Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Fusion glycoprotein F0 [Cleaved into: Fusion glycoprotein F1; Fusion glycoprotein F2]

 FUS_ISAV8               Reviewed;         444 AA.
Q8V3T9;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
10-MAY-2017, entry version 36.
RecName: Full=Fusion glycoprotein F0;
Contains:
RecName: Full=Fusion glycoprotein F1;
Contains:
RecName: Full=Fusion glycoprotein F2;
Flags: Precursor;
Name=P3;
Infectious salmon anemia virus (isolate Atlantic
salmon/Norway/810/9/99) (ISAV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Isavirus.
NCBI_TaxID=652965;
NCBI_TaxID=8049; Gadus morhua (Atlantic cod).
NCBI_TaxID=8019; Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
NCBI_TaxID=8022; Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
NCBI_TaxID=8060; Pollachius virens (Saithe) (Gadus virens).
NCBI_TaxID=8030; Salmo salar (Atlantic salmon).
NCBI_TaxID=8032; Salmo trutta (Brown trout).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11807235;
Clouthier S.C., Rector T., Brown N.E., Anderson E.D.;
"Genomic organization of infectious salmon anaemia virus.";
J. Gen. Virol. 83:421-428(2002).
[2]
FUNCTION.
PubMed=16160182; DOI=10.1128/JVI.79.19.12544-12553.2005;
Aspehaug V., Mikalsen A.B., Snow M., Biering E., Villoing S.;
"Characterization of the infectious salmon anemia virus fusion
protein.";
J. Virol. 79:12544-12553(2005).
[3]
INTERACTION WITH HEMAGGLUTININ ESTERASE.
PubMed=24486627; DOI=10.1099/vir.0.061648-0;
Fourrier M., Lester K., Thoen E., Mikalsen A., Evensen O., Falk K.,
Collet B., McBeath A.;
"Deletions in the highly polymorphic region (HPR) of infectious salmon
anaemia virus HPR0 haemagglutinin-esterase enhance viral fusion and
influence the interaction with the fusion protein.";
J. Gen. Virol. 95:1015-1024(2014).
[4]
FUNCTION.
PubMed=26082488; DOI=10.1074/jbc.M115.644781;
Cook J.D., Soto-Montoya H., Korpela M.K., Lee J.E.;
"Electrostatic architecture of the infectious salmon anemia virus
(ISAV) core fusion protein illustrates a carboxyl-carboxylate pH
sensor.";
J. Biol. Chem. 290:18495-18504(2015).
-!- FUNCTION: Class I viral fusion protein. Under the current model,
the protein has at least 3 conformational states: pre-fusion
native state, pre-hairpin intermediate state, and post-fusion
hairpin state. During viral and target cell membrane fusion, the
heptad repeat (HR) regions assume a trimer-of-hairpins structure,
positioning the fusion peptide in close proximity to the C-
terminal region of the ectodomain. The formation of this structure
appears to drive apposition and subsequent fusion of viral and
target cell membranes. Directs fusion of viral and cellular
membranes leading to delivery of the nucleocapsid into the
cytoplasm. The trimer of F1-F2 (F protein) probably interacts with
HE at the virion surface. Upon HE binding to its cellular
receptor, the hydrophobic fusion peptide is unmasked and interacts
with the cellular membrane, inducing the fusion between cell and
virion membranes. {ECO:0000269|PubMed:16160182,
ECO:0000269|PubMed:26082488}.
-!- SUBUNIT: Homotrimer of disulfide-linked F1-F2 (PubMed:16160182).
Interacts with Hemagglutinin esterase (PubMed:24486627).
{ECO:0000269|PubMed:16160182, ECO:0000269|PubMed:24486627}.
-!- SUBCELLULAR LOCATION: Virion membrane. Host membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
-!- PTM: The inactive precursor F0 is glycosylated and proteolytically
cleaved into F1 and F2 to be functionally active. The cleavage is
mediated by cellular proteases during the transport and maturation
of the polypeptide. {ECO:0000269|PubMed:16160182}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF404343; AAL67959.1; -; Viral_cRNA.
RefSeq; YP_145801.1; NC_006500.2.
SMR; Q8V3T9; -.
PRIDE; Q8V3T9; -.
GeneID; 3170815; -.
KEGG; vg:3170815; -.
Proteomes; UP000008772; Genome.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
InterPro; IPR025167; Fusion_F0_Isavirus.
Pfam; PF13044; Fusion_F0; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Host membrane;
Membrane; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Virion.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 444 Fusion glycoprotein F0.
/FTId=PRO_0000403919.
CHAIN 18 276 Fusion glycoprotein F1.
/FTId=PRO_0000403920.
CHAIN 277 444 Fusion glycoprotein F2.
/FTId=PRO_0000403921.
TOPO_DOM 18 413 Extracellular. {ECO:0000250}.
TRANSMEM 414 434 Helical. {ECO:0000255}.
TOPO_DOM 435 444 Cytoplasmic. {ECO:0000250}.
REGION 277 292 Fusion peptide. {ECO:0000250}.
SITE 276 277 Cleavage; by host. {ECO:0000250}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 359 359 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
SEQUENCE 444 AA; 48773 MW; 388C3090B65C8D41 CRC64;
MAFLTILVLF LFKEVLCEPC ICENPTCLGI TIPQAGFVRS APGGVLLTET ITERPQLTEW
TTSRPKLEET LWLDGETKNG KVSQTLFEAI QGTQMENCAV KAVLDTTFVN LTKQDIVLGK
IKVSEFGGDS DISKCGRKGL KVFICGGTVG YVTRGCPPEE CKGKKGRMMA LEPTTDCGVE
KGLTTDRIKT GMLDITSCCT QHGCTKGIRV EVPSPVLVSS KCQEVTFRVV PFHSVPDKLG
FARTSSFTLK ANFVNKHGWS KYNFNLRGFP GEEFIKCCGF TLGVGGAWFQ AYLNGMVQGD
GAASADDVKE KLNGIIDQIN KANTLLEGEI EAVRRIAYMN QASSLQNQVE IGLIGEYLNI
SSWLETTTLT KTEEGLMKNG WCQSNTHCWC PPKPTIVPTI GYVDSIKEVT GTSWWMVMIH
YIIVGLIVIV VVVFGLKLWG CLRR


