ID   HBB_NOTEU               Reviewed;         147 AA.
AC   Q6H1U7;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX   NCBI_TaxID=9315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=15461421; DOI=10.1007/s00239-004-2584-0;
RA   Wheeler D., Hope R.M., Cooper S.J.B., Gooley A.A., Holland R.A.B.;
RT   "Linkage of the beta-like omega-globin gene to alpha-like globin genes in
RT   an Australian marsupial supports the chromosome duplication model for
RT   separation of globin gene clusters.";
RL   J. Mol. Evol. 58:642-652(2004).
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   EMBL; AY450928; AAS15710.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6H1U7; -.
DR   SMR; Q6H1U7; -.
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   2: Evidence at transcript level;
KW   Acetylation; Heme; Iron; Metal-binding; Oxygen transport; Phosphoprotein;
KW   S-nitrosylation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02086"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052999"
FT   BINDING         64
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         93
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         2
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000250|UniProtKB:P02086"
FT   MOD_RES         13
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         83
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         94
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         145
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
SQ   SEQUENCE   147 AA;  16133 MW;  E26AA246BEF51DDC CRC64;
     MVHLTAEEKN AITSLWGKVA IEQTGGEALG RLLIVYPWTS RFFDHFGDLS NAKAVMSNPK
     VLAHGAKVLV AFGDAIKNLD NLKGTFAKLS ELHCDKLHVD PENFKLLGNI IVICLAEHFG
     KEFTIDAQVA WQKLVAGVAN ALAHKYH