ID   HBL1_MEDSA              Reviewed;         160 AA.
AC   Q9FVL0;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Non-symbiotic hemoglobin 1;
DE   AltName: Full=MEDsa GLB1;
GN   Name=MHB1; Synonyms=GLB1;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Varia;
RX   PubMed=11018535; DOI=10.1016/s0014-5793(00)02049-4;
RA   Seregelyes C., Mustardy L., Ayaydin F., Sass L., Kovacs L., Endre G.,
RA   Lukacs N., Kovacs I., Vass I., Kiss G.B., Horvath G.V., Dudits D.;
RT   "Nuclear localization of a hypoxia-inducible novel non-symbiotic hemoglobin
RT   in cultured alfalfa cells.";
RL   FEBS Lett. 482:125-130(2000).
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.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm. Note=But not in the
CC       nucleolus, and to a lower extent, cytoplasmic.
CC   -!- TISSUE SPECIFICITY: Root specific.
CC   -!- INDUCTION: By hypoxia, but not by cold stress.
CC   -!- MISCELLANEOUS: Constant level of protein accumulation after induction
CC       by hypoxia may indicate a higher turnover.
CC   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR   EMBL; AF172172; AAG29748.1; -; mRNA.
DR   AlphaFoldDB; Q9FVL0; -.
DR   SMR; Q9FVL0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
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   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   PANTHER; PTHR22924; PTHR22924; 1.
DR   Pfam; PF00042; Globin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Heme; Iron; Metal-binding; Nucleus; Stress response.
FT   CHAIN           1..160
FT                   /note="Non-symbiotic hemoglobin 1"
FT                   /id="PRO_0000193020"
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"
SQ   SEQUENCE   160 AA;  17958 MW;  A4425F7E6F6DEB4B CRC64;
     MGTLDTKGFT EEQEALVVKS WNAMKKNSAE LGLKLFLKIF EIAPSAQKLF SFLKDSKVPL
     EQNTKLKPHA MSVFLMTCES AVQLRKSGKV TVRESSLKKL GANHFKYGVV DEHFEVTKFA
     LLETIKEAVP EMWSPAMKNA WGEAYDQLVN AIKSEMKPSS