate RVI/
SHANDONG.CHN/02, Isolate RVI/SLV/02 and
Isolate RVI/TOKOYO.JPN/90).
VARIANT 411 411 S -> A (in strain: Isolate RVI/CAL.USA/
97, Isolate RVI/MYS/01, Isolate RVI/
SAITAMA.JPN/94, Isolate RVI/SHANDONG.CHN/
02 and Isolate RVI/TOKOYO.JPN/90).
VARIANT 413 413 T -> P (in strain: Isolate RVI/ISR/75,
Isolate RVI/ISR/79 and Isolate RVI/ISR/
88).
VARIANT 414 414 A -> T (in strain: Isolate RVI/ISR/79).
VARIANT 415 415 A -> S (in strain: Isolate RVI/SLV/02).
VARIANT 416 416 T -> A (in strain: Isolate RVI/PAN/99).
VARIANT 417 418 PA -> LT (in strain: Isolate RVI/
SHANDONG.CHN/02).
VARIANT 420 420 A -> V (in strain: Isolate RVI/CAL.USA/
97, Isolate RVI/SAITAMA.JPN/94, Isolate
RVI/SHANDONG.CHN/00, Isolate RVI/
SHANDONG.CHN/00 and Isolate RVI/
TOKOYO.JPN/90).
VARIANT 421 421 P -> R (in strain: Isolate RVI/
SAITAMA.JPN/94).
VARIANT 422 422 A -> T (in strain: Isolate RVI/MYS/01).
VARIANT 426 426 A -> T (in strain: Isolate RVI/ISR/88).
VARIANT 430 430 D -> G (in strain: Isolate RVI/ISR/75).
VARIANT 473 473 A -> V (in strain: Isolate RVI/
SHANDONG.CHN/02).
VARIANT 484 484 V -> I (in strain: Isolate RVI/MYS/01).
VARIANT 497 497 R -> H (in strain: Isolate RVI/ISR/79 and
Isolate RVI/ISR/88).
VARIANT 511 511 V -> A (in strain: Isolate RVI/MYS/01).
VARIANT 528 528 A -> T (in strain: Isolate RVI/SLV/02).
VARIANT 542 542 F -> V (in strain: Isolate RVI/MYS/01,
Isolate RVI/SAITAMA.JPN/94 and Isolate
RVI/SHANDONG.CHN/02).
VARIANT 549 549 V -> I (in strain: Isolate RVI/
SAITAMA.JPN/94).
VARIANT 552 552 F -> L (in strain: Isolate RVI/SLV/02).
VARIANT 577 577 N -> T (in strain: Isolate RVI/CAL.USA/
91, Isolate RVI/ISR/75, Isolate RVI/ISR/
79, Isolate RVI/ISR/88, Isolate RVI/PAN/
99 and Isolate RVI/SLV/02).
VARIANT 599 599 T -> A (in strain: Isolate RVI/CAL.USA/
91, Isolate RVI/ISR/75, Isolate RVI/ISR/
79, Isolate RVI/ISR/88 and Isolate RVI/
PAN/99).
VARIANT 606 606 A -> T (in strain: Isolate RVI/
SHANDONG.CHN/02).
VARIANT 634 634 E -> D (in strain: Isolate RVI/
TOKOYO.JPN/90).
VARIANT 639 639 V -> I (in strain: Isolate RVI/SLV/02).
VARIANT 682 682 S -> T (in strain: Isolate RVI/MYS/01).
VARIANT 746 746 R -> G (in strain: Isolate RVI/CAL.USA/
97).
VARIANT 756 756 A -> V (in strain: Isolate RVI/CAL.USA/
91, Isolate RVI/CAL.USA/97, Isolate RVI/
ISR/75, Isolate RVI/ISR/79, Isolate RVI/
ISR/88, Isolate RVI/MYS/01, Isolate RVI/
PAN/99, Isolate RVI/SAITAMA.JPN/94,
Isolate RVI/SHANDONG.CHN/02, Isolate RVI/
SLV/02 and Isolate RVI/TOKOYO.JPN/90).
VARIANT 757 757 S -> L (in strain: Isolate RVI/
TOKOYO.JPN/90).
VARIANT 915 915 A -> T (in strain: Isolate RVI/Anhui.CHN/
00 and Isolate RVI/SHANDONG.CHN/00).
VARIANT 915 915 A -> V (in strain: Isolate RVI/
SAITAMA.JPN/94 and Isolate RVI/
TOKOYO.JPN/90).
VARIANT 919 919 A -> T (in strain: Isolate RVI/
SAITAMA.JPN/94).
VARIANT 920 920 L -> F (in strain: Isolate RVI/
SHANDONG.CHN/02).
VARIANT 986 986 E -> D (in strain: Isolate RVI/ISR/75).
VARIANT 1036 1036 A -> T (in strain: Isolate RVI/
SAITAMA.JPN/94).
VARIANT 1039 1039 A -> T (in strain: Isolate RVI/CAL.USA/
97, Isolate RVI/MYS/01Isolate RVI/
SAITAMA.JPN/94, Isolate RVI/SHANDONG.CHN/
02 and Isolate RVI/TOKOYO.JPN/90).
VARIANT 1041 1041 L -> P (in strain: Isolate RVI/ISR/79).
VARIANT 1042 1042 L -> F (in strain: Isolate RVI/
SHANDONG.CHN/00).
SEQUENCE 1063 AA; 114721 MW; 9C15B97F7CFAF1BD CRC64;
MASTTPITME DLQKALEAQS RALRAELAAG ASQSRRPRPP RQRDSSTSGD DSGRDSGGPR
RRRGNRGRGQ LRDWSRAPPP PEERQESRSQ TPAPKPSRAP PQQPQPPRMQ TGRGGSAPRP
ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT EACVTSWLWS EGEGAVFYRV DLHFTNLGTP
PLDEDGRWDP ALMYNPCGPE PPAHVVRAYN QPAGDVRGVW GKGERTYAEQ DFRVGGTRWH
RLLRMPVRGL DGDSAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL AAVAVGTARA
GLQPRADMAA PPTLPQPPRA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH HRNASDVLPG
HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA TPTPFTTAAN STTAATPATA
PAPCHAGLND SCGGFLSGCG PMRLRHGADT RCGRLICGLS TTAQYPPTRF GCAMRWGLPP
WELVVLTARP EDGWTCRGVP AHPGTRCPEL VSPMGRATCS PASALWLATA NALSLDHALA
AFVLLVPWVL IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQTP
VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPT APCARIWNGT
QRACTFWAVN AYSSGGYAQL ASYFNPGGSY YKQYHPTACE VEPAFGHSDA ACWGFPTDTV
MSVFALASYV QHPHKTVRVK FHTETRTVWQ LSVAGASCNV TTEHPFCNTP HGQLEVQVPP
DPGDLVEYIM NYTGNQQSRW GLGSPNCHGP DWASPVCQRH SPDCSRLVGA TPERPRLRLV
DADDPLLRTA PGPGEVWVTP VIGSQARKCG LHIRAGPYGH ATVEMPEWIH AHTTSDPWHP
PGPLGLKFKT VRPVALPRAL APPRNVRVTG CYQCGTPALV EGLAPGGGNC HLTVNGEDVG
AFPPGKFVTA ALLNTPPPYQ VSCGGESDRA SARVIDPAAQ SFTGVVYGTH TTAVSETRQT
WAEWAAAHWW QLTLGAICAL LLAGLLACCA KCLYYLRGAI APR


