HBA1_HYLLA
ID HBA1_HYLLA Reviewed; 142 AA.
AC Q9TS35;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 85.
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 Hylobates lar (Common gibbon) (White-handed gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hylobates.
OX NCBI_TaxID=9580;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=1526980; DOI=10.1016/s0021-9258(19)36976-5;
RA Bailey A.D., Stanhope M., Slightom J.L., Goodman M., Shen C.C.,
RA Shen C.-K.J.;
RT "Tandemly duplicated alpha globin genes of gibbon.";
RL J. Biol. Chem. 267:18398-18406(1992).
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; M94634; AAK13563.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9TS35; -.
DR SMR; Q9TS35; -.
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 2: Evidence at transcript level;
KW Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT CHAIN 1..142
FT /note="Hemoglobin subunit alpha-1"
FT /id="PRO_0000052654"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455883"
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; 15268 MW; 04E13666527BFF69 CRC64;
MVLSPADKTN VKAAWGKVGA HAGDYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHHPAEFTP
AVHASLDKFL ASVSTVLTSK YR