HBA1_CAPHI
ID HBA1_CAPHI Reviewed; 142 AA.
AC P0CH25; P01970; P68238;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Hemoglobin subunit alpha-1;
DE AltName: Full=Alpha-1-globin;
DE AltName: Full=Hemoglobin alpha-1 chain;
DE Contains:
DE RecName: Full=Hemopressin {ECO:0000250|UniProtKB:P01946};
GN Name=HBA1;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-76.
RX PubMed=6282825; DOI=10.1016/s0021-9258(18)34504-6;
RA Schon E.A., Wernke S.M., Lingrel J.B.;
RT "Gene conversion of two functional goat alpha-globin genes preserves only
RT minimal flanking sequences.";
RL J. Biol. Chem. 257:6825-6835(1982).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, CLEAVAGE OF INITIATOR METHIONINE, AND VARIANT
RP TYR-76.
RX PubMed=5658544; DOI=10.1016/s0021-9258(19)34192-4;
RA Huisman T.H.J., Brandt G., Wilson J.B.;
RT "The structure of goat hemoglobins. II. Structural studies of the alpha
RT chains of the hemoglobins A and B.";
RL J. Biol. Chem. 243:3675-3686(1968).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 2-142.
RX PubMed=17909297; DOI=10.1107/s1744309107044296;
RA Neelagandan K., Moorthy P.S., Balasubramanian M., Ponnuswamy M.N.;
RT "Crystallization of sheep (Ovis aries) and goat (Capra hircus) haemoglobins
RT under unbuffered low-salt conditions.";
RL Acta Crystallogr. F 63:887-889(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-142.
RX PubMed=19356147; DOI=10.2174/092986609787847992;
RA Moorthy P.S., Neelagandan K., Balasubramanian M., Ponnuswamy M.N.;
RT "Purification, crystallization and preliminary X-ray diffraction studies on
RT goat (Capra hircus) hemoglobin - a low oxygen affinity species.";
RL Protein Pept. Lett. 16:454-456(2009).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. {ECO:0000250}.
CC -!- FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of
CC the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks
CC cannabinoid receptor CNR1 and subsequent signaling.
CC {ECO:0000250|UniProtKB:P01946}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Adult goat and other mammalian species produce unequal
CC amounts of alpha-globin from non-allelic loci.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; J00043; AAA30909.1; -; Genomic_DNA.
DR PIR; A92379; HAGT.
DR RefSeq; XP_017895579.1; XM_018040090.1.
DR PDB; 2RI4; X-ray; 2.70 A; A/C/I/K=2-142.
DR PDB; 3D1A; X-ray; 2.61 A; A/C=1-142.
DR PDB; 3EU1; X-ray; 3.00 A; A/C=2-142.
DR PDBsum; 2RI4; -.
DR PDBsum; 3D1A; -.
DR PDBsum; 3EU1; -.
DR AlphaFoldDB; P0CH25; -.
DR SMR; P0CH25; -.
DR STRING; 9925.ENSCHIP00000030098; -.
DR PRIDE; P0CH25; -.
DR Ensembl; ENSCHIT00000037968; ENSCHIP00000030098; ENSCHIG00000024771.
DR GeneID; 102168680; -.
DR KEGG; chx:102168680; -.
DR GeneTree; ENSGT00940000154590; -.
DR OMA; FGKIGGQ; -.
DR OrthoDB; 1398217at2759; -.
DR EvolutionaryTrace; P0CH25; -.
DR Proteomes; UP000291000; Chromosome 25.
DR Bgee; ENSCHIG00000024771; Expressed in ovary and 17 other tissues.
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; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5658544"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-1"
FT /id="PRO_0000052582"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455849"
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 VARIANT 76
FT /note="D -> Y (in alpha-1-B)"
FT /evidence="ECO:0000269|PubMed:5658544,
FT ECO:0000269|PubMed:6282825"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:3D1A"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3EU1"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:3D1A"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:3D1A"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2RI4"
FT HELIX 120..138
FT /evidence="ECO:0007829|PDB:3D1A"
SQ SEQUENCE 142 AA; 15164 MW; 1C3CF84DEB3C2176 CRC64;
MVLSAADKSN VKAAWGKVGG NAGAYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
EKVAAALTKA VGHLDDLPGT LSDLSDLHAH KLRVDPVNFK LLSHSLLVTL ACHLPNDFTP
AVHASLDKFL ANVSTVLTSK YR
