HBA_PERCR
ID HBA_PERCR Reviewed; 141 AA.
AC B3EWD3;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Hemoglobin subunit alpha {ECO:0000303|PubMed:22718635};
OS Peromyscus crinitus (Canyon mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Peromyscus.
OX NCBI_TaxID=144753;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Erythrocyte {ECO:0000269|PubMed:22718635};
RX PubMed=22718635; DOI=10.1515/hsz-2011-0196;
RA Laskay U.A., Burg J., Kaleta E.J., Vilcins I.M., Telford Iii S.R.,
RA Barbour A.G., Wysocki V.H.;
RT "Development of a host blood meal database: de novo sequencing of
RT hemoglobin from nine small mammals using mass spectrometry.";
RL Biol. Chem. 393:195-201(2012).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. {ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR AlphaFoldDB; B3EWD3; -.
DR SMR; B3EWD3; -.
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_0000415587"
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 /evidence="ECO:0000250|UniProtKB:P01966,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
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 /evidence="ECO:0000250|UniProtKB:P01966,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
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 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
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"
FT UNSURE 2
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 17
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 29
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 66
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 73
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 76
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 80
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 83
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 86
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 91
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 100
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 101
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 105
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 106
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 109
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 125
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 129
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 136
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
SQ SEQUENCE 141 AA; 14986 MW; B82D55D33A873B6B CRC64;
VLSAEDKANV KAVWSKLGGH GAEYGAEALG RMFESHPTTK TYPFHFDVSH GSAQVKGHGK
KVADALATAA SHLDDLPGAL SALSDLHAHK LRVDPVNFKL LSHCLLVTLA AHHPAEFTPA
AHASLDKFLA SVSTVLTSKY R
