ID   HBA4_XENLA              Reviewed;         142 AA.
AC   P06637; Q5D089;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Hemoglobin subunit alpha-4;
DE   AltName: Full=Alpha-4-globin;
DE   AltName: Full=Alpha-T4;
DE   AltName: Full=Hemoglobin alpha-4 chain;
GN   Name=hba4;
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=2993998; DOI=10.1093/nar/13.15.5407;
RA   Banville D., Williams J.G.;
RT   "The pattern of expression of the Xenopus laevis tadpole alpha-globin genes
RT   and the amino acid sequence of the three major tadpole alpha-globin
RT   polypeptides.";
RL   Nucleic Acids Res. 13:5407-5421(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This is a larval (tadpole) alpha-globin.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- POLYMORPHISM: Alpha T4 may be an allele of alpha T3.
CC       {ECO:0000305|PubMed:2993998}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; X02797; CAA26565.1; -; mRNA.
DR   EMBL; BC053833; AAH53833.1; -; mRNA.
DR   PIR; B24338; B24338.
DR   RefSeq; NP_001079749.1; NM_001086280.2.
DR   AlphaFoldDB; P06637; -.
DR   SMR; P06637; -.
DR   MaxQB; P06637; -.
DR   DNASU; 379438; -.
DR   GeneID; 379438; -.
DR   KEGG; xla:379438; -.
DR   CTD; 379438; -.
DR   Xenbase; XB-GENE-6255815; hba4.S.
DR   OMA; RIMAFIN; -.
DR   OrthoDB; 1398217at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 379438; Expressed in internal ear and 6 other tissues.
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   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-4"
FT                   /id="PRO_0000052810"
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"
SQ   SEQUENCE   142 AA;  15453 MW;  60D65877B4AC7D29 CRC64;
     MTLTDSDKAA IVALWGKIAP QASAIGAEAL ERLFLSYPQT KTYFSHFDVS HGSADLSNHG
     GKVVNALGEA AKHIDDLDSA LSTLSDLHAY NLRIDPGNFK LLSHTIQVTL AIHFHKEFDA
     ATQAAWDKFL AEVATVLTSK YR