ID   HBB1_ONCMY              Reviewed;         146 AA.
AC   P02142;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Hemoglobin subunit beta-1;
DE   AltName: Full=Beta-1-globin;
DE   AltName: Full=Hemoglobin beta-1 chain;
DE   AltName: Full=Hemoglobin beta-I chain;
GN   Name=hbb1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6824687; DOI=10.1016/0167-4838(83)90360-6;
RA   Barra D., Petruzzelli R., Bossa F., Brunori M.;
RT   "Primary structure of hemoglobin from trout (Salmo irideus) amino acid
RT   sequence of the beta chain of trout Hb I.";
RL   Biochim. Biophys. Acta 742:72-77(1983).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=8683580; DOI=10.1006/jmbi.1996.0355;
RA   Tame J.R.H., Wilson J.C., Weber R.E.;
RT   "The crystal structures of trout Hb I in the deoxy and carbonmonoxy
RT   forms.";
RL   J. Mol. Biol. 259:749-760(1996).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: This hemoglobin differs from other fish hemoglobins in
CC       lacking a residue between 121 and 122.
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   PIR; A02462; HBTR1.
DR   PDB; 1OUT; X-ray; 2.30 A; B=1-146.
DR   PDB; 1OUU; X-ray; 2.50 A; B/D=1-146.
DR   PDBsum; 1OUT; -.
DR   PDBsum; 1OUU; -.
DR   AlphaFoldDB; P02142; -.
DR   SMR; P02142; -.
DR   MINT; P02142; -.
DR   EvolutionaryTrace; P02142; -.
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   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta-1"
FT                   /id="PRO_0000053100"
FT   BINDING         63
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:P80044"
FT   BINDING         92
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:0000269|PubMed:8683580,
FT                   ECO:0007744|PDB:1OUT, ECO:0007744|PDB:1OUU"
FT   HELIX           5..16
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           20..34
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           36..41
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           51..56
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           58..69
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           71..76
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           101..118
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           124..141
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:1OUT"
SQ   SEQUENCE   146 AA;  15881 MW;  2065A57D9D1D6071 CRC64;
     VEWTDAEKST ISAVWGKVNI DEIGPLALAR VLIVYPWTQR YFGSFGNVST PAAIMGNPKV
     AAHGKVVCGA LDKAVKNMGN ILATYKSLSE THANKLFVDP DNFRVLADVL TIVIAAKFGA
     SFTPEIQATW QKFMKVVVAA MGSRYF