ID   HBA2_XENLA              Reviewed;         142 AA.
AC   P02013;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Hemoglobin subunit alpha-2;
DE   AltName: Full=Alpha-2-globin;
DE   AltName: Full=Hemoglobin alpha-2 chain;
DE   AltName: Full=Hemoglobin alpha-minor chain;
GN   Name=hba2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6298748; DOI=10.1093/nar/11.5.1543;
RA   Knoechel W., Meyerhof W., Hummel S., Grundmann U.;
RT   "Molecular cloning and sequencing of mRNAs coding for minor adult globin
RT   polypeptides of Xenopus laevis.";
RL   Nucleic Acids Res. 11:1543-1553(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3148743; DOI=10.1007/bf02143498;
RA   Stalder J., Wirthmueller U., Beck J., Gruber A., Meyerhof W., Knoechel W.,
RA   Weber R.;
RT   "Primary structure and evolutionary relationship between the adult alpha-
RT   globin genes and their 5'-flanking regions of Xenopus laevis and Xenopus
RT   tropicalis.";
RL   J. Mol. Evol. 28:64-71(1988).
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; X01559; CAA25712.1; -; mRNA.
DR   EMBL; X14261; CAA32474.1; -; Genomic_DNA.
DR   PIR; A02342; HAXL2.
DR   AlphaFoldDB; P02013; -.
DR   SMR; P02013; -.
DR   Proteomes; UP000186698; Genome assembly.
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; 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   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Oxygen transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..142
FT                   /note="Hemoglobin subunit alpha-2"
FT                   /id="PRO_0000052808"
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        24
FT                   /note="K -> T (in Ref. 2; CAA32474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="S -> L (in Ref. 2; CAA32474)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   142 AA;  15774 MW;  E42356ACEA29283F CRC64;
     MLLSADDKKH IKAIMPSIAA HGDKFGGEAS YRMFLVNPKT KTYFPSFDFH HNSKQITSHG
     KKVVDALNEA ANHLDNIAGS MSKLSDLHAY DLRVDPGNFP LLAHNLLVVV AMHFPKQFDP
     ATHKALDKFL ATVSTVLTSK YR