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EIAAB34629 Ammonium transporter Rh type C,C15orf6,CDRC2,Homo sapiens,Human,PDRC2,Rh family type C glycoprotein,Rh glycoprotein kidney,Rh type C glycoprotein,RHCG,Rhesus blood group family type C glycoprotein,RHG
E0674r ELISA kit Adipocyte membrane protein,Cd36,Fat,Fatty acid translocase,Fatty acid transport protein,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV,Rat,Rattu 96T
E0674r ELISA Adipocyte membrane protein,Cd36,Fat,Fatty acid translocase,Fatty acid transport protein,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV,Rat,Rattus nor 96T
65-102 anti_SARS spike glycoprotein antibody (clone 3A2) 250ug
65-101 anti_SARS spike glycoprotein antibody (clone 3A2) 50ug
65-102 anti_SARS spike glycoprotein antibody (clone 3A2) 250ug
65-101 anti_SARS spike glycoprotein antibody (clone 3A2) 50ug
65-102 anti_SARS spike glycoprotein antibody (clone 3A2) 250ug
65-101 anti_SARS spike glycoprotein antibody (clone 3A2) 50ug
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
MAB7942 SARS spike glycoprotein monoclonal antibody, clone 3A2 250 ug
E0674b ELISA kit Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
E0674b ELISA Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
U0674b CLIA Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
U0674m CLIA Cd36,Glycoprotein IIIb,GPIIIB,GPIV,Mouse,Mus musculus,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
E0674m ELISA Cd36,Glycoprotein IIIb,GPIIIB,GPIV,Mouse,Mus musculus,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
E0674m ELISA kit Cd36,Glycoprotein IIIb,GPIIIB,GPIV,Mouse,Mus musculus,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T


 

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