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HBA_TAMHU
ID   HBA_TAMHU               Reviewed;         141 AA.
AC   B3EWD7;
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   Tamiasciurus hudsonicus (American red squirrel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Sciurinae; Tamiasciurini; Tamiasciurus.
OX   NCBI_TaxID=10009;
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; B3EWD7; -.
DR   SMR; B3EWD7; -.
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_0000415590"
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         8
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
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          34
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:22718635"
FT   UNSURE          48
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;  6429DDDC62767090 CRC64;
     VLSAADKTNV KSAWDKLGGH GAEYGAEALG RMFLSFPTTK TYPFHFDLSH GSAQPQGHGK
     KVAEALATAA GHLDDLPGAL SALSDLHAHK LRVDPVNFKL LSHCLLVTLA AHMPAEFTPA
     VHASLDKFLA SVSTVLTSKY R
 
 
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