ID   HBA_CROSI               Reviewed;         141 AA.
AC   B0M2T2;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Hemoglobin subunit alpha {ECO:0000250|UniProtKB:P01966};
DE   AltName: Full=Alpha-globin {ECO:0000250|UniProtKB:P01966};
DE   AltName: Full=Hemoglobin alpha chain {ECO:0000303|PubMed:22648692};
GN   Name=HBA {ECO:0000250|UniProtKB:P01966};
OS   Crocodylus siamensis (Siamese crocodile).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Longirostres; Crocodylidae;
OC   Crocodylus.
OX   NCBI_TaxID=68455;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Erythrocyte {ECO:0000269|PubMed:22648692};
RX   PubMed=22648692; DOI=10.1007/s10930-012-9424-7;
RA   Srihongthong S., Pakdeesuwan A., Daduang S., Araki T., Dhiravisit A.,
RA   Thammasirirak S.;
RT   "Complete amino acid sequence of globin chains and biological activity of
RT   fragmented crocodile hemoglobin (Crocodylus siamensis).";
RL   Protein J. 31:466-476(2012).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues. Has antimicrobial activity against B.subtilis ATCC
CC       6633. Has antioxidant activity. {ECO:0000269|PubMed:22648692,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC       {ECO:0000305}.
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   AlphaFoldDB; B0M2T2; -.
DR   SMR; B0M2T2; -.
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   CHAIN           1..141
FT                   /note="Hemoglobin subunit alpha"
FT                   /id="PRO_0000421840"
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                   /evidence="ECO:0000250|UniProtKB:P01966,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000250|UniProtKB:P01966,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   141 AA;  15590 MW;  A97FD545985C191C CRC64;
     VLSSDDKCNV KAVWCKVAGH LEEYGAEALE RMFCAYPQTK IYFPHFDLSH GSAQIRAHGK
     KVFAALHEAV NHIDDLPGAL CRLSELHAHS LRVDPVNFKF LAQCVLVVVA IHHPGSLTPE
     VHASLDKFLC AVSSVLTSKY R