Related products :

Catalog number Product name Quantity
CNB-1434602 Human RSV (A2) Fusion glycoprotein _ RSV_F Protein (His Tag) 20
VSV11-P VSV-Glycoprotein (fusion-tag) Control blocking peptide #1 100 ug
CNB-1436391 Human RSV Fusion Glycoprotein _ RSV_F Antibody 100
VSV11-M Monoclonal VSV-Glycoprotein (fusion-tag) antibody, ascites 100 ul
abx109412 Polyclonal Rabbit Distemper virus Fusion glycoprotein F0 Antibody 100 μg
abx109081 Polyclonal Rabbit Distemper virus Fusion glycoprotein F0 Antibody (HRP) 100 μg
abx107664 Polyclonal Rabbit Distemper virus Fusion glycoprotein F0 Antibody (FITC) 100 μg
abx106250 Polyclonal Rabbit Distemper virus Fusion glycoprotein F0 Antibody (Biotin) 100 μg
C01286M Respiratory Syncytial Virus (RSV) Fusion Protein (46kDa & 22kDa S-S linked glycoprotein) host: Mouse 1mg
C01286M Respiratory Syncytial Virus (RSV) Fusion Protein (46kDa & 22kDa S-S linked glycoprotein)Mouse Purified IgG2b 1mg
EIAAB27950 Erg1,NEM-sensitive fusion protein,N-ethylmaleimide-sensitive fusion protein,Nsf,Rat,Rattus norvegicus,Vesicle-fusing ATPase,Vesicular-fusion protein NSF
EIAAB27951 Homo sapiens,Human,NEM-sensitive fusion protein,N-ethylmaleimide-sensitive fusion protein,NSF,Vesicle-fusing ATPase,Vesicular-fusion protein NSF
18-003-44267 Erythrocyte membrane glycoprotein Rh50 - Rh-associated glycoprotein. isoform CRA_b; Rh-associated glycoprotein; Rh50 glycoprotein Polyclonal 0.1 mg Protein A
EIAAB27952 Mouse,Mus musculus,NEM-sensitive fusion protein,N-ethylmaleimide-sensitive fusion protein,Nsf,Protein SKD2,Skd2,Suppressor of K(+) transport growth defect 2,Vesicle-fusing ATPase,Vesicular-fusion prot
orb80263 Rat Apoliprotein J protein The Clusterin Rat was constructed as recombinant protein with N-terminal fusion of T7-Tag (16AA) and C-terminal fusion of His-Tag (9AA). The Clusterin Rat His-Tagged Fusion 2
27-956 Alpha2-HS glycoprotein (AHSG), a glycoprotein present in the serum, is synthesized by hepatocytes. The AHSG molecule consists of two polypeptide chains, which are both cleaved from a proprotein encode 0.05 mg
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
U0674b CLIA Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
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
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
EIAAB34596 Ammonium transporter Rh type A,Erythrocyte membrane glycoprotein Rh50,Rat,Rattus norvegicus,Rh family type A glycoprotein,Rh type A glycoprotein,Rh50,Rhag,Rhesus blood group family type A glycoprotein
EIAAB34597 Ammonium transporter Rh type A,Erythrocyte membrane glycoprotein Rh50,Mouse,Mus musculus,Rh family type A glycoprotein,Rh type A glycoprotein,Rh50,Rhag,Rhesus blood group family type A glycoprotein


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur