HBA_FELCA
ID HBA_FELCA Reviewed; 141 AA.
AC P07405;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=4063071; DOI=10.1515/bchm3.1985.366.2.699;
RA Abbasi A., Braunitzer G.;
RT "The primary structure of hemoglobins from the domestic cat (Felis catus,
RT Felidae).";
RL Biol. Chem. Hoppe-Seyler 366:699-704(1985).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A25203; A25203.
DR PDB; 3D4X; X-ray; 2.20 A; A/C=1-141.
DR PDB; 3GQP; X-ray; 2.00 A; A/C=1-141.
DR PDB; 3GQR; X-ray; 2.40 A; A/C/E/G=1-141.
DR PDB; 3GYS; X-ray; 2.90 A; A/C/E/G=1-141.
DR PDBsum; 3D4X; -.
DR PDBsum; 3GQP; -.
DR PDBsum; 3GQR; -.
DR PDBsum; 3GYS; -.
DR AlphaFoldDB; P07405; -.
DR SMR; P07405; -.
DR STRING; 9685.ENSFCAP00000009652; -.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_10_2_1; -.
DR InParanoid; P07405; -.
DR OMA; FGKIGGQ; -.
DR TreeFam; TF332328; -.
DR EvolutionaryTrace; P07405; -.
DR Proteomes; UP000011712; 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_0000052635"
FT PEPTIDE 95..103
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455877"
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 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 HELIX 4..17
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 53..71
FT /evidence="ECO:0007829|PDB:3GQP"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:3GQP"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:3GQP"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:3D4X"
SQ SEQUENCE 141 AA; 15305 MW; 86A8047BEF8A2171 CRC64;
VLSAADKSNV KACWGKIGSH AGEYGAEALE RTFCSFPTTK TYFPHFDLSH GSAQVKAHGQ
KVADALTQAV AHMDDLPTAM SALSDLHAYK LRVDPVNFKF LSHCLLVTLA CHHPAEFTPA
VHASLDKFFS AVSTVLTSKY R
