ID HBA_PTEPO Reviewed; 141 AA. AC P14390; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 03-AUG-2022, entry version 90. DE RecName: Full=Hemoglobin subunit alpha; DE AltName: Full=Alpha-globin; DE AltName: Full=Hemoglobin alpha chain; DE Contains: DE RecName: Full=Hemopressin {ECO:0000250|UniProtKB:P01946}; GN Name=HBA; OS Pteropus poliocephalus (Grey-headed flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae; OC Pteropodinae; Pteropus. OX NCBI_TaxID=9403; RN [1] RP PROTEIN SEQUENCE. RX PubMed=3228493; DOI=10.1515/bchm3.1988.369.2.975; RA Kleinschmidt T., Sgouros J.G., Pettigrew J.D., Braunitzer G.; RT "The primary structure of the hemoglobin from the grey-headed flying fox RT (Pteropus poliocephalus) and the black flying fox (P. alecto, RT Megachiroptera)."; RL Biol. Chem. Hoppe-Seyler 369:975-984(1988). CC -!- FUNCTION: Involved in oxygen transport from the lung to the various CC peripheral tissues. 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 -!- TISSUE SPECIFICITY: Red blood cells. CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE- CC ProRule:PRU00238}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; S01310; HAFXG. DR AlphaFoldDB; P14390; -. DR SMR; P14390; -. 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; Phosphoprotein; Transport. FT CHAIN 1..141 FT /note="Hemoglobin subunit alpha" FT /id="PRO_0000052745" FT PEPTIDE 95..103 FT /note="Hemopressin" FT /evidence="ECO:0000250|UniProtKB:P01946" FT /id="PRO_0000455936" 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 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" SQ SEQUENCE 141 AA; 15222 MW; 9F5AEF633458A46E CRC64; VLSSTDKSNV KAAWDKVGGN VGEYGAEALE RMFLSFPTTK TYFPHFDLAH GSSQVKAHGK KVGDALTNAV GHMDDLPGAL SALSDLHAYK LRVDPVNFKL LSHCLLVTLA NHLPNDFTPA VHASLDKFLA SVSTVLTSKY R //