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

Two-on-two hemoglobin-3 (AtGLB3) (2-on-2 hemoglobin-3)

 GLB3_ARATH              Reviewed;         175 AA.
Q67XG0; O65532; Q946U7;
19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
22-NOV-2017, entry version 109.
RecName: Full=Two-on-two hemoglobin-3;
Short=AtGLB3;
AltName: Full=2-on-2 hemoglobin-3;
Name=GLB3; OrderedLocusNames=At4g32690; ORFNames=F4D11.110;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DIMERIZATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
STRAIN=cv. Columbia;
PubMed=11526234; DOI=10.1073/pnas.191349198;
Watts R.A., Hunt P.W., Hvitved A.N., Hargrove M.S., Peacock W.J.,
Dennis E.S.;
"A hemoglobin from plants homologous to truncated hemoglobins of
microorganisms.";
Proc. Natl. Acad. Sci. U.S.A. 98:10119-10124(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Shinn P., Chen H., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
STRAIN=cv. Columbia;
PubMed=21741261; DOI=10.1016/j.plaphy.2011.06.005;
Wang Y., Elhiti M., Hebelstrup K.H., Hill R.D., Stasolla C.;
"Manipulation of hemoglobin expression affects Arabidopsis shoot
organogenesis.";
Plant Physiol. Biochem. 49:1108-1116(2011).
[7]
FUNCTION, AND INTERACTION WITH RGLG3 AND RGLG4.
PubMed=27497447; DOI=10.1093/pcp/pcw122;
Nagels Durand A., Inigo S., Ritter A., Iniesto E., De Clercq R.,
Staes A., Van Leene J., Rubio V., Gevaert K., De Jaeger G.,
Pauwels L., Goossens A.;
"The Arabidopsis iron-sulfur protein GRXS17 is a target of the
ubiquitin E3 ligases RGLG3 and RGLG4.";
Plant Cell Physiol. 57:1801-1813(2016).
[8]
X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH HEME.
PubMed=24816109; DOI=10.1107/S1399004714004878;
Reeder B.J., Hough M.A.;
"The structure of a class 3 nonsymbiotic plant haemoglobin from
Arabidopsis thaliana reveals a novel N-terminal helical extension.";
Acta Crystallogr. D 70:1411-1418(2014).
-!- FUNCTION: Hemoglobin-like protein that exhibits an unusual
concentration-independent binding of O(2) and CO. May promote
shoot organogenesis from root explants in vitro (PubMed:11526234,
PubMed:21741261). Inhibits RGLG3 and RGLG4 ubiquitination activity
(PubMed:27497447). {ECO:0000269|PubMed:11526234,
ECO:0000269|PubMed:21741261, ECO:0000269|PubMed:27497447}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:24816109};
Note=Binds 1 heme group per subunit.
{ECO:0000269|PubMed:24816109};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=411 nm {ECO:0000269|PubMed:11526234};
Note=The absorbance spectrum of deoxy-GLB3 is unique as the
protein forms a transient six-coordinate structure with
absorption peaks at 538 and 565 nm after reduction and
deoxygenation, which slowly converts to a five-coordinate
structure with an absorption peak at 548 nm.;
-!- SUBUNIT: Homodimer when ferric (Probable). Interacts with RGLG3
and RGLG4 (PubMed:27497447). {ECO:0000269|PubMed:27497447,
ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed ubiquitously, with higher levels in
root tissue than in shoot tissue. {ECO:0000269|PubMed:11526234}.
-!- DISRUPTION PHENOTYPE: Slight reduction of the number of shoots
