ID GLB32_LOTJA Reviewed; 168 AA.
AC I3SAV1;
DT 29-MAY-2024, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 24-JUL-2024, entry version 30.
DE RecName: Full=Group 2 truncated hemoglobin 3-2 {ECO:0000303|PubMed:21073469, ECO:0000305|PubMed:34387337};
DE Short=LjGlb3-2 {ECO:0000303|PubMed:21073469, ECO:0000303|PubMed:34387337};
DE AltName: Full=Phytoglobin 3.2 {ECO:0000305};
DE Short=Phytogb3.2 {ECO:0000305};
DE AltName: Full=Two-on-two hemoglobin 3-2 {ECO:0000305|PubMed:34387337};
DE Short=2-on-2 hemoglobin 3-2 {ECO:0000305|PubMed:34387337};
GN Name=GLB3-2 {ECO:0000303|PubMed:21073469, ECO:0000303|PubMed:34387337};
GN OrderedLocusNames=LotjaGi1g1v0172000 {ECO:0000305|PubMed:34387337};
GN ORFNames=Lj1g3v0948590 {ECO:0000305|PubMed:34387337};
OS Lotus japonicus (Lotus corniculatus var. japonicus).
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; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY NITRIC OXIDE, AND
RP REPRESSION BY CYTOKININS.
RC STRAIN=cv. MG20;
RX PubMed=21073469; DOI=10.1111/j.1469-8137.2010.03527.x;
RA Bustos-Sanmamed P., Tovar-Mendez A., Crespi M., Sato S., Tabata S.,
RA Becana M.;
RT "Regulation of nonsymbiotic and truncated hemoglobin genes of Lotus
RT japonicus in plant organs and in response to nitric oxide and hormones.";
RL New Phytol. 189:765-776(2011).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Gifu B-129;
RX PubMed=34387337; DOI=10.1093/jxb/erab376;
RA Villar I., Rubio M.C., Calvo-Begueria L., Perez-Rontome C., Larrainzar E.,
RA Wilson M.T., Sandal N., Mur L.A., Wang L., Reeder B., Duanmu D.,
RA Uchiumi T., Stougaard J., Becana M.;
RT "Three classes of hemoglobins are required for optimal vegetative and
RT reproductive growth of Lotus japonicus: genetic and biochemical
RT characterization of LjGlb2-1.";
RL J. Exp. Bot. 72:7778-7791(2021).
CC -!- FUNCTION: Hemoglobin-like protein that exhibits an unusual
CC concentration-independent binding of O(2) and CO (By similarity).
CC Required for general plant development and during nodulation
CC (PubMed:34387337). May promote shoot organogenesis from root explants
CC (By similarity). {ECO:0000250|UniProtKB:Q67XG0,
CC ECO:0000269|PubMed:34387337}.
CC -!- SUBUNIT: Homodimer when ferric. {ECO:0000250|UniProtKB:Q67XG0}.
CC -!- TISSUE SPECIFICITY: Equally expressed in all organs, including root
CC nodules, leaves, roots, stems, flowers and fruits.
CC {ECO:0000269|PubMed:21073469}.
CC -!- DEVELOPMENTAL STAGE: In nodules, mainly localized in the cortex, and,
CC to a lower extent, in the vascular bundles and infected tissues
CC (PubMed:21073469). As nodule aged, restricted in the mid-cortex and
CC inner cortex, vascular bundles, and periphery of infected zone
CC (PubMed:21073469). {ECO:0000269|PubMed:21073469}.
CC -!- INDUCTION: Repressed by cytokinins (CK, an equimolar mixture of kinetin
CC and 6-benzyl-aminopurine) in roots. {ECO:0000269|PubMed:21073469}.
CC -!- DISRUPTION PHENOTYPE: Reduced shoots, roots and leaves size and fewer
CC leaves, but increased number of flowers and small pods containing less
CC seeds (PubMed:34387337). Delayed nodules formation of smaller size
CC (PubMed:34387337). {ECO:0000269|PubMed:34387337}.
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group II
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT137598; AFK37393.1; -; mRNA.
DR AlphaFoldDB; I3SAV1; -.
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; IEA:UniProtKB-KW.
DR GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR CDD; cd19755; TrHb2_AtGlb3-like_O; 1.
DR Gene3D; 1.10.490.10; Globins; 1.
DR InterPro; IPR044203; GlbO/GLB3-like.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR PANTHER; PTHR47366; TWO-ON-TWO HEMOGLOBIN-3; 1.
DR PANTHER; PTHR47366:SF1; TWO-ON-TWO HEMOGLOBIN-3; 1.
DR Pfam; PF01152; Bac_globin; 1.
DR SUPFAM; SSF46458; Globin-like; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Metal-binding; Nodulation; Oxygen transport; Transport.
FT CHAIN 1..168
FT /note="Group 2 truncated hemoglobin 3-2"
FT /id="PRO_0000460304"
FT BINDING 98
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:0000250|UniProtKB:Q67XG0"
SQ SEQUENCE 168 AA; 19522 MW; D68B22689B4EC341 CRC64;
MQSLQHKASE WSGVPSDEAF AIDDTNRFLK LGLQTFINLS TNFYNRVYDD DEEWFRSIFA
DSEKQNAIQN QYEFFVQRMG GPPLFSQRRG HPALIGRHRP FPVTHEAAER WLHHMQQALD
STPDIDDDSK IKMQNFFRHT AYFLVAGNEL KKQNEQMPCK HAAGSDNS
//