ID HBB_DASNO Reviewed; 147 AA. AC P02087; Q45XI0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 29-MAY-2024, entry version 116. DE RecName: Full=Hemoglobin subunit beta; DE AltName: Full=Beta-globin; DE AltName: Full=Hemoglobin beta chain; GN Name=HBB; OS Dasypus novemcinctus (Nine-banded armadillo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Xenarthra; Cingulata; Dasypodidae; Dasypus. OX NCBI_TaxID=9361; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Sloan A.M., Campbell K.L.; RT "Atypical molecular evolution of afrotherian and xenarthran beta-globin RT cluster genes."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 2-147. RX PubMed=7236709; DOI=10.1016/0005-2795(81)90148-3; RA de Jong W.W., Leunissen J.A.M., Cuijpers H.T.; RT "Primary structure of the major beta-chain of armadillo (Dasypus RT novemcinctus) haemoglobin."; RL Biochim. Biophys. Acta 668:57-62(1981). 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. 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 EMBL; DQ091213; AAZ22684.1; -; Genomic_DNA. DR PIR; A02403; HBDN. DR AlphaFoldDB; P02087; -. DR SMR; P02087; -. DR HOGENOM; CLU_003827_10_0_1; -. DR TreeFam; TF333268; -. DR Proteomes; UP000694943; Unplaced. 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:0031721; F:hemoglobin alpha binding; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:UniProtKB-KW. 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 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 PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1. DR PANTHER; PTHR11442:SF42; HEMOGLOBIN SUBUNIT BETA; 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 Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding; KW Oxygen transport; Phosphoprotein; S-nitrosylation; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P02086, FT ECO:0000269|PubMed:7236709" FT CHAIN 2..147 FT /note="Hemoglobin subunit beta" FT /id="PRO_0000052945" FT DOMAIN 3..147 FT /note="Globin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238" FT BINDING 64 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 BINDING 93 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 MOD_RES 2 FT /note="N-acetylvaline" FT /evidence="ECO:0000250|UniProtKB:P02086" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68871" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P68871" FT MOD_RES 83 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P68871" FT MOD_RES 94 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P68871" FT MOD_RES 145 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P68871" FT CONFLICT 24 FT /note="C -> H (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 105 FT /note="K -> R (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="L -> M (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 125..126 FT /note="WH -> HW (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 133 FT /note="K -> R (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 147 AA; 16351 MW; D19F317BDC662898 CRC64; MVNLTSDEKT AVLALWNKVD VEDCGGEALG RLLVVYPWTQ RFFESFGDLS TPAAVFANAK VKAHGKKVLT SFGEGMNHLD NLKGTFAKLS ELHCDKLHVD PENFKLLGNM LVVVLARHFG KEFDWHMHAC FQKVVAGVAN ALAHKYH //