HBL2_ARATH
ID HBL2_ARATH Reviewed; 158 AA.
AC O24521;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Non-symbiotic hemoglobin 2;
DE AltName: Full=ARAth GLB2;
DE Short=Hb2;
GN Name=AHB2; Synonyms=GLB2; OrderedLocusNames=At3g10520;
GN ORFNames=F13M14.20, F18K10.9;
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 [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=cv. C24;
RX PubMed=9342391; DOI=10.1073/pnas.94.22.12230;
RA Trevaskis B., Watts R.A., Andersson C.R., Llewellyn D.J., Hargrove M.S.,
RA Olson J.S., Dennis E.S., Peacock W.J.;
RT "Two hemoglobin genes in Arabidopsis thaliana: the evolutionary origins of
RT leghemoglobins.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12230-12234(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May not function as an oxygen storage or transport protein,
CC but might act as an oxygen sensor or play a role in electron transfer,
CC possibly to a bound oxygen molecule. Has a low affinity for O(2).
CC -!- SUBUNIT: Unable to dimerize. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves but not in roots.
CC -!- INDUCTION: By low temperature but not by low oxygen levels,
CC dehydration, heat shock, wounding or oxidative stress.
CC -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR EMBL; U94999; AAB82770.1; -; Genomic_DNA.
DR EMBL; AC011560; AAG51381.1; -; Genomic_DNA.
DR EMBL; AC013428; AAF76353.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74919.1; -; Genomic_DNA.
DR EMBL; AY087650; AAM65188.1; -; mRNA.
DR RefSeq; NP_187663.1; NM_111887.3.
DR AlphaFoldDB; O24521; -.
DR SMR; O24521; -.
DR STRING; 3702.AT3G10520.1; -.
DR PaxDb; O24521; -.
DR PRIDE; O24521; -.
DR ProteomicsDB; 247164; -.
DR EnsemblPlants; AT3G10520.1; AT3G10520.1; AT3G10520.
DR GeneID; 820216; -.
DR Gramene; AT3G10520.1; AT3G10520.1; AT3G10520.
DR KEGG; ath:AT3G10520; -.
DR Araport; AT3G10520; -.
DR TAIR; locus:2075780; AT3G10520.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_11_2_1; -.
DR InParanoid; O24521; -.
DR OMA; DEMKEAW; -.
DR OrthoDB; 1379813at2759; -.
DR PhylomeDB; O24521; -.
DR PRO; PR:O24521; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O24521; baseline and differential.
DR Genevisible; O24521; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; ISS:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:TAIR.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:TAIR.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR001032; Leghaemoglobin.
DR InterPro; IPR019824; Leghaemoglobin_Fe_BS.
DR PANTHER; PTHR22924; PTHR22924; 1.
DR Pfam; PF00042; Globin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
DR PROSITE; PS00208; PLANT_GLOBIN; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Metal-binding; Reference proteome.
FT CHAIN 1..158
FT /note="Non-symbiotic hemoglobin 2"
FT /id="PRO_0000193012"
FT BINDING 66
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 101
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
SQ SEQUENCE 158 AA; 17871 MW; 9E3E145432E0BEA0 CRC64;
MGEIGFTEKQ EALVKESWEI LKQDIPKYSL HFFSQILEIA PAAKGLFSFL RDSDEVPHNN
PKLKAHAVKV FKMTCETAIQ LREEGKVVVA DTTLQYLGSI HLKSGVIDPH FEVVKEALLR
TLKEGLGEKY NEEVEGAWSQ AYDHLALAIK TEMKQEES
