ID   HBA3_LITCT              Reviewed;         141 AA.
AC   P02011;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Hemoglobin subunit alpha-3;
DE   AltName: Full=Alpha-3-globin;
DE   AltName: Full=Hemoglobin alpha-3 chain;
DE   AltName: Full=Hemoglobin alpha-III chain, larval;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX   PubMed=6965939; DOI=10.1016/s0021-9258(19)85697-1;
RA   Maruyama T., Watt K.W.K., Riggs A.;
RT   "Hemoglobins of the tadpole of the bullfrog, Rana catesbeiana. Amino acid
RT   sequence of the alpha chain of a major component.";
RL   J. Biol. Chem. 255:3285-3293(1980).
CC   -!- FUNCTION: This is a tadpole (larval) alpha chain.
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   PIR; A02340; HAFG3T.
DR   AlphaFoldDB; P02011; -.
DR   SMR; P02011; -.
DR   iPTMnet; P02011; -.
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   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..141
FT                   /note="Hemoglobin subunit alpha-3"
FT                   /id="PRO_0000052749"
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   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:6965939"
SQ   SEQUENCE   141 AA;  14874 MW;  7B87E60248EDDD0F CRC64;
     SLSASEKAAV LSIVGKIGSQ GSALGSEALT RLFLSFPQTK TYFPHFDLTP GSADLNTHGG
     KIINALAGAA NHLDDLAGNL SSLSDLHAYN LRVDPGNFPL LAHIIQVVLA THFPGDFTAE
     VQAAWDKFLA LVSAVLTSKY R