HBA_MUSGR
ID HBA_MUSGR Reviewed; 141 AA.
AC Q9YGW2;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
GN Name=HBA;
OS Mustelus griseus (Spotless smooth hound).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Triakidae;
OC Mustelus.
OX NCBI_TaxID=89020;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miyazaki G., Yoshimatu K., Kawasaki Y., Suzuki T.;
RT "Hemoglobin alpha chain of spotless smooth hound (Mustelus griseus).";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-141.
RX PubMed=11243818; DOI=10.1006/jmbi.2000.4446;
RA Naoi Y., Chong K.T., Yoshimatsu K., Miyazaki G., Tame J.R., Park S.Y.,
RA Adachi S., Morimoto H.;
RT "The functional similarity and structural diversity of human and
RT cartilaginous fish hemoglobins.";
RL J. Mol. Biol. 307:259-270(2001).
CC -!- FUNCTION: Involved in oxygen transport from gills 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 EMBL; AB023800; BAA75399.1; -; mRNA.
DR PDB; 1GCV; X-ray; 2.00 A; A/C=2-141.
DR PDB; 1GCW; X-ray; 2.00 A; A/C=2-141.
DR PDBsum; 1GCV; -.
DR PDBsum; 1GCW; -.
DR AlphaFoldDB; Q9YGW2; -.
DR SMR; Q9YGW2; -.
DR EvolutionaryTrace; Q9YGW2; -.
DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT CHAIN 1..141
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052695"
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 HELIX 5..20
FT /evidence="ECO:0007829|PDB:1GCV"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:1GCV"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1GCV"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:1GCV"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1GCV"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1GCV"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:1GCV"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1GCV"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:1GCV"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:1GCV"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1GCV"
SQ SEQUENCE 141 AA; 15428 MW; 8CE99D085937AC7B CRC64;
MAFTACEKQT IGKIAQVLAK SPEAYGAECL ARLFVTHPGS KSYFEYKDYS AAGAKVQVHG
GKVIRAVVKA AEHVDDLHSH LETLALTHGK KLLVDPQNFP MLSECIIVTL ATHLTEFSPD
THCAVDKLLS AICQELSSRY R
