HBA_EQUHE
ID HBA_EQUHE Reviewed; 142 AA.
AC P01961; Q9TVA4; Q9XSE8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Hemoglobin subunit alpha-1/2;
DE AltName: Full=Alpha-1/2-globin;
DE AltName: Full=Hemoglobin alpha-1/2 chain;
OS Equus hemionus kulan (Turkmenian kulan) (Equus onager kulan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=73334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9847419; DOI=10.1007/pl00006436;
RA Oakenfull E.A., Clegg J.B.;
RT "Phylogenetic relationships within the genus Equus and the evolution of
RT alpha and theta globin genes.";
RL J. Mol. Evol. 47:772-783(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=7061044; DOI=10.1515/bchm2.1982.363.1.59;
RA Mazur G., Braunitzer G.;
RT "The sequence of hemoglobins from an asiatic wild ass and a mountain
RT zebra.";
RL Hoppe-Seyler's Z. Physiol. Chem. 363:59-71(1982).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- POLYMORPHISM: There are two alleles. The sequence shown is that of
CC alpha-1. {ECO:0000269|PubMed:9847419}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; AF129137; AAB93465.1; -; Genomic_DNA.
DR EMBL; AF129136; AAB93465.1; JOINED; Genomic_DNA.
DR EMBL; AF129139; AAB93466.1; -; Genomic_DNA.
DR EMBL; AF129138; AAB93466.1; JOINED; Genomic_DNA.
DR PIR; A02283; HAHOK.
DR AlphaFoldDB; P01961; -.
DR SMR; P01961; -.
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:7061044"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-1/2"
FT /id="PRO_0000052629"
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 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"
FT VARIANT 21
FT /note="N -> H (in alpha-2)"
FT CONFLICT 141
FT /note="Y -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 15206 MW; 82B837BC14C1D1B2 CRC64;
MVLSAADKTN VKAAWSKVGG NAGDFGAEAL ERMFLGFPTT KTYFPHFDLS HGSAQVKAHG
KKVGDALTLA VGHLDDLPGA LSNLSDLHAH KLRVDPVNFK LLSHCLLSTL AVHLPNDFTP
AVHASLDKFL STVSTVLTSK YR
