ID   HBB_CHRBR               Reviewed;         146 AA.
AC   P60526;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Chrysocyon brachyurus (Maned wolf).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Chrysocyon.
OX   NCBI_TaxID=68728;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=14683506; DOI=10.2174/0929866033478564;
RA   Fadel V., Canduri F., Olivieri J.R., Smarra A.L., Colombo M.F.,
RA   Bonilla-Rodriguez G.O., de Azevedo W.F. Jr.;
RT   "Crystal structure of hemoglobin from the maned wolf (Chrysocyon
RT   brachyurus) using synchrotron radiation.";
RL   Protein Pept. Lett. 10:551-559(2003).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PDB; 1FHJ; X-ray; 1.80 A; B/D=1-146.
DR   PDB; 2B7H; X-ray; 2.20 A; B/D=1-146.
DR   PDBsum; 1FHJ; -.
DR   PDBsum; 2B7H; -.
DR   AlphaFoldDB; P60526; -.
DR   SMR; P60526; -.
DR   EvolutionaryTrace; P60526; -.
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; Acetylation; Heme; Iron; Metal-binding; Oxygen transport;
KW   Phosphoprotein; S-nitrosylation; Transport.
FT   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052927"
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   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   MOD_RES         1
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000250|UniProtKB:P02086"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         59
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         82
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         93
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         144
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   HELIX           5..15
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           20..34
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           36..45
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           51..56
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           58..76
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           101..118
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           124..141
FT                   /evidence="ECO:0007829|PDB:1FHJ"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:1FHJ"
SQ   SEQUENCE   146 AA;  15996 MW;  ECD68B81D53608F1 CRC64;
     VHLTAEEKSL VSGLWGKVNV DEVGGEALGR LLIVYPWTQR FFDSFGDLST PDAVMSNAKV
     KAHGKKVLNS FSDGLKNLDN LKGTFAKLSE LHCDKLHVDP ENFKLLGNVL VCVLAHHFGK
     EFTPQVQAAY QKVVAGVANA LAHKYH