ID   HBAA_CHENI              Reviewed;         142 AA.
AC   P83135; Q60HV4;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Hemoglobin subunit alpha-A;
DE   AltName: Full=Alpha-A-globin;
DE   AltName: Full=Hemoglobin alpha-A chain;
GN   Name=HBAA {ECO:0000250|UniProtKB:P08850};
OS   Chelonoidis niger (Galapagos giant tortoise) (Geochelone nigra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Chelonoidis.
OX   NCBI_TaxID=66189;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC81725.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shishikura F.;
RT   "Nucleotide sequences for globin genes (alpha A, alpha D, and beta) of the
RT   Galapagos giant tortoise, Geochelone nigra.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAC81725.1}
RP   PROTEIN SEQUENCE OF 2-142.
RC   TISSUE=Erythrocyte {ECO:0000269|Ref.2};
RA   Shishikura F.;
RT   "A comparative study on hemoglobins from the two giant tortoises,
RT   Geochelone nigra and Geochelone gigantea.";
RL   Submitted (OCT-2001) to UniProtKB.
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues. {ECO:0000305}.
CC   -!- SUBUNIT: Heterotetramer of two alpha-A chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; AB116518; BAC81725.1; -; Genomic_DNA.
DR   AlphaFoldDB; P83135; -.
DR   SMR; P83135; -.
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   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..142
FT                   /note="Hemoglobin subunit alpha-A"
FT                   /id="PRO_0000052829"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   142 AA;  15752 MW;  0E4A283FEC528CB2 CRC64;
     MVLTAGDKAN VKTVWSKVGS HLEEYGSETL ERLFIVYPST KTYFPHFDLH HDSAQVRAHG
     RKVLSALGEA VNHIDDIPGA LSKLSDLHAQ TLRVDPVNFK LLNLCFVVVV GRHHPTILTP
     EVHVSLDKFL SAVATALTSK YR