HBA1_EQUQB
ID HBA1_EQUQB Reviewed; 142 AA.
AC Q9XSN3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 88.
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 Equus quagga burchellii (Plains zebra) (Equus burchelli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus; Equus quagga.
OX NCBI_TaxID=89252;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9847419; DOI=10.1007/pl00006436;
RA Oakenfull E.A., Clegg J.B.;
RT "Phylogenetic relationships within the genus Equus and the evolution of
RT alpha and theta globin genes.";
RL J. Mol. Evol. 47:772-783(1998).
RN [2]
RP AMINO-ACID COMPOSITION, AND MAPPING OF PEPTIDES.
RX PubMed=5354968; DOI=10.1016/s0021-9258(18)63495-7;
RA Kitchen H., Easley C.W.;
RT "Structural comparison of the hemoglobins of the genus Equus with those of
RT ruminants.";
RL J. Biol. Chem. 244:6533-6542(1969).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
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 -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; U70200; AAB93461.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XSN3; -.
DR SMR; Q9XSN3; -.
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 Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT CHAIN 1..142
FT /note="Hemoglobin subunit alpha-1"
FT /id="PRO_0000052625"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455870"
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"
SQ SEQUENCE 142 AA; 15220 MW; 979F83EBD30317E0 CRC64;
MVLSADDKSN VKAAWGKVGG NAGEFGAEAL ERMFLGFPTT KTYFPHFDLS HGSAQVKAHG
KKVGDALTLA VGHLDDLPGA LSNLSDLHAH KLRVDPVNFK LLSHCLLSTL AVHLPNDFTP
AVHASLDKFL STVSTVLTSK YR
