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

Gag-Pro polyprotein [Cleaved into: Matrix protein p15 (MA); Capsid protein p24 (CA); Nucleocapsid protein p12-pro; Protease (EC 3.4.23.-); p13]

 PRO_BLVAU               Reviewed;         571 AA.
P0DOI1;
20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
20-DEC-2017, sequence version 1.
20-JUN-2018, entry version 4.
RecName: Full=Gag-Pro polyprotein;
Contains:
RecName: Full=Matrix protein p15;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p12-pro;
Contains:
RecName: Full=Protease;
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
Contains:
RecName: Full=p13;
Bovine leukemia virus (isolate Australian) (BLV).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Deltaretrovirus.
NCBI_TaxID=11903;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2167927; DOI=10.1099/0022-1317-71-8-1737;
Coulston J., Naif H., Brandon R., Kumar S., Khan S., Daniel R.C.W.,
Lavin M.F.;
"Molecular cloning and sequencing of an Australian isolate of proviral
bovine leukaemia virus DNA: comparison with other isolates.";
J. Gen. Virol. 71:1737-1746(1990).
[2]
RIBOSOMAL FRAMESHIFT.
PubMed=6094258;
Sagata N., Yasunaga T., Ikawa Y.;
"Identification of a potential protease-coding gene in the genomes of
bovine leukemia and human T-cell leukemia viruses.";
FEBS Lett. 178:79-82(1984).
[3]
DOMAIN LATE-BUDDING, AND MUTAGENESIS OF 100-PRO--TYR-103.
PubMed=12134053; DOI=10.1128/JVI.76.16.8485-8493.2002;
Wang H., Norris K.M., Mansky L.M.;
"Analysis of bovine leukemia virus gag membrane targeting and late
domain function.";
J. Virol. 76:8485-8493(2002).
-!- FUNCTION: Gag-Pro polyprotein: The matrix domain targets Gag, Gag-
Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a
multipartite membrane binding signal, that includes its
myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Matrix protein p15: Matrix protein.
{ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Capsid protein p24: Forms the spherical core of the
virus that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250|UniProtKB:P10274}.
-!- FUNCTION: Nucleocapsid protein p12-pro: Binds strongly to viral
nucleic acids and promote their aggregation. Also destabilizes the
nucleic acids duplexes via highly structured zinc-binding motifs.
{ECO:0000250|UniProtKB:P10274}.
-!- FUNCTION: Protease: The aspartyl protease mediates proteolytic
cleavages of Gag and Gag-Pol polyproteins during or shortly after
the release of the virion from the plasma membrane. Cleavages take
place as an ordered, step-wise cascade to yield mature proteins.
This process is called maturation. Displays maximal activity
during the budding process just prior to particle release from the
cell. {ECO:0000255|PROSITE-ProRule:PRU00275}.
-!- SUBUNIT: Gag-Pro polyprotein: Homodimer; the homodimers are part
of the immature particles. Gag-Pro polyprotein: Interacts with
human TSG101 and NEDD4; these interactions are essential for
budding and release of viral particles. Matrix protein p15:
Homodimer; further assembles as homohexamers.
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Matrix protein p15: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p12-pro: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Name=Gag-Pro polyprotein;
IsoId=P0DOI1-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting between gag-pro.
{ECO:0000269|PubMed:6094258, ECO:0000305};
Name=Gag polyprotein;
IsoId=P25058-1; Sequence=External;
Note=Produced by conventional translation.
{ECO:0000269|PubMed:6094258, ECO:0000305};
Name=Gag-Pro-Pol polyprotein;
IsoId=P25059-1; Sequence=External;
Note=Produced by -1 ribosomal frameshiftings between gag-pro and
pro-pol. {ECO:0000269|PubMed:6094258, ECO:0000305};
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle release. They
can occur individually or in close proximity within structural
proteins. They interacts with sorting cellular proteins of the
multivesicular body (MVB) pathway. Most of these proteins are
class E vacuolar protein sorting factors belonging to ESCRT-I,
ESCRT-II or ESCRT-III complexes. Matrix protein p15 contains one L
domain: a PPXY motif which binds to the WW domains of the
ubiquitin ligase NEDD4. {ECO:0000250|UniProtKB:P03345}.
-!- PTM: Gag-Pro polyprotein: Specific enzymatic cleavages by the
viral protease yield mature proteins. The polyprotein is cleaved
during and after budding, this process is termed maturation. The
protease is autoproteolytically processed at its N- and C-termini.
{ECO:0000250|UniProtKB:P10274}.
-!- PTM: Gag polyprotein: Myristoylated. Myristoylation of the matrix
(MA) domain mediates the transport and binding of Gag polyproteins
to the host plasma membrane and is required for the assembly of
viral particles. {ECO:0000250|UniProtKB:P03345,
ECO:0000250|UniProtKB:P10274}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; D00647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
SMR; P0DOI1; -.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.185.10; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
InterPro; IPR003139; D_retro_matrix.
InterPro; IPR036989; D_retro_matrix_sf.
InterPro; IPR000721; Gag_p24.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF02228; Gag_p19; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
Aspartyl protease; Capsid protein; Host-virus interaction; Hydrolase;
Lipoprotein; Metal-binding; Myristate; Phosphoprotein; Protease;
Repeat; Ribosomal frameshifting; Viral budding;
Viral budding via the host ESCRT complexes; Viral matrix protein;
Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000255}.
CHAIN 2 571 Gag-Pro polyprotein.
/FTId=PRO_0000442564.
CHAIN 2 109 Matrix protein p15.
/FTId=PRO_0000442565.
CHAIN 110 323 Capsid protein p24.
/FTId=PRO_0000442566.
CHAIN 324 419 Nucleocapsid protein p12-pro.
/FTId=PRO_0000442567.
CHAIN 420 544 Protease.
/FTId=PRO_0000442568.
CHAIN 545 571 p13.
/FTId=PRO_0000442569.
REPEAT 342 362
REPEAT 367 387
DOMAIN 447 525 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
ZN_FING 345 362 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 370 387 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
MOTIF 100 103 PPXY motif.
{ECO:0000269|PubMed:12134053}.
COMPBIAS 560 563 Poly-Pro. {ECO:0000255}.
ACT_SITE 452 452 Protease; shared with dimeric partner.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
SITE 109 110 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03345}.
SITE 323 324 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03345}.
SITE 419 420 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03345}.
SITE 544 545 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03345}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255}.
MUTAGEN 100 103 PPPY->AAAA: Greatly reduced release of
new viral particles.
{ECO:0000269|PubMed:12134053}.
SEQUENCE 571 AA; 62261 MW; 68890E386172F54F CRC64;
MGNSPSYNPP AGISPSDWLN LLQSAQRLNP RPSPSDFTDL KNYIHWFHKT QKKPWTFTSG
GPASCPPGKF GRVPLVLATL NEVLSNDEGA PGASAPEEQP PPYDPPAVLP IISEGNRNRH
RAWALRELQD IKKEIENKAP GSQVWIQTLR LAILQADPTP ADLEQLCQYI ASPVDQTAHM
TSLTAAIAAE AANTLQGFNP KMGTLTQQSA QPNAGDLRSQ YQNLWLQAWK NLPTRPSVQP
WSTIVQGPAE SYVEFVNRLQ ISLADNLPDG VPKEPIIDSL SYANANKECQ QILQGRGLVA
APVGQKLQAC AHWAPKTKQP AILVHTPGPK MPGPRQPAPK RPPPGPCYRC LKEGHWARDC
PTKTTGPPPG PCPICKDPSH WKRDCPTLKS KKLIEGGPSA PQIITPITDS LSEAELECLL
SIPLARSRPS VAVYLSGPWL QPSQNQALML VDTGAENTVL PQNWLVRDYP RTPAAVLGAG
GISRNRYNWL QGPLTLALKP EGPFITIPKI LVDTFDKWQI LGRDVLSRLQ ASISIPEEVH
PPVVGVLDAP PSHIGLEHLP PPPEVPQFPL N


