ID   HBB1_ARCGL              Reviewed;         132 AA.
AC   Q1AGS3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Hemoglobin subunit beta-1;
DE   AltName: Full=Beta-1-globin;
DE   AltName: Full=Hemoglobin beta-1 chain;
DE   Flags: Fragment;
GN   Name=hbb1;
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:AAZ99828.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RC   TISSUE=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       Hb 2 is a heterotetramer of two alpha-2 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}.
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   EMBL; DQ125476; AAZ99828.1; -; mRNA.
DR   AlphaFoldDB; Q1AGS3; -.
DR   SMR; Q1AGS3; -.
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; cd08925; Hb-beta-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; IPR002337; Hemoglobin_b.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT   CHAIN           <1..132
FT                   /note="Hemoglobin subunit beta-1"
FT                   /id="PRO_0000247580"
FT   BINDING         49
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:P45720,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         78
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:P45720,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAZ99828.1"
SQ   SEQUENCE   132 AA;  14591 MW;  39581D97BEEC21F4 CRC64;
     WSKIDIDVCG PLALQRCLIV YPWTQRYFGS FGDLSTVAAI MGNPKVAQHG VVALTGLRTA
     LDHMDEIKST YAALSVLHSE KLHVDPDNFR LLCECLTIVI AGKMGKKLSP DMQAAWQKYL
     CAVVSALGRQ YH