HBA_PIG
ID HBA_PIG Reviewed; 141 AA.
AC P01965;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=565742;
RA Braunitzer G., Schrank B., Stangl A., Scheithauer U.;
RT "Hemoglobins, XXI. Sequence analysis of porcine hemoglobin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 359:137-146(1978).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=7990139; DOI=10.1006/jmbi.1994.1751;
RA Katz D.S., White S.P., Huang W., Kumar R., Christianson D.W.;
RT "Structure determination of aquomet porcine hemoglobin at 2.8-A
RT resolution.";
RL J. Mol. Biol. 244:541-553(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10713517; DOI=10.1107/s0907444900000093;
RA Lu T.-H., Panneerselvam K., Liaw Y.-C., Kan P., Lee C.-J.;
RT "Structure determination of porcine haemoglobin.";
RL Acta Crystallogr. D 56:304-312(2000).
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 PIR; A02288; HAPG.
DR PDB; 1QPW; X-ray; 1.80 A; A/C=1-141.
DR PDB; 2PGH; X-ray; 2.80 A; A/C=1-141.
DR PDB; 4F4O; X-ray; 2.90 A; A/D/G/J=1-141.
DR PDBsum; 1QPW; -.
DR PDBsum; 2PGH; -.
DR PDBsum; 4F4O; -.
DR AlphaFoldDB; P01965; -.
DR SMR; P01965; -.
DR DIP; DIP-38534N; -.
DR IntAct; P01965; 2.
DR STRING; 9823.ENSSSCP00000008517; -.
DR PaxDb; P01965; -.
DR PeptideAtlas; P01965; -.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P01965; -.
DR OMA; SNEDKAC; -.
DR EvolutionaryTrace; P01965; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P01965; SS.
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_0000052731"
FT PEPTIDE 95..103
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455926"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238,
FT ECO:0000269|PubMed:7990139"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238,
FT ECO:0000269|PubMed:7990139"
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 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 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 HELIX 4..15
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1QPW"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2PGH"
FT HELIX 53..70
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:1QPW"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:1QPW"
SQ SEQUENCE 141 AA; 15039 MW; 95869BABB4C4EDB8 CRC64;
VLSAADKANV KAAWGKVGGQ AGAHGAEALE RMFLGFPTTK TYFPHFNLSH GSDQVKAHGQ
KVADALTKAV GHLDDLPGAL SALSDLHAHK LRVDPVNFKL LSHCLLVTLA AHHPDDFNPS
VHASLDKFLA NVSTVLTSKY R
