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 //