HBA_PSIKR
ID HBA_PSIKR Reviewed; 141 AA.
AC P19831;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
GN Name=HBA;
OS Psittacula krameri (Rose-ringed parakeet).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Psittacula.
OX NCBI_TaxID=9228;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3255379; DOI=10.1007/bf01024874;
RA Islam A., Beg O.U., Persson B., Zaidi Z.H., Joernvall H.;
RT "Primary structure of the hemoglobin alpha-chain of rose-ringed parakeet
RT (Psittacula krameri).";
RL J. Protein Chem. 7:561-569(1988).
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 -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A30332; A30332.
DR PDB; 2ZFB; X-ray; 3.00 A; A=1-141.
DR PDBsum; 2ZFB; -.
DR AlphaFoldDB; P19831; -.
DR SMR; P19831; -.
DR EvolutionaryTrace; P19831; -.
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 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT CHAIN 1..141
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052742"
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 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 HELIX 4..16
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:2ZFB"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 53..71
FT /evidence="ECO:0007829|PDB:2ZFB"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:2ZFB"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:2ZFB"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2ZFB"
SQ SEQUENCE 141 AA; 15126 MW; FB0EC4BBF2F01AF4 CRC64;
VLSGTDKTNV KSIFSKIGGQ ADDYGAEALE RMFVTYPQTK TYFPHFDVSP GSAQVKAHGK
KVAGGLSEAA NHIDDIATSL SKLSDLHAQK LRVDPVNFKL LGQCFLVVVA IHNPSALTPE
AHASLDKFLC AVGLVLTAKY R