HBAD_ANAPL
ID HBAD_ANAPL Reviewed; 141 AA.
AC P04442;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Hemoglobin subunit alpha-D;
DE AltName: Full=Alpha-D-globin;
DE AltName: Full=Hemoglobin alpha-D chain;
GN Name=HBAD;
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].
RC STRAIN=Pekin breed;
RX PubMed=6547470;
RA Frankis R.C., Paddock G.V.;
RT "Nucleotide sequences for the duck globin mRNAs.";
RL J. Mol. Appl. Genet. 2:381-391(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-141.
RC STRAIN=Pekin breed;
RX PubMed=6888376; DOI=10.1007/bf00777480;
RA Ben-Tahar S., Scherrer K.;
RT "Determination of the primary sequence of the duck alpha D globin mRNA and
RT comparison of all adult duck and chick globin mRNA sequences.";
RL Mol. Biol. Rep. 9:101-113(1983).
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.
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 -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; M16787; AAA49149.1; -; mRNA.
DR EMBL; K01942; AAA49220.1; -; mRNA.
DR PIR; S13971; HADKDD.
DR RefSeq; NP_001297719.1; NM_001310790.1.
DR AlphaFoldDB; P04442; -.
DR SMR; P04442; -.
DR Ensembl; ENSAPLT00020028994; ENSAPLP00020026923; ENSAPLG00020018296.
DR GeneID; 101800520; -.
DR KEGG; apla:101800520; -.
DR OrthoDB; 1398217at2759; -.
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; IPR002340; Hemoglobin_zeta.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
DR PRINTS; PR00816; ZETAHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT CHAIN 1..141
FT /note="Hemoglobin subunit alpha-D"
FT /id="PRO_0000052816"
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"
SQ SEQUENCE 141 AA; 15746 MW; 7F23AC9F0170A6EB CRC64;
MLTAEDKKLI TQLWEKVAGH QEEFGSEALQ RMFLAYPQTK TYFPHFDLHP GSEQVRGHGK
KVAAALGNAV KSLDNLSQAL SELSNLHAYN LRVDPVNFKL LAQCFQVVLA AHLGKDYSPE
MHAAFDKFMS AVAAVLAEKY R
