HBAD_CHICK
ID HBAD_CHICK Reviewed; 141 AA.
AC P02001; Q549K7; Q78AJ9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Hemoglobin subunit alpha-D;
DE AltName: Full=Alpha-D-globin;
DE AltName: Full=Hemoglobin alpha-D chain;
GN Name=HBAD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP PRELIMINARY PROTEIN SEQUENCE.
RX PubMed=1225908;
RA Takei H., Ota Y., Wu K.C., Kiyohara T., Matsuda G.;
RT "Amino acid sequence of the alpha chain of chicken AI hemoglobin.";
RL J. Biochem. 77:1345-1347(1975).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6273837; DOI=10.1073/pnas.78.10.5998;
RA Dodgson J.B., McCune K.C., Rusling D.J., Krust A., Engel J.D.;
RT "Adult chicken alpha-globin genes alpha A and alpha D: no anemic shock
RT alpha-globin exists in domestic chickens.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:5998-6002(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6300093; DOI=10.1016/s0021-9258(18)32669-3;
RA Dodgson J.B., Engel J.D.;
RT "The nucleotide sequence of the adult chicken alpha-globin genes.";
RL J. Biol. Chem. 258:4623-4629(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=White leghorn;
RX PubMed=1656392; DOI=10.1093/nar/19.19.5321;
RA Lewis W., Lee J.D., Dodgson J.B.;
RT "Adult chicken alpha-globin gene expression in transfected QT6 quail cells:
RT evidence for a negative regulatory element in the alpha D gene region.";
RL Nucleic Acids Res. 19:5321-5329(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11157800; DOI=10.1093/hmg/10.4.371;
RA Flint J., Tufarelli C., Peden J., Clark K., Daniels R.J., Hardison R.,
RA Miller W., Philipsen S., Tan-Un K.C., McMorrow T., Frampton J., Alter B.P.,
RA Frischauf A.-M., Higgs D.R.;
RT "Comparative genome analysis delimits a chromosomal domain and identifies
RT key regulatory elements in the alpha globin cluster.";
RL Hum. Mol. Genet. 10:371-382(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhao Z., Sjakste N., De Moura-Gallo C.V., Ioudinkova E.S., Razin S.V.,
RA Scherrer K.;
RT "Organization of the chicken domain of alpha-globin genes.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 1-63 AND 94-122.
RC TISSUE=Embryo;
RX PubMed=7054172; DOI=10.1016/s0021-9258(19)68242-6;
RA Chapman B.S., Hood L.E., Tobin A.J.;
RT "Minor early embryonic chick hemoglobin M. Amino acid sequences of the
RT epsilon and alpha D chains.";
RL J. Biol. Chem. 257:651-658(1982).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10037733; DOI=10.1074/jbc.274.10.6411;
RA Knapp J.E., Oliveira M.A., Xie Q., Ernst S.R., Riggs A.F., Hackert M.L.;
RT "The structural and functional analysis of the hemoglobin D component from
RT chicken.";
RL J. Biol. Chem. 274:6411-6420(1999).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha-D chains and two beta chains. The
CC component D forms dimers of tetramers upon deoxygenation.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- DEVELOPMENTAL STAGE: In birds, the alpha-D chain occurs in a minor
CC hemoglobin component, called hemoglobin d, which is expressed in late
CC embryonic and adult life.
CC -!- MISCELLANEOUS: Ref.6 chain was isolated from Hbm, the least abundant of
CC the four early chick hemoglobins.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; M15378; AAA48584.1; -; Genomic_DNA.
DR EMBL; V00411; CAA23702.1; -; Genomic_DNA.
DR EMBL; X59989; CAA42605.1; -; Genomic_DNA.
DR EMBL; AY016020; AAL35403.1; -; Genomic_DNA.
DR EMBL; AF098919; AAM09072.1; -; Genomic_DNA.
DR PIR; B92421; HACH1.
DR RefSeq; NP_001004375.1; NM_001004375.2.
DR PDB; 1HBR; X-ray; 2.30 A; A/C=1-141.
DR PDBsum; 1HBR; -.
DR AlphaFoldDB; P02001; -.
DR SMR; P02001; -.
DR IntAct; P02001; 1.
DR STRING; 9031.ENSGALP00000038912; -.
DR Allergome; 8240; Gal d HG.
DR PaxDb; P02001; -.
DR Ensembl; ENSGALT00000060227; ENSGALP00000053010; ENSGALG00000031597.
DR GeneID; 416651; -.
DR KEGG; gga:416651; -.
DR CTD; 102090670; -.
DR VEuPathDB; HostDB:geneid_416651; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000165231; -.
DR HOGENOM; CLU_003827_10_2_1; -.
DR InParanoid; P02001; -.
DR OMA; HAAFDKF; -.
DR OrthoDB; 1398217at2759; -.
DR PhylomeDB; P02001; -.
DR EvolutionaryTrace; P02001; -.
DR PRO; PR:P02001; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000031597; Expressed in lung and 13 other tissues.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..141
FT /note="Hemoglobin subunit alpha-D"
FT /id="PRO_0000052822"
FT BINDING 58
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 87
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 16
FT /note="K -> R (in Ref. 4 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="F -> L (in Ref. 2; AAA48584)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="V -> C (in Ref. 2 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..110
FT /note="LA -> RL (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 53..71
FT /evidence="ECO:0007829|PDB:1HBR"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:1HBR"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:1HBR"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1HBR"
SQ SEQUENCE 141 AA; 15695 MW; 1FE426969B7B5384 CRC64;
MLTAEDKKLI QQAWEKAASH QEEFGAEALT RMFTTYPQTK TYFPHFDLSP GSDQVRGHGK
KVLGALGNAV KNVDNLSQAM AELSNLHAYN LRVDPVNFKL LSQCIQVVLA VHMGKDYTPE
VHAAFDKFLS AVSAVLAEKY R
