HBB_TREBE
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 03-AUG-2022, entry version 130.
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}.
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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 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; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR002337; Hemoglobin_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 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
