HBB_TACAC
ID HBB_TACAC Reviewed; 147 AA.
AC P02110;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Tachyglossus aculeatus aculeatus (Southeast Australian short-beaked
OS echidna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Tachyglossidae; Tachyglossus.
OX NCBI_TaxID=49271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Kidney;
RA Lee M.H., Shroff R., Hope R.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=4663350; DOI=10.1071/bi9720989;
RA Whittaker R.G., Fisher W.K., Thompson E.O.P.;
RT "Studies on monotreme proteins. I. Amino acid sequence of the beta-chain of
RT haemoglobin from the echidna, Tachyglossus aculeatus aculeatus.";
RL Aust. J. Biol. Sci. 25:989-1004(1972).
RN [3]
RP VARIANTS GLU-6 AND ALA-139.
RX PubMed=4798231; DOI=10.1071/bi9731327;
RA Thompson E.O.P., Fisher W.K., Whittaker R.G.;
RT "Studies on monotreme proteins. 3. Amino acid sequence of the alpha- and
RT beta-globin chains of the minor haemoglobin from the echidna, Tachyglossus
RT aculeatus aculeatus.";
RL Aust. J. Biol. Sci. 26:1327-1335(1973).
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 -!- MISCELLANEOUS: In a single animal, two types of beta chains were
CC obtained from hemoglobin I having the alpha-1 B chain variant.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; L23800; AAB42177.1; -; Genomic_DNA.
DR PIR; A90087; HBTG.
DR AlphaFoldDB; P02110; -.
DR SMR; P02110; -.
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 Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Phosphoprotein; S-nitrosylation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086,
FT ECO:0000269|PubMed:4663350"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000053120"
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 45
FT /note="Phosphoserine"
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"
FT VARIANT 6
FT /note="G -> E (in allelic variant)"
FT /evidence="ECO:0000269|PubMed:4798231"
FT VARIANT 139
FT /note="S -> A (in allelic variant)"
FT /evidence="ECO:0000269|PubMed:4798231"
SQ SEQUENCE 147 AA; 16105 MW; F4F4B145998A6B19 CRC64;
MVHLSGSEKT AVTNLWGHVN VNELGGEALG RLLVVYPWTQ RFFESFGDLS SADAVMGNAK
VKAHGAKVLT SFGDALKNLD NLKGTFAKLS ELHCDKLHVD PENFNRLGNV LVVVLARHFS
KEFTPEAQAA WQKLVSGVSH ALAHKYH
