HBA_CANLF
ID HBA_CANLF Reviewed; 141 AA.
AC P60529; P01952;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
DE Contains:
DE RecName: Full=Hemopressin {ECO:0000250|UniProtKB:P01946};
GN Name=HBA;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=864726; DOI=10.1007/bf01796112;
RA Brimhall B., Duerst M., Jones R.T.;
RT "The amino acid sequence of dog (Canis familiaris) hemoglobin.";
RL J. Mol. Evol. 9:231-235(1977).
RN [2]
RP GENE FAMILY ORGANIZATION.
RX PubMed=1016221; DOI=10.1007/bf00485137;
RA Dresler S.L., Brimhall B., Jones R.T.;
RT "Multiple structural genes for the alpha chain of canine (Canis familiaris)
RT hemoglobin.";
RL Biochem. Genet. 14:1065-1070(1976).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=21543841; DOI=10.1107/s0907444911006044;
RA Bhatt V.S., Zaldivar-Lopez S., Harris D.R., Couto C.G., Wang P.G.,
RA Palmer A.F.;
RT "Structure of Greyhound hemoglobin: origin of high oxygen affinity.";
RL Acta Crystallogr. D 67:395-402(2011).
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 {ECO:0000269|PubMed:21543841}.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- MISCELLANEOUS: The sequence shown is one of two non-allelic alpha
CC chains from dog.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A02274; HADG.
DR PIR; B92970; HADG2.
DR PDB; 2QLS; X-ray; 3.50 A; A/C=1-141.
DR PDB; 3GOU; X-ray; 3.00 A; A/C=1-141.
DR PDB; 3PEL; X-ray; 1.90 A; A=1-141.
DR PDBsum; 2QLS; -.
DR PDBsum; 3GOU; -.
DR PDBsum; 3PEL; -.
DR AlphaFoldDB; P60529; -.
DR SMR; P60529; -.
DR STRING; 9612.ENSCAFP00000038026; -.
DR PaxDb; P60529; -.
DR PRIDE; P60529; -.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P60529; -.
DR OMA; FGKIGGQ; -.
DR EvolutionaryTrace; P60529; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Oxygen transport; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..141
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052580"
FT PEPTIDE 95..103
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455847"
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 MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 7
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 11
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 16
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 16
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT VARIANT 130
FT /note="A -> T (in second chain)"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:3PEL"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3GOU"
FT HELIX 53..70
FT /evidence="ECO:0007829|PDB:3PEL"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:3PEL"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3GOU"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:3PEL"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:3PEL"
SQ SEQUENCE 141 AA; 15217 MW; 548EB12A1BEBA3E4 CRC64;
VLSPADKTNI KSTWDKIGGH AGDYGGEALD RTFQSFPTTK TYFPHFDLSP GSAQVKAHGK
KVADALTTAV AHLDDLPGAL SALSDLHAYK LRVDPVNFKL LSHCLLVTLA CHHPTEFTPA
VHASLDKFFA AVSTVLTSKY R
