HBA1_ANAMI
ID HBA1_ANAMI Reviewed; 143 AA.
AC P83270;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Hemoglobin subunit alpha-1;
DE AltName: Full=Alpha-1-globin;
DE AltName: Full=Hemoglobin alpha-1 chain;
GN Name=hba1;
OS Anarhichas minor (Arctic spotted wolffish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Zoarcales; Anarhichadidae; Anarhichas.
OX NCBI_TaxID=65739;
RN [1]
RP PROTEIN SEQUENCE OF 2-143, FUNCTION, TISSUE SPECIFICITY, AND ACETYLATION AT
RP SER-2.
RX PubMed=12118003; DOI=10.1074/jbc.m202474200;
RA Verde C., Carratore V., Riccio A., Tamburrini M., Parisi E., Di Prisco G.;
RT "The functionally distinct hemoglobins of the Arctic spotted wolffish
RT Anarhichas minor.";
RL J. Biol. Chem. 277:36312-36320(2002).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000269|PubMed:12118003}.
CC -!- SUBUNIT: Hb1 is a heterotetramer of two alpha-1 chains and two beta-1
CC chains.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:12118003}.
CC -!- MISCELLANEOUS: Hb1 displays a low, effector-enhanced Bohr effect and no
CC Root effect.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR AlphaFoldDB; P83270; -.
DR SMR; P83270; -.
DR iPTMnet; P83270; -.
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 Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..143
FT /note="Hemoglobin subunit alpha-1"
FT /id="PRO_0000052544"
FT BINDING 60
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 89
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 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12118003"
SQ SEQUENCE 143 AA; 15763 MW; 0F92508DA7BCC3BF CRC64;
MSLTAKDKDT VRAFWAKASG KAAEIGSDAL SRMLVVYPQT KTYFSHWKDL SPGSEPVKKH
GKSVMGGVAD AVMKIEDLNA GLLNLSELHA FTLRVDPANF KILSHNILVV MAIMFPKDFT
PEVHVAMDKF LAALSRALAE KYR