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 16-SEP-2015, entry version 91. 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; OC Mammalia; 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- RT globin 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 CC various 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 STRING; 9361.ENSDNOP00000001827; -. DR PRIDE; P02087; -. DR eggNOG; NOG269316; -. DR HOGENOM; HOG000036868; -. DR HOVERGEN; HBG009709; -. DR OrthoDB; EOG7B8S5H; -. DR TreeFam; TF333268; -. DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. DR GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.490.10; -; 1. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin-like. DR InterPro; IPR012292; Globin/Proto. DR InterPro; IPR002337; Haemoglobin_b. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00814; BETAHAEM. DR SUPFAM; SSF46458; SSF46458; 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 1 Removed. {ECO:0000250|UniProtKB:P02086, FT ECO:0000269|PubMed:7236709}. FT CHAIN 2 147 Hemoglobin subunit beta. FT /FTId=PRO_0000052945. FT METAL 64 64 Iron (heme distal ligand). FT METAL 93 93 Iron (heme proximal ligand). FT MOD_RES 2 2 N-acetylvaline. FT {ECO:0000250|UniProtKB:P02086}. FT MOD_RES 45 45 Phosphoserine. FT {ECO:0000250|UniProtKB:P68871}. FT MOD_RES 60 60 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P68871}. FT MOD_RES 83 83 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P68871}. FT MOD_RES 94 94 S-nitrosocysteine. FT {ECO:0000250|UniProtKB:P68871}. FT MOD_RES 145 145 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P68871}. FT CONFLICT 24 24 C -> H (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 105 105 K -> R (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 115 115 L -> M (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 125 126 WH -> HW (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 133 133 K -> R (in Ref. 2; AA sequence). FT {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 //