HBB_SMICR
ID HBB_SMICR Reviewed; 147 AA.
AC Q28932;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Sminthopsis crassicaudata (Fat-tailed dunnart) (Phascogale crassicaudata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sminthopsis.
OX NCBI_TaxID=9301;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1843.1B; TISSUE=Liver;
RX PubMed=8752008; DOI=10.1093/oxfordjournals.molbev.a025651;
RA Cooper S.J.B., Murphy R., Dolman G., Hussey D., Hope R.M.;
RT "A molecular and evolutionary study of the beta-globin gene family of the
RT Australian marsupial Sminthopsis crassicaudata.";
RL Mol. Biol. Evol. 13:1012-1022(1996).
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; Z69592; CAA93439.1; -; Genomic_DNA.
DR PIR; B49402; B49402.
DR AlphaFoldDB; Q28932; -.
DR SMR; Q28932; -.
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; S-nitrosylation;
KW 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_0000053109"
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 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; 16081 MW; EFD62EBFD53EDE86 CRC64;
MVHLSAEEKG HINAIWSKVS VDQTGAEALG RLLIVYPWTS RFFDHFGDLS SAKGVMGNAK
VQGHGAKVLT SFGDAVKNMD NLKGTFAKLS ELHCDKLHVD PENFRLLGNI LVICLAEHFG
KDFTPEVQAA WQKLVAGVAT ALAHKYH
