HBB1_CHAMP
ID HBB1_CHAMP Reviewed; 147 AA.
AC P68087;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Hemoglobin subunit beta-1;
DE AltName: Full=Beta-1-globin;
DE AltName: Full=Hemoglobin beta-1 chain;
DE AltName: Full=Hemoglobin beta-I chain;
GN Name=HBB1;
OS Chalinolobus morio (Chocolate-wattled bat) (Lobe-lipped bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Chalinolobus.
OX NCBI_TaxID=50353;
RN [1]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=8590629; DOI=10.1515/bchm3.1995.376.10.603;
RA Singer G.A.M., Kleinschmidt T., Braunitzer G.;
RT "The primary structure of the hemoglobin from the lobe-lipped bat
RT (Chalinolobus morio, microchiroptera).";
RL Biol. Chem. Hoppe-Seyler 376:603-609(1995).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- SUBUNIT: Hb1 is a heterotetramer of two alpha chains and two beta-1
CC 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 AlphaFoldDB; P68087; -.
DR SMR; P68087; -.
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 Methylation; Oxygen transport; Phosphoprotein; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086,
FT ECO:0000269|PubMed:8590629"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta-1"
FT /id="PRO_0000052922"
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 18
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02088"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02091"
FT MOD_RES 60
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 105
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11517"
SQ SEQUENCE 147 AA; 15964 MW; 86BC9AEC802819E9 CRC64;
MVHLTGEEKA AVTGLWGKVN VEEVGGEALG RLLVVYPWTQ RFFDSFGDLS NAGAVMGNAK
VKAHGKKVLN SFGEGLKNLD NLKGTFAKLS ELHCDKLHVD PENFRLLGNV LVVVLARHFG
KDFTPPVQAA FQKLAQGVAT ALAHKYH
