HBA_PTEGI
ID HBA_PTEGI Reviewed; 141 AA.
AC D0VX09; P86191;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Hemoglobin subunit alpha {ECO:0000250|UniProtKB:P14389};
DE AltName: Full=Alpha-globin {ECO:0000250|UniProtKB:P14389};
DE AltName: Full=Hemoglobin alpha chain {ECO:0000250|UniProtKB:P14389, ECO:0000312|PDB:3FH9};
DE Contains:
DE RecName: Full=Hemopressin {ECO:0000250|UniProtKB:P01946};
GN Name=HBA {ECO:0000250|UniProtKB:P14389};
OS Pteropus giganteus (Indian flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=143291;
RN [1] {ECO:0000305, ECO:0000312|PDB:3FH9}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS).
RA Moorthy P.S., Neelagandan K., Balasubramanian M., Thenmozhi M.,
RA Ponnuswamy M.N.;
RT "Crystal structure determination of Indian flying fox (Pteropus giganteus)
RT at 1.62 A resolution.";
RL Submitted (DEC-2008) to the PDB data bank.
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. {ECO:0000305}.
CC -!- FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of
CC the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks
CC cannabinoid receptor CNR1 and subsequent signaling.
CC {ECO:0000250|UniProtKB:P01946}.
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 PDB; 3FH9; X-ray; 1.62 A; A=1-141.
DR PDBsum; 3FH9; -.
DR AlphaFoldDB; D0VX09; -.
DR SMR; D0VX09; -.
DR PRIDE; D0VX09; -.
DR EvolutionaryTrace; D0VX09; -.
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 3D-structure; Acetylation; Heme; Iron; Metal-binding; Oxygen transport;
KW Phosphoprotein; Transport.
FT CHAIN 1..141
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000398145"
FT PEPTIDE 95..103
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455935"
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:0000305"
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:0000305"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 7
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 11
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 16
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 16
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 53..71
FT /evidence="ECO:0007829|PDB:3FH9"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:3FH9"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:3FH9"
SQ SEQUENCE 141 AA; 15150 MW; 90BEF3B2FF9E78B9 CRC64;
VLSSTDKSNV KAAWDKVGGN VGEYGAEALE RMFLSFPTTK TYFPHFDLAH GSSQVKAHGK
KVGDALTNAV GHIDDLPGAL SALSDLHAYK LRVDPVNFKL LSHCLLVTLA SHLPSDFTPA
VHASLDKFLA SVSTVLTSKY R
