HBA_PONPY
ID HBA_PONPY Reviewed; 142 AA.
AC P06635;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=HBA1;
GN and
GN Name=HBA2;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1 AND HBA2).
RX PubMed=3456594; DOI=10.1073/pnas.83.5.1413;
RA Marks J., Shaw J.-P., Shen C.-K.J.;
RT "The orangutan adult alpha-globin gene locus: duplicated functional genes
RT and a newly detected member of the primate alpha-globin gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1413-1417(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3561513; DOI=10.1038/326717a0;
RA Shaw J.-P., Marks J., Shen C.-K.J.;
RT "Evidence that the recently discovered theta 1-globin gene is functional in
RT higher primates.";
RL Nature 326:717-720(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT GLY-58.
RX PubMed=15871050; DOI=10.1007/s00239-004-0201-x;
RA Steiper M.E., Wolfe N.D., Karesh W.B., Kilbourn A.M., Bosi E.J., Ruvolo M.;
RT "The population genetics of the alpha-2 globin locus of orangutans (Pongo
RT pygmaeus).";
RL J. Mol. Evol. 60:400-408(2005).
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 EMBL; M12158; AAA66030.1; -; Genomic_DNA.
DR EMBL; M12157; AAA66031.1; -; Genomic_DNA.
DR EMBL; AY372078; AAR29172.1; -; Genomic_DNA.
DR EMBL; AY372079; AAR29173.1; -; Genomic_DNA.
DR EMBL; AY372080; AAR29174.1; -; Genomic_DNA.
DR EMBL; AY372081; AAR29175.1; -; Genomic_DNA.
DR EMBL; AY372082; AAR29176.1; -; Genomic_DNA.
DR EMBL; AY372083; AAR29177.1; -; Genomic_DNA.
DR EMBL; AY372084; AAR29178.1; -; Genomic_DNA.
DR EMBL; AY372085; AAR29179.1; -; Genomic_DNA.
DR EMBL; AY372086; AAR29180.1; -; Genomic_DNA.
DR EMBL; AY372087; AAR29181.1; -; Genomic_DNA.
DR EMBL; AY372088; AAR29182.1; -; Genomic_DNA.
DR EMBL; AY372089; AAR29183.1; -; Genomic_DNA.
DR EMBL; AY372090; AAR29184.1; -; Genomic_DNA.
DR EMBL; AY372091; AAR29185.1; -; Genomic_DNA.
DR EMBL; AY372092; AAR29186.1; -; Genomic_DNA.
DR EMBL; AY372093; AAR29187.1; -; Genomic_DNA.
DR EMBL; AY372094; AAR29188.1; -; Genomic_DNA.
DR EMBL; AY372095; AAR29189.1; -; Genomic_DNA.
DR EMBL; AY372096; AAR29190.1; -; Genomic_DNA.
DR EMBL; AY372097; AAR29191.1; -; Genomic_DNA.
DR EMBL; AY372098; AAR29192.1; -; Genomic_DNA.
DR EMBL; AY372099; AAR29193.1; -; Genomic_DNA.
DR EMBL; AY372100; AAR29194.1; -; Genomic_DNA.
DR EMBL; AY372101; AAR29195.1; -; Genomic_DNA.
DR EMBL; AY372102; AAR29196.1; -; Genomic_DNA.
DR EMBL; AY372103; AAR29197.1; -; Genomic_DNA.
DR EMBL; AY372104; AAR29198.1; -; Genomic_DNA.
DR EMBL; AY372105; AAR29199.1; -; Genomic_DNA.
DR EMBL; AY372106; AAR29200.1; -; Genomic_DNA.
DR EMBL; AY372107; AAR29201.1; -; Genomic_DNA.
DR EMBL; AY372108; AAR29202.1; -; Genomic_DNA.
DR EMBL; AY372109; AAR29203.1; -; Genomic_DNA.
DR EMBL; AY372110; AAR29204.1; -; Genomic_DNA.
DR PIR; B25126; B25126.
DR PIR; B27792; B27792.
DR AlphaFoldDB; P06635; -.
DR BMRB; P06635; -.
DR SMR; P06635; -.
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 2: Evidence at transcript level;
KW Acetylation; Heme; Iron; Metal-binding; Oxygen transport; Phosphoprotein;
KW Transport.
FT CHAIN 1..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052736"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455928"
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 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"
FT VARIANT 58
FT /note="D -> G"
FT /evidence="ECO:0000269|PubMed:15871050"
FT /id="VAR_019063"
SQ SEQUENCE 142 AA; 15332 MW; 16EE747A245446E7 CRC64;
MVLSPADKTN VKTAWGKVGA HAGDYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKDHG
KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
AVHASLDKFL ASVSTVLTSK YR
