ID HBB_TREBE Reviewed; 147 AA. AC P80044; O93350; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 134. DE RecName: Full=Hemoglobin subunit beta; DE AltName: Full=Beta-globin; DE AltName: Full=Hemoglobin beta chain; GN Name=hbb; OS Trematomus bernacchii (Emerald rockcod) (Pseudotrematomus bernacchii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Trematomus. OX NCBI_TaxID=40690; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9671736; DOI=10.1073/pnas.95.15.8670; RA Bargelloni L., Marcato S., Patarnello T.; RT "Antarctic fish hemoglobins: evidence for adaptive evolution at subzero RT temperature."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8670-8675(1998). RN [2] RP PROTEIN SEQUENCE OF 2-147, FUNCTION, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY RP (2.5 ANGSTROMS). RC TISSUE=Blood; RX PubMed=1560461; DOI=10.1016/0022-2836(92)91007-c; RA Camardella L., Caruso C., D'Avino R., di Prisco G., Rutigliano B., RA Tamburrini M., Fermi G., Perutz M.F.; RT "Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid RT sequence, oxygen equilibria and crystal structure of its carbonmonoxy RT derivative."; RL J. Mol. Biol. 224:449-460(1992). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-147 IN COMPLEX WITH HEME. RX PubMed=7623382; DOI=10.1006/jmbi.1995.0405; RA Ito N., Komiyama N.H., Fermi G.; RT "Structure of deoxyhaemoglobin of the antarctic fish Pagothenia bernacchii RT with an analysis of the structural basis of the Root effect by comparison RT of the liganded and unliganded haemoglobin structures."; RL J. Mol. Biol. 250:648-658(1995). CC -!- FUNCTION: Involved in oxygen transport from gills to the various CC peripheral tissues. {ECO:0000269|PubMed:1560461}. CC -!- SUBUNIT: Hb1 is a heterotetramer of two alpha chains and two beta CC chains. {ECO:0000269|PubMed:1560461}. CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- MISCELLANEOUS: This fish has three hemoglobins: Hb1 (major) and two CC minor hemoglobins (about 1-2% of the total). Hb1 has a strong alkaline CC Bohr effect, and at low pH exhibits the reduced ligand affinity and CC cooperativity that comprise the Root effect. 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; AF067570; AAC41388.1; -; mRNA. DR PIR; S21678; S21678. DR PDB; 1HBH; X-ray; 2.20 A; B/D=2-147. DR PDB; 1PBX; X-ray; 2.50 A; B=2-147. DR PDB; 1S5X; X-ray; 2.40 A; B=2-147. DR PDB; 1S5Y; X-ray; 2.50 A; B/D=2-147. DR PDB; 2H8D; X-ray; 1.78 A; B/D=2-147. DR PDB; 2H8F; X-ray; 1.30 A; B/D=2-147. DR PDB; 2PEG; X-ray; 1.48 A; B=2-147. DR PDB; 3GKV; X-ray; 1.40 A; B=2-147. DR PDB; 3GQG; X-ray; 1.73 A; B/D=2-147. DR PDB; 4G51; X-ray; 2.50 A; B/D=2-147. DR PDB; 4IRO; X-ray; 2.20 A; B/D=2-147. DR PDB; 4ODC; X-ray; 1.54 A; B=2-147. DR PDBsum; 1HBH; -. DR PDBsum; 1PBX; -. DR PDBsum; 1S5X; -. DR PDBsum; 1S5Y; -. DR PDBsum; 2H8D; -. DR PDBsum; 2H8F; -. DR PDBsum; 2PEG; -. DR PDBsum; 3GKV; -. DR PDBsum; 3GQG; -. DR PDBsum; 4G51; -. DR PDBsum; 4IRO; -. DR PDBsum; 4ODC; -. DR AlphaFoldDB; P80044; -. DR SMR; P80044; -. DR MINT; P80044; -. DR OrthoDB; 3779905at2759; -. DR EvolutionaryTrace; P80044; -. DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro. 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 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: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 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding; KW Oxygen transport; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1560461" FT CHAIN 2..147 FT /note="Hemoglobin subunit beta" FT /id="PRO_0000053046" 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 /evidence="ECO:0007744|PDB:1S5X, ECO:0007744|PDB:1S5Y, FT ECO:0007744|PDB:2PEG, ECO:0007744|PDB:4IRO" 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 /evidence="ECO:0000269|PubMed:7623382, FT ECO:0007744|PDB:1HBH, ECO:0007744|PDB:1PBX, FT ECO:0007744|PDB:1S5X, ECO:0007744|PDB:1S5Y, FT ECO:0007744|PDB:2H8D, ECO:0007744|PDB:2H8F, FT ECO:0007744|PDB:2PEG, ECO:0007744|PDB:3GKV, FT ECO:0007744|PDB:3GQG, ECO:0007744|PDB:4G51, FT ECO:0007744|PDB:4IRO, ECO:0007744|PDB:4ODC" FT HELIX 6..18 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 21..35 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 37..42 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:2H8D" FT HELIX 52..56 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 59..70 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 73..76 FT /evidence="ECO:0007829|PDB:2H8F" FT TURN 77..80 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 87..95 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 102..119 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 125..144 FT /evidence="ECO:0007829|PDB:2H8F" SQ SEQUENCE 147 AA; 16264 MW; 0C9A4B07948A81B2 CRC64; MVEWTDKERS IISDIFSHMD YDDIGPKALS RCLIVYPWTQ RHFSGFGNLY NAEAIIGNAN VAAHGIKVLH GLDRGVKNMD NIAATYADLS TLHSEKLHVD PDNFKLLSDC ITIVLAAKMG HAFTAETQGA FQKFLAVVVS ALGKQYH //