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

DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.-) (Deoxycytidine deaminase) (Fragment)

 ABC3G_CHLAE             Reviewed;         377 AA.
Q7YR25;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
23-MAY-2018, entry version 70.
RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G;
EC=3.5.4.-;
AltName: Full=Deoxycytidine deaminase;
Flags: Fragment;
Name=APOBEC3G;
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus.
NCBI_TaxID=9534;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN DNA C TO U EDITING, AND
SPECIES-SPECIFIC RESTRICTION TO HIV-1 INFECTION.
PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4;
Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R.,
Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.;
"Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
Cell 114:21-31(2003).
[2]
FUNCTION IN SFV RESTRICTION.
PubMed=16378963; DOI=10.1128/JVI.80.2.605-614.2006;
Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A.,
Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.;
"Restriction of foamy viruses by APOBEC cytidine deaminases.";
J. Virol. 80:605-614(2006).
[3]
REVIEW.
PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350;
Chiu Y.L., Greene W.C.;
"The APOBEC3 cytidine deaminases: an innate defensive network opposing
exogenous retroviruses and endogenous retroelements.";
Annu. Rev. Immunol. 26:317-353(2008).
-!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an
inhibitor of retrovirus replication and retrotransposon mobility
via deaminase-dependent and -independent mechanisms. Exhibits
antiviral activity against vif-deficient: HIV-1 and simian
immunodeficiency viruses (SIVs) and also simian foamy virus (SFV).
After the penetration of retroviral nucleocapsids into target
cells of infection and the initiation of reverse transcription, it
can induce the conversion of cytosine to uracil in the minus-sense
single-strand viral DNA, leading to G-to-A hypermutations in the
subsequent plus-strand viral DNA. The resultant detrimental levels
of mutations in the proviral genome, along with a deamination-
independent mechanism that works prior to the proviral
integration, together exert efficient antiretroviral effects in
infected target cells. Selectively targets single-stranded DNA and
does not deaminate double-stranded DNA or single- or double-
stranded RNA. May inhibit the mobility of LTR retrotransposons.
{ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:16378963}.
-!- CATALYTIC ACTIVITY: 2'-deoxycytidine in single-stranded DNA +
H(2)O = 2'-deoxyuridine in single-stranded DNA + NH(3).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Assembly into ribonucleoprotein complexes of
high-molecular-mass (HMM) inhibits its enzymatic activity.
Antiviral activity is neutralized by the simian immunodeficiency
virus (SIV-agm) virion infectivity factor (VIF), that prevents its
incorporation into progeny virions by both inhibiting its
translation and/or by inducing its ubiquitination and subsequent
degradation by the 26S proteasome (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Homooligomer. Can bind RNA to form
ribonucleoprotein complexes of high-molecular-mass (HMM) or low-
molecular-mass (LMM). HMM is inactive and heterogeneous in protein
composition because of binding nonselectively to cellular RNAs,
which in turn are associated with variety of cellular proteins.
The LMM form which is enzymatically active has few or no RNAs
associated. Its ability to form homooligomer is distinct from its
ability to assemble into HMM. Interacts with APOBEC3B, APOBEC3F,
MOV10, AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent
manner. Interacts with AGO1, AGO3 and PKA/PRKACA (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Note=Mainly
cytoplasmic, small amount are found in the nucleus. {ECO:0000250}.
-!- DOMAIN: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-
dependent oligomerization and virion incorporation whereas the
CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase
activity and substrate sequence specificity. {ECO:0000250}.
-!- MISCELLANEOUS: Accumulation of APOBEC3G induced non-lethal
hypermutation could contribute to the genetic variation of primate
lentiviral populations.
-!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY331714; AAP85254.1; -; mRNA.
ProteinModelPortal; Q7YR25; -.
SMR; Q7YR25; -.
PRIDE; Q7YR25; -.
HOVERGEN; HBG050434; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0047844; F:deoxycytidine deaminase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009972; P:cytidine deamination; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0070383; P:DNA cytosine deamination; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR013158; APOBEC_N.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
Pfam; PF08210; APOBEC_N; 2.
SUPFAM; SSF53927; SSF53927; 2.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
1: Evidence at protein level;
Antiviral defense; Cytoplasm; Hydrolase; Immunity; Innate immunity;
Metal-binding; Nucleus; Phosphoprotein; Repeat; Zinc.
CHAIN 1 >377 DNA dC->dU-editing enzyme APOBEC-3G.
/FTId=PRO_0000171758.
DOMAIN 29 138 CMP/dCMP-type deaminase 1.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
DOMAIN 214 327 CMP/dCMP-type deaminase 2.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
REGION 1 60 Essential for cytoplasmic localization.
{ECO:0000250}.
REGION 209 335 Necessary for homooligomerization.
{ECO:0000250}.
REGION 312 319 Interaction with DNA. {ECO:0000250}.
ACT_SITE 259 259 Proton donor. {ECO:0000250}.
METAL 65 65 Zinc. {ECO:0000250}.
METAL 97 97 Zinc. {ECO:0000250}.
METAL 100 100 Zinc. {ECO:0000250}.
METAL 257 257 Zinc; catalytic. {ECO:0000250}.
METAL 287 287 Zinc; catalytic. {ECO:0000250}.
METAL 290 290 Zinc; catalytic. {ECO:0000250}.
SITE 244 244 Interaction with DNA. {ECO:0000250}.
MOD_RES 32 32 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:Q9HC16}.
MOD_RES 218 218 Phosphothreonine; by PKA and CAMK2.
{ECO:0000250|UniProtKB:Q9HC16}.
NON_TER 377 377
SEQUENCE 377 AA; 44720 MW; C68093826FA89342 CRC64;
MNPQIRNMVE QMEPDIFVYY FNNRPILSGR NTVWLCYEVK TKDPSGPPLD ANIFQGKLYP
EAKDHPEMKF LHWFRKWRQL HRDQEYEVTW YVSWSPCTRC ANSVATFLAE DPKVTLTIFV
ARLYYFWKPD YQQALRILCQ ERGGPHATMK IMNYNEFQHC WNEFVDGQGK PFKPRKNLPK
HYTLLHATLG ELLRHVMDPG TFTSNFNNKP WVSGQRETYL CYKVERSHND TWVLLNQHRG
FLRNQAPDRH GFPKGRHAEL CFLDLIPFWK LDDQQYRVTC FTSWSPCFSC AQKMAKFISN
NKHVSLCIFA ARIYDDQGRC QEGLRTLHRD GAKIAVMNYS EFEYCWDTFV DRQGRPFQPW
DGLDEHSQAL SGRLRAI


