HBA1_GOBGI
ID HBA1_GOBGI Reviewed; 142 AA.
AC P83611;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Hemoglobin subunit alpha-1;
DE AltName: Full=Alpha-1-globin;
DE AltName: Full=Hemoglobin alpha-1 chain;
GN Name=hba1;
OS Gobionotothen gibberifrons (Humped rockcod) (Notothenia gibberifrons).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Gobionotothen.
OX NCBI_TaxID=36202 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBUNIT, MASS SPECTROMETRY, AND ACETYLATION AT SER-1.
RC TISSUE=Blood {ECO:0000269|PubMed:14511380};
RX PubMed=14511380; DOI=10.1046/j.1432-1033.2003.03786.x;
RA Marinakis P., Tamburrini M., Carratore V., di Prisco G.;
RT "Unique features of the hemoglobin system of the Antarctic fish
RT Gobionotothen gibberifrons.";
RL Eur. J. Biochem. 270:3981-3987(2003).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues.
CC -!- SUBUNIT: Hb 1 is a heterotetramer of two alpha-1 and two beta-1 chains.
CC {ECO:0000269|PubMed:14511380}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=15597; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:14511380};
CC -!- MISCELLANEOUS: This fish has two hemoglobins: Hb1 (major) and Hb2
CC (about 15-20% of the total). They display the Root effect and the
CC alkaline Bohr effect, which is enhanced by organophosphate and to a
CC lesser extent by chloride.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238, ECO:0000305}.
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DR AlphaFoldDB; P83611; -.
DR SMR; P83611; -.
DR iPTMnet; P83611; -.
DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
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; 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 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-1"
FT /id="PRO_0000052640"
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: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:0000255|PROSITE-ProRule:PRU00238"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:14511380"
SQ SEQUENCE 142 AA; 15560 MW; 30748CFEAE2917A2 CRC64;
SLSVKDKAAV RALWSKISKS SDAIGNDALS RMIVVYPQTK TYFSHWPDVT PGSAHIKAHG
KKVMGGIALA VSKIDDLNAG LLELSEQHAY KLRVDPANFK ILNHCILVVI STMFPKDFTP
EAHVSLDKFL SGVALALAER YR
