ID HBA_SAPAP Reviewed; 142 AA. AC P01928; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-NOV-2024, entry version 102. 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 Sapajus apella (Brown-capped capuchin) (Cebus apella). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae; OC Cebinae; Sapajus. OX NCBI_TaxID=9515; RN [1] RP PROTEIN SEQUENCE OF 2-142. RX PubMed=4215719; RA Matsuda G., Maita T., Watanabe B., Araya A., Morokuma K., Ota Y., RA Goodman M., Barnabas J., Prychodko W.; RT "The amino acid sequences of the alpha and beta polypeptide chains of adult RT hemoglobin of the capuchin monkey (Cebus apella)."; RL Hoppe-Seyler's Z. Physiol. Chem. 354:1513-1516(1973). 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; A02254; HAMQA. DR AlphaFoldDB; P01928; -. DR BMRB; P01928; -. DR SMR; P01928; -. DR OrthoDB; 2939502at2759; -. DR Proteomes; UP000504640; Unplaced. DR GO; GO:0072562; C:blood microparticle; IEA:TreeGrafter. DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IEA:TreeGrafter. DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro. DR GO; GO:0031720; F:haptoglobin binding; IEA:TreeGrafter. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0043177; F:organic acid binding; IEA:TreeGrafter. DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IEA:TreeGrafter. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter. DR CDD; cd08927; Hb-alpha-like; 1. DR FunFam; 1.10.490.10:FF:000002; Hemoglobin subunit alpha; 1. DR Gene3D; 1.10.490.10; Globins; 1. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin-like_sf. DR InterPro; IPR012292; Globin/Proto. DR InterPro; IPR002338; Hemoglobin_a-typ. DR InterPro; IPR050056; Hemoglobin_oxygen_transport. DR InterPro; IPR002339; Hemoglobin_pi. DR PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1. DR PANTHER; PTHR11442:SF48; HEMOGLOBIN SUBUNIT ALPHA; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00612; ALPHAHAEM. DR PRINTS; PR00815; PIHAEM. DR SUPFAM; SSF46458; Globin-like; 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; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P18969" FT CHAIN 2..142 FT /note="Hemoglobin subunit alpha" FT /id="PRO_0000052592" FT PEPTIDE 96..104 FT /note="Hemopressin" FT /evidence="ECO:0000250|UniProtKB:P01946" FT /id="PRO_0000455852" FT DOMAIN 2..142 FT /note="Globin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238" FT BINDING 59 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" 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" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P69905" FT MOD_RES 8 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 9 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P69905" FT MOD_RES 12 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 17 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P69905" FT MOD_RES 17 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 25 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P69905" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P69905" FT MOD_RES 41 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P69905" FT MOD_RES 103 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 109 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 125 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 135 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 138 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P01942" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01942" SQ SEQUENCE 142 AA; 15255 MW; 404C5216FF7D22AE CRC64; MVLSPADKTN VKTAWGKVGG HAGDYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG KKVADALSNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHHPADFTP AVHASLDKFL ASVSTVLTSK YR //