HBB0_MOUSE
ID HBB0_MOUSE Reviewed; 147 AA.
AC P04443; Q61346;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Hemoglobin subunit beta-H0;
DE AltName: Full=Beta-H0-globin;
DE AltName: Full=Hemoglobin beta-H0 chain;
GN Name=Hbb-bh0;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2926808; DOI=10.1016/0022-2836(89)90363-x;
RA Shehee W.R., Loeb D.D., Adey N.B., Burton F.H., Casavant N.C., Cole P.,
RA Davies C.J., McGraw R.A., Schichman S.A., Severynse D.M., Voliva C.F.,
RA Weyter F.W., Wisely G.B., Edgell M.H., Hutchison C.A. III;
RT "Nucleotide sequence of the BALB/c mouse beta-globin complex.";
RL J. Mol. Biol. 205:41-62(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6323438; DOI=10.1016/s0021-9258(17)43157-7;
RA Hill A., Hardies S.C., Phillips S.J., Davis M.G., Hutchison C.A. III,
RA Edgell M.H.;
RT "Two mouse early embryonic beta-globin gene sequences. Evolution of the
RT nonadult beta-globins.";
RL J. Biol. Chem. 259:3739-3747(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-105.
RX PubMed=6250710; DOI=10.1016/0092-8674(80)90123-3;
RA Jahn C.L., Hutchison C.A. III, Phillips S.J., Weaver S., Haigwood N.L.,
RA Voliva C.F., Edgell M.H.;
RT "DNA sequence organization of the beta-globin complex in the BALB/c
RT mouse.";
RL Cell 21:159-168(1980).
CC -!- FUNCTION: This is a minor early embryonic beta chain.
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; X14061; CAA32220.1; -; Genomic_DNA.
DR EMBL; J00416; AAB59637.1; -; Genomic_DNA.
DR EMBL; V00723; CAA24102.1; -; Genomic_DNA.
DR PIR; A02418; HBMSH0.
DR AlphaFoldDB; P04443; -.
DR SMR; P04443; -.
DR iPTMnet; P04443; -.
DR PhosphoSitePlus; P04443; -.
DR MaxQB; P04443; -.
DR PeptideAtlas; P04443; -.
DR PRIDE; P04443; -.
DR MGI; MGI:96023; Hbb-bh0.
DR InParanoid; P04443; -.
DR PhylomeDB; P04443; -.
DR PRO; PR:P04443; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P04443; protein.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IDA:MGI.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0031721; F:hemoglobin alpha binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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 Heme; Iron; Metal-binding; Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..147
FT /note="Hemoglobin subunit beta-H0"
FT /id="PRO_0000053022"
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 CONFLICT 61..63
FT /note="IKA -> NKT (in Ref. 3; CAA24102)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="D -> H (in Ref. 2; AAB59637)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="D -> N (in Ref. 3; CAA24102)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> V (in Ref. 1; CAA32220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16384 MW; 1C5E6911D3BDCE28 CRC64;
MVHFTAEEKA AITSIWDKVD LEKVGGETLG RLLIVYPWTQ RFFDKFGNLS SAQAIMGNPR
IKAHGKKVLT SLGLAVKNMD NLKETFAHLS ELHCDKLHAD PENFKLLGNM LVIVLSSYFG
KEFTAEAQAA WQKLVVGVAT ALSHKYH