Related products :

Catalog number Product name Quantity
SCH-OBT1904X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa340_390), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Appli 1 mg
OBT1906 RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 0.1 mg
OBT1905X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicat 1 mg
OBT1906X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 1 mg
OBT1904X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa340_390), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Appli 1 mg
SCH-OBT1906 RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 0.1 mg
SCH-OBT1906X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 1 mg
SCH-OBT1905X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicat 1 mg
orb81558 Hepatitis Virus Nucleocapsid (core) Genotype-2b protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81557 Hepatitis Virus Nucleocapsid (core) Genotype-2a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81556 Hepatitis Virus Nucleocapsid (core) Genotype-1b protein The E.coli derived recombinant multimer protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fus 100
orb81561 Hepatitis Virus Nucleocapsid (core) Genotype-4 protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81559 Hepatitis Virus Nucleocapsid (core) Genotype-3a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81567 Hepatitis Virus Nucleocapsid (core) (105-302) protein The E.coli derived recombinant protein from E1 region contains the HCV core nucleocapsid immunodominant regions, amino acids 105-302. The protein 100
29-694 SEMG1 is the predominant protein in semen. The secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes 0.1 mg
29-695 SEMG1 is the predominant protein in semen. The secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes 0.1 mg
orb81568 Hepatitis Virus Nucleocapsid (core) 24 protein The HCV Core 24 genotype-1b, E.coli derived recombinant protein, contains the HCV core nucleocapsid immunodominant regions. The protein is fused with b-g 100
orb81769 Measles Virus Nucleocapsid protein The E.coli derived recombinant protein contains the nucleocapsid immunodominant regions, 89-165 amino acids. For research use only. 100
orb81570 Hepatitis Virus Nucleocapsid (core) 22kDa protein The E.coli derived recombinant protein contains the HCV core nucleocapsid genotype 1b, immunodominant regions, amino acids 2-192, 22kDa.The protein is 100
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
orb81638 Hantavirus protein The Hantavirus nucleocapsid (N) fusion protein protein is expressed in E.coli and fused to GST-tag having Mw of 37 kDa. Hantavirus nucleocapsid (N) is conserved among different stra 100
E1639p ELISA kit 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
U1639p CLIA 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
orb81536 SARS Associated Coronavirus Matrix protein The E.coli derived 30kDa recombinant protein contains the Matrix protein 182-216 amino acids immunodominant regions. For research use only. 100
E1639p ELISA 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | 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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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