ID HBB_LATCH Reviewed; 146 AA. AC P23741; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 02-SEP-2026, entry version 105. DE RecName: Full=Hemoglobin subunit beta; DE AltName: Full=Beta-globin; DE AltName: Full=Hemoglobin beta chain; GN Name=HBB; OS Latimeria chalumnae (Coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897; RN [1] RP PROTEIN SEQUENCE. RX PubMed=1958318; DOI=10.1515/bchm3.1991.372.2.599; RA Gorr T., Kleinschmidt T., Sgouros J.G., Kasang L.; RT "A 'living fossil' sequence: primary structure of the coelacanth (Latimeria RT chalumnae) hemoglobin -- evolutionary and functional aspects."; RL Biol. Chem. Hoppe-Seyler 372:599-612(1991). RN [2] RP PHYLOGENETIC COMPARISONS. RX PubMed=2034288; DOI=10.1038/351394a0; RA Gorr T., Kleinschmidt T., Fricke H.; RT "Close tetrapod relationships of the coelacanth Latimeria indicated by RT haemoglobin sequences."; RL Nature 351:394-397(1991). CC -!- FUNCTION: Involved in oxygen transport from the lung to the various CC peripheral tissues. CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains (an CC easy dimerization is also reported). CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE- CC ProRule:PRU00238}. 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 PIR; S15449; S15449. DR AlphaFoldDB; P23741; -. DR SMR; P23741; -. DR FunCoup; P23741; 31. DR STRING; 7897.ENSLACP00000005370; -. DR eggNOG; KOG3378; Eukaryota. DR InParanoid; P23741; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0072562; C:blood microparticle; IEA:TreeGrafter. DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IEA:TreeGrafter. DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro. DR GO; GO:0031720; F:haptoglobin binding; IEA:TreeGrafter. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0043177; F:organic acid binding; IEA:TreeGrafter. DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. DR GO; GO:0005344; F:oxygen carrier activity; IEA:TreeGrafter. DR GO; GO:0004601; F:peroxidase activity; IEA:TreeGrafter. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter. DR CDD; cd08925; Hb-beta-like; 1. DR FunFam; 1.10.490.10:FF:000001; Hemoglobin subunit beta; 1. DR Gene3D; 1.10.490.10; Globins; 1. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin-like_sf. DR InterPro; IPR012292; Globin/Proto. DR InterPro; IPR002337; Hemoglobin_b. DR InterPro; IPR050056; Hemoglobin_oxygen_transport. DR PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1. DR PANTHER; PTHR11442:SF7; HEMOGLOBIN SUBUNIT EPSILON; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00814; BETAHAEM. DR SUPFAM; SSF46458; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport; KW Reference proteome; Transport. FT CHAIN 1..146 FT /note="Hemoglobin subunit beta" FT /id="PRO_0000052985" FT DOMAIN 2..146 FT /note="Globin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238" FT BINDING 63 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 92 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 146 AA; 16872 MW; E61EA7DBB67EFC52 CRC64; VHWTETERAT IETVYQKLHL DEVGREALTR LFIVYPWTTR YFKSFGDLSS SKAIASNPKV TEHGLKVMNK LTEAIHNLDH IKDLFHKLSE KHFHELHVDP QNFKLLSKCL IIVLATKLGK QLTPDVQATW EKLLSVVVAA LSREYH //