produced by root explants in vitro; root explants are first
cultured on an initial auxin-rich callus induction medium (CIM)
followed by a transfer onto a cytokinin-containing shoot induction
medium (SIM). {ECO:0000269|PubMed:21741261}.
-!- SIMILARITY: Belongs to the truncated hemoglobin family. Group II
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA18592.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB79986.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF376062; AAK55409.1; -; mRNA.
EMBL; AL022537; CAA18592.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161581; CAB79986.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE86104.1; -; Genomic_DNA.
EMBL; AK175236; BAD42999.1; -; mRNA.
EMBL; AK176859; BAD44622.1; -; mRNA.
EMBL; AK220670; BAD95217.1; -; mRNA.
EMBL; AK229442; BAF01302.1; -; mRNA.
EMBL; BT024768; ABD59106.1; -; mRNA.
PIR; T04457; T04457.
RefSeq; NP_567901.1; NM_119421.5.
UniGene; At.20909; -.
PDB; 4C0N; X-ray; 1.77 A; A=1-175.
PDB; 4C44; X-ray; 2.65 A; A=1-175.
PDBsum; 4C0N; -.
PDBsum; 4C44; -.
ProteinModelPortal; Q67XG0; -.
SMR; Q67XG0; -.
BioGrid; 14690; 3.
STRING; 3702.AT4G32690.1; -.
PaxDb; Q67XG0; -.
EnsemblPlants; AT4G32690.1; AT4G32690.1; AT4G32690.
GeneID; 829404; -.
Gramene; AT4G32690.1; AT4G32690.1; AT4G32690.
KEGG; ath:AT4G32690; -.
Araport; AT4G32690; -.
TAIR; locus:2125662; AT4G32690.
eggNOG; ENOG410IKRW; Eukaryota.
eggNOG; COG2346; LUCA.
HOGENOM; HOG000005818; -.
InParanoid; Q67XG0; -.
OMA; ACKHAAN; -.
OrthoDB; EOG09360OBH; -.
PhylomeDB; Q67XG0; -.
PRO; PR:Q67XG0; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q67XG0; baseline and differential.
Genevisible; Q67XG0; AT.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen carrier activity; IDA:TAIR.
GO; GO:0015671; P:oxygen transport; IDA:TAIR.
GO; GO:0009733; P:response to auxin; TAS:TAIR.
GO; GO:0001666; P:response to hypoxia; IEP:TAIR.
InterPro; IPR009050; Globin-like_sf.
InterPro; IPR001486; Hemoglobin_trunc.
Pfam; PF01152; Bac_globin; 1.
SUPFAM; SSF46458; SSF46458; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Heme; Iron; Metal-binding;
Oxygen transport; Reference proteome; Transport.
CHAIN 1 175 Two-on-two hemoglobin-3.
/FTId=PRO_0000425543.
METAL 98 98 Iron (heme proximal ligand).
{ECO:0000244|PDB:4C0N,
ECO:0000244|PDB:4C44,
ECO:0000269|PubMed:24816109}.
BINDING 85 85 Heme. {ECO:0000250}.
CONFLICT 167 167 H -> P (in Ref. 1; AAK55409).
{ECO:0000305}.
HELIX 4 12 {ECO:0000244|PDB:4C0N}.
HELIX 16 19 {ECO:0000244|PDB:4C0N}.
HELIX 20 24 {ECO:0000244|PDB:4C0N}.
HELIX 27 31 {ECO:0000244|PDB:4C0N}.
HELIX 33 48 {ECO:0000244|PDB:4C0N}.
HELIX 53 56 {ECO:0000244|PDB:4C0N}.
HELIX 57 59 {ECO:0000244|PDB:4C0N}.
HELIX 64 78 {ECO:0000244|PDB:4C0N}.
HELIX 84 89 {ECO:0000244|PDB:4C0N}.
HELIX 94 98 {ECO:0000244|PDB:4C0N}.
HELIX 105 121 {ECO:0000244|PDB:4C0N}.
HELIX 127 148 {ECO:0000244|PDB:4C0N}.
SEQUENCE 175 AA; 20197 MW; 7EE582552A3BBD7F CRC64;
MQSLQDKASV LSGVDQAEAF AIDESNLFDK LGLQTFINLS TNFYTRVYDD EEEWFQSIFS
NSNKEDAIQN QYEFFVQRMG GPPLYSQRKG HPALIGRHRP FPVTHQAAER WLEHMQNALD
DSVDIDQDSK IKMMKFFRHT AFFLVAGNEL KNQNEKPKHK PQCACKHAAN KPAEE


