ID   HBB_ANAPL               Reviewed;         147 AA.
AC   P02114;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6894908; DOI=10.1016/0378-1119(81)90144-x;
RA   Hampe A., Therwath A., Soriano P., Galibert F.;
RT   "Nucleotide sequence analysis of a cloned duck beta-globin cDNA.";
RL   Gene 14:11-21(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}.
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DR   EMBL; J00926; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A02434; HBDK.
DR   PDB; 3EOK; X-ray; 2.10 A; B=2-147.
DR   PDBsum; 3EOK; -.
DR   AlphaFoldDB; P02114; -.
DR   SMR; P02114; -.
DR   EvolutionaryTrace; P02114; -.
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; Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052868"
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   HELIX           6..18
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           37..46
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           52..56
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           59..77
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           87..95
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           102..119
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           125..142
FT                   /evidence="ECO:0007829|PDB:3EOK"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:3EOK"
SQ   SEQUENCE   147 AA;  16450 MW;  ED86C6CB0F34E8E1 CRC64;
     MVHWTAEEKQ LITGLWGKVN VADCGAEALA RLLIVYPWTQ RFFASFGNLS SPTAILGNPM
     VRAHGKKVLT SFGDAVKNLD NIKNTFAQLS ELHCDKLHVD PENFRLLGDI LIIVLAAHFT
     KDFTPECQAA WQKLVRVVAH ALARKYH