HBA_PSEUR
ID HBA_PSEUR Reviewed; 142 AA.
AC P83623;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
GN Name=hba;
OS Pseudaphritis urvillii (Congolli) (Freshwater flathead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Pseudaphritis.
OX NCBI_TaxID=56722;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBUNIT, AND ACETYLATION AT SER-1.
RC TISSUE=Erythrocyte {ECO:0000269|PubMed:15340169};
RX PubMed=15340169; DOI=10.1110/ps.04861504;
RA Verde C., Howes B.D., De Rosa M.C., Raiola L., Smulevich G., Williams R.,
RA Giardina B., Parisi E., Di Prisco G.;
RT "Structure and function of the Gondwanian hemoglobin of Pseudaphritis
RT urvillii, a primitive notothenioid fish of temperate latitudes.";
RL Protein Sci. 13:2766-2781(2004).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues.
CC -!- SUBUNIT: Hb1 is a heterotetramer of two alpha chains and two beta-1
CC chains. Hb2 is a heterotetramer of two alpha chains and two beta-2
CC chains. {ECO:0000269|PubMed:15340169}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
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 AlphaFoldDB; P83623; -.
DR SMR; P83623; -.
DR iPTMnet; P83623; -.
DR GO; GO:0005833; C:hemoglobin complex; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0015671; P:oxygen transport; IDA:UniProtKB.
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 Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT CHAIN 1..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052741"
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 /evidence="ECO:0000250|UniProtKB:P80043,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
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 /evidence="ECO:0000250|UniProtKB:P80043,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:15340169"
SQ SEQUENCE 142 AA; 15661 MW; D14603197B57EBC4 CRC64;
SLTDKDKATV KALWGKISKS ADAVGADAVG RMIVVYPQTK TYFSHWPDLA PNSPHVKTHG
KTVMTGIALA VSKIDDLTNG LLELSEEHAY KMRVDPANFK ILSHCMLVVI ATMFPKEFTP
EAHVCLDKFL CAVSLALSER YR
