HBA2_OTOCR
ID HBA2_OTOCR Reviewed; 142 AA.
AC P01939;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Hemoglobin subunit alpha-B;
DE AltName: Full=Alpha-B-globin;
DE AltName: Full=Alpha-II;
DE AltName: Full=Hemoglobin alpha-B chain;
GN Name=HBAB;
OS Otolemur crassicaudatus (Brown greater galago) (Galago crassicaudatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=9463;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3586010; DOI=10.1016/0022-2836(86)90022-7;
RA Sawada I., Schmid C.W.;
RT "Primate evolution of the alpha-globin gene cluster and its Alu-like
RT repeats.";
RL J. Mol. Biol. 192:693-709(1986).
RN [2]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=4005042; DOI=10.1515/bchm3.1985.366.1.265;
RA Watanabe B., Fujii T., Nakashima Y., Maita T., Matsuda G.;
RT "Amino-acid sequences of the alpha and beta chains of adult hemoglobins of
RT the Grand Galago, Galago crassicaudatus.";
RL Biol. Chem. Hoppe-Seyler 366:265-269(1985).
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; M29648; AAA35449.1; -; Genomic_DNA.
DR PIR; A02261; HAGC.
DR PIR; A25597; A25597.
DR PIR; B25597; B25597.
DR AlphaFoldDB; P01939; -.
DR SMR; P01939; -.
DR PRIDE; P01939; -.
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 carrier activity; IEA:UniProtKB-KW.
DR CDD; cd08927; Hb-alpha-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; IPR002338; Hemoglobin_a-typ.
DR InterPro; IPR002339; Hemoglobin_pi.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
DR PRINTS; PR00815; PIHAEM.
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 Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4005042"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-B"
FT /id="PRO_0000052639"
FT BINDING 59
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 88
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 CONFLICT 20
FT /note="A -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="L -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="R -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="F -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="L -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 15520 MW; 5F1FF1A83E4868CA CRC64;
MVLSPTDKSN VKAAWEKVGA HAGDYGAEAL ERMFLSFPTT KTYFPHFDLS HGSTQVKGHG
KKVADALTNA VLHVDDMPSA LSALSDLHAH KLRVDPVNFK LLRHCLLVTL ACHHPAEFTP
AVHASLDKFM ASVSTVLTSK YR