Related products :

Catalog number Product name Quantity
29-718 Haptoglobin combines with free plasma hemoglobin, preventing loss of iron through the kidneys and protecting the kidneys from damage by hemoglobin, while making the hemoglobin accessible to degradativ 0.05 mg
U0996Rb CLIA Gamma-globin,HBG,Hemoglobin beta-3,Hemoglobin gamma chain,Hemoglobin subunit gamma,Oryctolagus cuniculus,Rabbit 96T
E0996Rb ELISA kit Gamma-globin,HBG,Hemoglobin beta-3,Hemoglobin gamma chain,Hemoglobin subunit gamma,Oryctolagus cuniculus,Rabbit 96T
E0996Rb ELISA Gamma-globin,HBG,Hemoglobin beta-3,Hemoglobin gamma chain,Hemoglobin subunit gamma,Oryctolagus cuniculus,Rabbit 96T
E0996h ELISA kit Gamma-1-globin,Hb F Agamma,HBG1,Hemoglobin gamma-1 chain,Hemoglobin gamma-A chain,Hemoglobin subunit gamma-1,Homo sapiens,Human,PRO2979 96T
E0996h ELISA Gamma-1-globin,Hb F Agamma,HBG1,Hemoglobin gamma-1 chain,Hemoglobin gamma-A chain,Hemoglobin subunit gamma-1,Homo sapiens,Human,PRO2979 96T
U0996h CLIA Gamma-1-globin,Hb F Agamma,HBG1,Hemoglobin gamma-1 chain,Hemoglobin gamma-A chain,Hemoglobin subunit gamma-1,Homo sapiens,Human,PRO2979 96T
20-272-192026 Hemoglobin - Mouse monoclonal [Haem2] to Hemoglobin; Hemoglobin alpha chain; Alpha-globin Monoclonal 0.1 mg
U0692r CLIA Beta-1-globin,Hbb,Hemoglobin beta chain, major-form,Hemoglobin beta-1 chain,Hemoglobin subunit beta-1,Rat,Rattus norvegicus 96T
E0692r ELISA kit Beta-1-globin,Hbb,Hemoglobin beta chain, major-form,Hemoglobin beta-1 chain,Hemoglobin subunit beta-1,Rat,Rattus norvegicus 96T
E0692r ELISA Beta-1-globin,Hbb,Hemoglobin beta chain, major-form,Hemoglobin beta-1 chain,Hemoglobin subunit beta-1,Rat,Rattus norvegicus 96T
18-272-196766 Hemoglobin - Goat polyclonal to Hemoglobin; Hemoglobin alpha chain; Alpha-globin Polyclonal 1 ml
18-272-196765 Hemoglobin (HRP) - Goat polyclonal to Hemoglobin (HRP); Hemoglobin alpha chain; Alpha-globin Polyclonal 1 mg
18-272-196737 Hemoglobin (HRP) - Sheep polyclonal to Hemoglobin (HRP); Hemoglobin alpha chain; Alpha-globin Polyclonal 1 mg
18-272-196734 Hemoglobin - Goat polyclonal to Hemoglobin; Hemoglobin alpha chain; Alpha-globin Polyclonal 2 ml
E0692m ELISA Beta-1-globin,Hbb-b1,Hemoglobin beta-1 chain,Hemoglobin beta-major chain,Hemoglobin subunit beta-1,Mouse,Mus musculus 96T
U0692m CLIA Beta-1-globin,Hbb-b1,Hemoglobin beta-1 chain,Hemoglobin beta-major chain,Hemoglobin subunit beta-1,Mouse,Mus musculus 96T
E0692m ELISA kit Beta-1-globin,Hbb-b1,Hemoglobin beta-1 chain,Hemoglobin beta-major chain,Hemoglobin subunit beta-1,Mouse,Mus musculus 96T
orb82002 Human Hemoglobin protein Hemoglobin is a purified platelets_hemostasis antigen. For research use only. 2 g
TA194 Hemoglobin Standard, 15g_dL, Ready to use, 10ml_vial, Hemoglobin Reagents 10
orb81996 Human Hemoglobin A1c protein Hemoglobin A1c (HbA1c) is a purified platelets_hemostasis antigen. For research use only. 1 mg
DIHB-250 QuantiChrom™ Hemoglobin Assay Kit, Quantitative determination of hemoglobin by colorimetric (400nm) method 250Tests
CT008 HumanAlbumin, Hemoglobin, Hemoglobin F, IgA, IgD, IgE, IgG, IgM, kappa, lambda, Transferrin 1 x 96
ER1030 Glycosylated Hemoglobin per Hemoglobin A1c Elisa Kit 96T
18-272-196736 Hemoglobin (FITC) - Sheep polyclonal to Hemoglobin (FITC); Hemoglobin alpha chain; Alpha-globin Polyclonal 1 mg


 

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