HBA_CAVPO
ID HBA_CAVPO Reviewed; 142 AA.
AC P01947;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=527943;
RA Braunitzer G., Schrank B., Stangl A., Wiesner H.;
RT "Respiration at high altitudes, phosphate-protein interaction: the sequence
RT of hemoglobins from guinea pig and dromedary.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:1941-1946(1979).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 2-142, AND SUBUNIT.
RX PubMed=20811494; DOI=10.1371/journal.pone.0012389;
RA Pairet B., Jaenicke E.;
RT "Structure of the altitude adapted hemoglobin of guinea pig in the R2-
RT state.";
RL PLoS ONE 5:E12389-E12389(2010).
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:20811494}.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A02269; HAGP.
DR RefSeq; XP_003478455.1; XM_003478407.3.
DR PDB; 3A0G; X-ray; 2.50 A; A=2-142.
DR PDB; 3HYU; X-ray; 1.67 A; A=2-142.
DR PDBsum; 3A0G; -.
DR PDBsum; 3HYU; -.
DR AlphaFoldDB; P01947; -.
DR SMR; P01947; -.
DR STRING; 10141.ENSCPOP00000000235; -.
DR Ensembl; ENSCPOT00000000270; ENSCPOP00000000235; ENSCPOG00000000267.
DR GeneID; 100712878; -.
DR KEGG; cpoc:100712878; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000154590; -.
DR HOGENOM; CLU_003827_10_2_1; -.
DR InParanoid; P01947; -.
DR OMA; FGKIGGQ; -.
DR OrthoDB; 1398217at2759; -.
DR TreeFam; TF332328; -.
DR EvolutionaryTrace; P01947; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000000267; Expressed in adult mammalian kidney and 13 other tissues.
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; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Oxygen transport; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P18969"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052591"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455851"
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 MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 8
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 12
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 17
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 41
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:3HYU"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:3HYU"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 96..114
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:3HYU"
SQ SEQUENCE 142 AA; 15361 MW; 7F095AF1C5C5910D CRC64;
MVLSAADKNN VKTTWDKIGG HAAEYVAEGL TRMFTSFPTT KTYFHHIDVS PGSGDIKAHG
KKVADALTTA VGHLDDLPTA LSTLSDVHAH KLRVDPVNFK FLNHCLLVTL AAHLGADFTP
SIHASLDKFF ASVSTVLTSK YR
