GLB3_ARATH
ID GLB3_ARATH Reviewed; 175 AA.
AC Q67XG0; O65532; Q946U7;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Two-on-two hemoglobin-3;
DE Short=AtGLB3;
DE AltName: Full=2-on-2 hemoglobin-3;
GN Name=GLB3; OrderedLocusNames=At4g32690; ORFNames=F4D11.110;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DIMERIZATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11526234; DOI=10.1073/pnas.191349198;
RA Watts R.A., Hunt P.W., Hvitved A.N., Hargrove M.S., Peacock W.J.,
RA Dennis E.S.;
RT "A hemoglobin from plants homologous to truncated hemoglobins of
RT microorganisms.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10119-10124(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=21741261; DOI=10.1016/j.plaphy.2011.06.005;
RA Wang Y., Elhiti M., Hebelstrup K.H., Hill R.D., Stasolla C.;
RT "Manipulation of hemoglobin expression affects Arabidopsis shoot
RT organogenesis.";
RL Plant Physiol. Biochem. 49:1108-1116(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH RGLG3 AND RGLG4.
RX PubMed=27497447; DOI=10.1093/pcp/pcw122;
RA Nagels Durand A., Inigo S., Ritter A., Iniesto E., De Clercq R., Staes A.,
RA Van Leene J., Rubio V., Gevaert K., De Jaeger G., Pauwels L., Goossens A.;
RT "The Arabidopsis iron-sulfur protein GRXS17 is a target of the ubiquitin E3
RT ligases RGLG3 and RGLG4.";
RL Plant Cell Physiol. 57:1801-1813(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=24816109; DOI=10.1107/s1399004714004878;
RA Reeder B.J., Hough M.A.;
RT "The structure of a class 3 nonsymbiotic plant haemoglobin from Arabidopsis
RT thaliana reveals a novel N-terminal helical extension.";
RL Acta Crystallogr. D 70:1411-1418(2014).
CC -!- FUNCTION: Hemoglobin-like protein that exhibits an unusual
CC concentration-independent binding of O(2) and CO. May promote shoot
CC organogenesis from root explants in vitro (PubMed:11526234,
CC PubMed:21741261). Inhibits RGLG3 and RGLG4 ubiquitination activity
CC (PubMed:27497447). {ECO:0000269|PubMed:11526234,
CC ECO:0000269|PubMed:21741261, ECO:0000269|PubMed:27497447}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:24816109};
CC Note=Binds 1 heme group per subunit. {ECO:0000269|PubMed:24816109};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=411 nm {ECO:0000269|PubMed:11526234};
CC Note=The absorbance spectrum of deoxy-GLB3 is unique as the protein
CC forms a transient six-coordinate structure with absorption peaks at
CC 538 and 565 nm after reduction and deoxygenation, which slowly
CC converts to a five-coordinate structure with an absorption peak at
CC 548 nm.;
CC -!- SUBUNIT: Homodimer when ferric (Probable). Interacts with RGLG3 and
CC RGLG4 (PubMed:27497447). {ECO:0000269|PubMed:27497447, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, with higher levels in root
CC tissue than in shoot tissue. {ECO:0000269|PubMed:11526234}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction of the number of shoots produced
CC by root explants in vitro; root explants are first cultured on an
CC initial auxin-rich callus induction medium (CIM) followed by a transfer
CC onto a cytokinin-containing shoot induction medium (SIM).
CC {ECO:0000269|PubMed:21741261}.
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group II
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18592.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79986.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF376062; AAK55409.1; -; mRNA.
DR EMBL; AL022537; CAA18592.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161581; CAB79986.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86104.1; -; Genomic_DNA.
DR EMBL; AK175236; BAD42999.1; -; mRNA.
DR EMBL; AK176859; BAD44622.1; -; mRNA.
DR EMBL; AK220670; BAD95217.1; -; mRNA.
DR EMBL; AK229442; BAF01302.1; -; mRNA.
DR EMBL; BT024768; ABD59106.1; -; mRNA.
DR PIR; T04457; T04457.
DR RefSeq; NP_567901.1; NM_119421.5.
DR PDB; 4C0N; X-ray; 1.77 A; A=1-175.
DR PDB; 4C44; X-ray; 2.65 A; A=1-175.
DR PDBsum; 4C0N; -.
DR PDBsum; 4C44; -.
DR AlphaFoldDB; Q67XG0; -.
DR SMR; Q67XG0; -.
DR BioGRID; 14690; 3.
DR STRING; 3702.AT4G32690.1; -.
DR PaxDb; Q67XG0; -.
DR PRIDE; Q67XG0; -.
DR ProteomicsDB; 221895; -.
DR EnsemblPlants; AT4G32690.1; AT4G32690.1; AT4G32690.
DR GeneID; 829404; -.
DR Gramene; AT4G32690.1; AT4G32690.1; AT4G32690.
DR KEGG; ath:AT4G32690; -.
DR Araport; AT4G32690; -.
DR TAIR; locus:2125662; AT4G32690.
DR eggNOG; ENOG502QRXE; Eukaryota.
DR HOGENOM; CLU_103526_0_0_1; -.
DR InParanoid; Q67XG0; -.
DR OMA; CKHATNK; -.
DR OrthoDB; 1349587at2759; -.
DR PhylomeDB; Q67XG0; -.
DR PRO; PR:Q67XG0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q67XG0; baseline and differential.
DR Genevisible; Q67XG0; AT.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IDA:TAIR.
DR GO; GO:0015671; P:oxygen transport; IDA:TAIR.
DR GO; GO:0009733; P:response to auxin; TAS:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IEP:TAIR.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR044203; GLB3-like.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR PANTHER; PTHR47366; PTHR47366; 1.
DR Pfam; PF01152; Bac_globin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT CHAIN 1..175
FT /note="Two-on-two hemoglobin-3"
FT /id="PRO_0000425543"
FT REGION 153..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000269|PubMed:24816109,
FT ECO:0007744|PDB:4C0N, ECO:0007744|PDB:4C44"
FT CONFLICT 167
FT /note="H -> P (in Ref. 1; AAK55409)"
FT /evidence="ECO:0000305"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:4C0N"
FT HELIX 127..148
FT /evidence="ECO:0007829|PDB:4C0N"
SQ 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
