HBL1_ARATH
ID HBL1_ARATH Reviewed; 160 AA.
AC O24520;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Non-symbiotic hemoglobin 1;
DE AltName: Full=ARAth GLB1;
DE Short=Hb1;
GN Name=AHB1; Synonyms=GLB1; OrderedLocusNames=At2g16060; ORFNames=F7H1.8;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 an unusually high affinity for
CC O(2) because of a very low dissociation constant.
CC -!- SUBUNIT: Dimer. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and rosette leaves.
CC -!- INDUCTION: By low oxygen levels but not by cold, dehydration, heat
CC shock, wounding or oxidative stress.
CC -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR EMBL; U94998; AAB82769.1; -; Genomic_DNA.
DR EMBL; AC007134; AAD26949.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06463.1; -; Genomic_DNA.
DR EMBL; BT006405; AAP21213.1; -; mRNA.
DR PIR; C84536; C84536.
DR RefSeq; NP_179204.1; NM_127165.4.
DR PDB; 3ZHW; X-ray; 2.22 A; A/B=1-160.
DR PDBsum; 3ZHW; -.
DR AlphaFoldDB; O24520; -.
DR SMR; O24520; -.
DR BioGRID; 1462; 1.
DR STRING; 3702.AT2G16060.1; -.
DR iPTMnet; O24520; -.
DR SwissPalm; O24520; -.
DR PaxDb; O24520; -.
DR PRIDE; O24520; -.
DR ProteomicsDB; 230286; -.
DR EnsemblPlants; AT2G16060.1; AT2G16060.1; AT2G16060.
DR GeneID; 816103; -.
DR Gramene; AT2G16060.1; AT2G16060.1; AT2G16060.
DR KEGG; ath:AT2G16060; -.
DR Araport; AT2G16060; -.
DR TAIR; locus:2052981; AT2G16060.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_11_2_1; -.
DR InParanoid; O24520; -.
DR OMA; MRQGYQD; -.
DR OrthoDB; 1379813at2759; -.
DR PhylomeDB; O24520; -.
DR PRO; PR:O24520; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O24520; baseline and differential.
DR Genevisible; O24520; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0001666; P:response to hypoxia; TAS: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 3D-structure; Heme; Iron; Metal-binding; Reference proteome.
FT CHAIN 1..160
FT /note="Non-symbiotic hemoglobin 1"
FT /id="PRO_0000193011"
FT BINDING 69
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 104
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"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:3ZHW"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3ZHW"
FT HELIX 28..42
FT /evidence="ECO:0007829|PDB:3ZHW"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3ZHW"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3ZHW"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3ZHW"
FT HELIX 66..87
FT /evidence="ECO:0007829|PDB:3ZHW"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:3ZHW"
FT HELIX 111..128
FT /evidence="ECO:0007829|PDB:3ZHW"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:3ZHW"
FT HELIX 135..157
FT /evidence="ECO:0007829|PDB:3ZHW"
SQ SEQUENCE 160 AA; 18034 MW; 1C4C2170B0FA6F11 CRC64;
MESEGKIVFT EEQEALVVKS WSVMKKNSAE LGLKLFIKIF EIAPTTKKMF SFLRDSPIPA
EQNPKLKPHA MSVFVMCCES AVQLRKTGKV TVRETTLKRL GASHSKYGVV DEHFEVAKYA
LLETIKEAVP EMWSPEMKVA WGQAYDHLVA AIKAEMNLSN
