HBA1_ARCGL
ID HBA1_ARCGL Reviewed; 143 AA.
AC Q1AGS5; P84602;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Hemoglobin subunit alpha-1;
DE AltName: Full=Alpha-1-globin;
DE AltName: Full=Hemoglobin alpha-1 chain;
GN Name=hba1;
OS Arctogadus glacialis (Arctic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Arctogadus.
OX NCBI_TaxID=185735;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAZ99826.1}
RP PROTEIN SEQUENCE OF 2-143, NUCLEOTIDE SEQUENCE [MRNA] OF 12-143, FUNCTION,
RP SUBUNIT, AND ACETYLATION AT SER-2.
RC TISSUE=Blood {ECO:0000269|PubMed:16717098}, and
RC Spleen {ECO:0000269|PubMed:16717098};
RX PubMed=16717098; DOI=10.1074/jbc.m513080200;
RA Verde C., Balestrieri M., de Pascale D., Pagnozzi D., Lecointre G.,
RA di Prisco G.;
RT "The oxygen transport system in three species of the boreal fish family
RT Gadidae. Molecular phylogeny of hemoglobin.";
RL J. Biol. Chem. 281:22073-22084(2006).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000269|PubMed:16717098, ECO:0000305}.
CC -!- SUBUNIT: Hb 1 is a heterotetramer of two alpha-1 and two beta-1 chains.
CC {ECO:0000269|PubMed:16717098}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; DQ125474; AAZ99826.1; -; mRNA.
DR AlphaFoldDB; Q1AGS5; -.
DR SMR; Q1AGS5; -.
DR iPTMnet; Q1AGS5; -.
DR PRIDE; Q1AGS5; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16717098"
FT CHAIN 2..143
FT /note="Hemoglobin subunit alpha-1"
FT /id="PRO_0000247575"
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:16717098"
SQ SEQUENCE 143 AA; 15797 MW; C15E149AEC63C8AB CRC64;
MSLSSKDKAT VKEFFGKMST RSDDIGAEAL SRLVAVYPQT KSYFSHWKDA SPGSAPVRKH
GITIMGGVYD AVTKIDDLKG GLLSLSELHA FMLRVDPVNF KLLAHCMLVC MSMVFPEEFT
PQVHVAVDKF LAQLALALAE KYR
