HBA_PANON
ID HBA_PANON Reviewed; 142 AA.
AC P63109; P04236;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 69.
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 Panthera onca (Jaguar) (Felis onca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC Panthera.
OX NCBI_TaxID=9690;
RN [1]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=3426807; DOI=10.1515/bchm3.1987.368.2.1385;
RA Ahmed A., Jahan M., Zaidi Z.H., Braunitzer G., Goeltenboth R.;
RT "The primary structure of the hemoglobins of the adult jaguar (Panthera
RT onco, Carnivora).";
RL Biol. Chem. Hoppe-Seyler 368:1385-1390(1987).
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}.
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DR PIR; S00521; HAJUA.
DR AlphaFoldDB; P63109; -.
DR SMR; P63109; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3426807"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052716"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455916"
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 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 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 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 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; 15558 MW; F9938B1FF8498254 CRC64;
MVLSSADKNN VKACWGKIGS HAGEYGAEAL ERTFCSFPTT KTYFPHFDLS HGSAQVQAHG
QKVADALTKA VAHINDLPNA LSDLSDLHAY KLRVDPVNFK FLSHCLLVTL ACHHPEEFTP
AVHASLDKFF SAVSTVLTSK YR
