HBA1_XENLA
ID HBA1_XENLA Reviewed; 142 AA.
AC P02012; Q6GP50;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Hemoglobin subunit alpha-1;
DE AltName: Full=Alpha-1-globin;
DE AltName: Full=Hemoglobin alpha-1 chain;
DE AltName: Full=Hemoglobin alpha-major chain;
GN Name=hba1;
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=6298747; DOI=10.1093/nar/11.5.1537;
RA Kay R.M., Harris R., Patient R.K., Williams J.G.;
RT "Complete nucleotide sequence of a cloned cDNA derived from the major adult
RT alpha-globin mRNA of X. laevis.";
RL Nucleic Acids Res. 11:1537-1542(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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-100 AND 127-142.
RX PubMed=7265209; DOI=10.1016/0022-2836(81)90216-3;
RA Partington G.A., Baralle F.E.;
RT "Isolation of a Xenopus laevis alpha-globin gene.";
RL J. Mol. Biol. 145:463-470(1981).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-142.
RX PubMed=6249685; DOI=10.1016/0012-1606(80)90326-7;
RA Richardson C., Cappello J., Cochran M.D., Armentrout R.W., Brown R.D.;
RT "Partial sequence analysis of Xenopus alpha- and beta-globin mRNA as
RT determined from recombinant DNA plasmids.";
RL Dev. Biol. 78:161-172(1980).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 129-142.
RX PubMed=7001356; DOI=10.1093/nar/8.12.2691;
RA Kay R.M., Harris R., Patient R.K., Williams J.G.;
RT "Molecular cloning of cDNA sequences coding for the major alpha- and beta-
RT globin polypeptides of adult Xenopus laevis.";
RL Nucleic Acids Res. 8:2691-2707(1980).
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; J00972; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X14259; CAA32472.1; -; Genomic_DNA.
DR EMBL; BC073294; AAH73294.1; -; mRNA.
DR EMBL; J00973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J00974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M15381; AAA49662.1; -; Genomic_DNA.
DR EMBL; M10577; AAA49732.1; -; mRNA.
DR PIR; A93456; HAXL1.
DR RefSeq; XP_018092516.1; XM_018237027.1.
DR AlphaFoldDB; P02012; -.
DR SMR; P02012; -.
DR GeneID; 108702027; -.
DR KEGG; xla:108702027; -.
DR CTD; 108702027; -.
DR Xenbase; XB-GENE-17345270; hba1.L.
DR OMA; ARMFIAY; -.
DR OrthoDB; 1398217at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 108702027; Expressed in lung and 19 other tissues.
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-1"
FT /id="PRO_0000052807"
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 29
FT /note="A -> S (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="S -> N (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..71
FT /note="EAS -> KLH (in Ref. 5; AAA49662)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="G -> S (in Ref. 5; AAA49662)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="F -> L (in Ref. 5; AAA49662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 15747 MW; 19EA7E6034CB64AD CRC64;
MLLSADDKKH IKAIMPAIAA HGDKFGGEAL YRMFIVNPKT KTYFPSFDFH HNSKQISAHG
KKVVDALNEA SNHLDNIAGS MSKLSDLHAY DLRVDPGNFP LLAHNILVVV AMNFPKQFDP
ATHKALDKFL ATVSTVLTSK YR
