ID   HBB_AYTFU               Reviewed;         147 AA.
AC   P84792;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
OS   Aythya fuligula (Tufted duck) (Anas fuligula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Aythyinae; Aythya.
OX   NCBI_TaxID=219594;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-147, AND MASS SPECTROMETRY.
RC   TISSUE=Erythrocyte {ECO:0000269|PubMed:11829480};
RX   PubMed=11829480; DOI=10.1006/bbrc.2002.6399;
RA   Abbasi A., Lutfullah G.;
RT   "Molecular basis of bird respiration: primary hemoglobin structure
RT   component from Tufted duck (Aythya fuligula, Anseriformes)-role of
RT   alpha99Arg in formation of a complex salt bridge network.";
RL   Biochem. Biophys. Res. Commun. 291:176-184(2002).
RN   [2] {ECO:0000305}
RP   MASS SPECTROMETRY.
RX   PubMed=15567161; DOI=10.1016/j.bbrc.2004.10.209;
RA   Lutfullah G., Ali S.A., Abbasi A.;
RT   "Molecular mechanism of high altitude respiration: primary structure of a
RT   minor hemoglobin component from Tufted duck (Aythya fuligula,
RT   Anseriformes).";
RL   Biochem. Biophys. Res. Commun. 326:123-130(2005).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues. The beta chain is a component of adult hemoglobin A
CC       and D. {ECO:0000305}.
CC   -!- SUBUNIT: Heterotetramer of two alpha (or alpha-D) and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=16321.19; Mass_error=1.16; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11829480};
CC   -!- MASS SPECTROMETRY: Mass=16321; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15567161};
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P84792; -.
DR   SMR; P84792; -.
DR   Proteomes; UP000504639; Genome assembly.
DR   GO; GO:0005833; C:hemoglobin complex; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0015671; P:oxygen transport; IDA:UniProtKB.
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   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11829480"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000227533"
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"
SQ   SEQUENCE   147 AA;  16452 MW;  7E0DC7EF297296A9 CRC64;
     MVHWTAEEKQ IITGLWGKVN VADCGAEALA RLLIVYPWTQ RFFSSFGNLS SPTAILGNPM
     VRAHGKKVLT SFGDAVKNLD NIKNTFAQLS ELHCDKLHVD PENFRLLGDI LIVVLAAHFS
     KEFTPECQAA WQKLVRVVAH ALARKYH