Related products :

Catalog number Product name Quantity
18-661-15176 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.1 mg
18-003-42392 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.05 mg Aff Pur
18-003-42392 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.1 mg Protein A
18-003-42391 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.05 mg Aff Pur
18-003-42391 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.1 mg Protein A
EIAAB34199 Adar3,Adarb2,Double-stranded RNA-specific editase B2,dsRNA adenosine deaminase B2,Rat,Rattus norvegicus,Red2,RNA-dependent adenosine deaminase 3,RNA-editing deaminase 2,RNA-editing enzyme 2
EIAAB34198 Adar3,Adarb2,Double-stranded RNA-specific editase B2,dsRNA adenosine deaminase B2,Mouse,Mus musculus,Red2,RNA-dependent adenosine deaminase 3,RNA-editing deaminase 2,RNA-editing enzyme 2
EIAAB34200 ADAR3,ADARB2,Double-stranded RNA-specific editase B2,dsRNA adenosine deaminase B2,Homo sapiens,Human,RED2,RNA-dependent adenosine deaminase 3,RNA-editing deaminase 2,RNA-editing enzyme 2
EIAAB34197 Adarb1,Double-stranded RNA-specific editase 1,dsRNA adenosine deaminase,Rat,Rattus norvegicus,Red1,RNA-editing deaminase 1,RNA-editing enzyme 1
EIAAB34196 Adar2,Adarb1,Double-stranded RNA-specific editase 1,dsRNA adenosine deaminase,Mouse,Mus musculus,Red1,RNA-editing deaminase 1,RNA-editing enzyme 1
EIAAB34195 ADAR2,ADARB1,Double-stranded RNA-specific editase 1,DRADA2,dsRNA adenosine deaminase,Homo sapiens,Human,RED1,RNA-editing deaminase 1,RNA-editing enzyme 1
E1078b Rabbit ELISA Kit FOR C->U-editing enzyme APOBEC-1 96T
ABC3F_HUMAN Human ELISA Kit FOR DNA dC->dU-editing enzyme APOBEC-3F 96T
CSB-EL001919RA Rat C->U-editing enzyme APOBEC-1(APOBEC1) ELISA kit 96T
ABEC3_MOUSE Mouse ELISA Kit FOR DNA dC->dU-editing enzyme APOBEC-3 96T
E1116h Rat ELISA Kit FOR Putative C->U-editing enzyme APOBEC-4 96T
ABEC2_HUMAN Human ELISA Kit FOR Probable C->U-editing enzyme APOBEC-2 96T
ABC3A_HUMAN Human ELISA Kit FOR Probable DNA dC->dU-editing enzyme APOBEC-3A 96T
CSB-EL001919RA Rat C->U-editing enzyme APOBEC-1(APOBEC1) ELISA kit SpeciesRat 96T
CSB-EL001928RA Rat Putative C->U-editing enzyme APOBEC-4(APOBEC4) ELISA kit 96T
CSB-EL001927HU Human DNA dC->dU-editing enzyme APOBEC-3H(APOBEC3H) ELISA kit 96T
G5244 Putative C->U-editing enzyme APOBEC-4 (APOBEC4), Rat, ELISA Kit 96T
CSB-EL001925HU Human DNA dC->dU-editing enzyme APOBEC-3F(APOBEC3F) ELISA kit 96T
AE56033RB Rabbit C->U-editing enzyme APOBEC-1 (APOBEC1) ELISA Kit 48T
CSB-EL001926HU Human DNA dC->dU-editing enzyme APOBEC-3G(APOBEC3G) ELISA kit 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 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