HBB_OTOCR
ID HBB_OTOCR Reviewed; 146 AA.
AC P02050;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Hemoglobin subunit beta-1/2;
DE AltName: Full=Beta-1/2-globin;
DE AltName: Full=Hemoglobin beta-1/2 chain;
GN Name=HBB;
OS Otolemur crassicaudatus (Brown greater galago) (Galago crassicaudatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=9463;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=4005042; DOI=10.1515/bchm3.1985.366.1.265;
RA Watanabe B., Fujii T., Nakashima Y., Maita T., Matsuda G.;
RT "Amino-acid sequences of the alpha and beta chains of adult hemoglobins of
RT the Grand Galago, Galago crassicaudatus.";
RL Biol. Chem. Hoppe-Seyler 366:265-269(1985).
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 -!- POLYMORPHISM: There are two alleles. The sequence shown is that of
CC beta-1. {ECO:0000269|PubMed:4005042}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A02367; HBGC.
DR PIR; A90683; HBGC2.
DR AlphaFoldDB; P02050; -.
DR SMR; P02050; -.
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 CHAIN 1..146
FT /note="Hemoglobin subunit beta-1/2"
FT /id="PRO_0000052961"
FT BINDING 63
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 92
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 1
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 93
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT VARIANT 125
FT /note="E -> Q (in beta-2)"
FT /evidence="ECO:0000269|PubMed:4005042"
SQ SEQUENCE 146 AA; 15934 MW; FC2BEB1E091FACEE CRC64;
VHLTPDEKNA VCALWGKVNV EEVGGEALGR LLVVYPWTQR FFDSFGDLSS PSAVMGNPKV
KAHGKKVLSA FSDGLQHLDN LCGTFAKLSE LHCDKLHVNP ENFRLLGNVL VCVLAHHFGK
DFTPEVQAAY EKVVAGVATA LAHKYH
