ID   HBB1_VARAL              Reviewed;         146 AA.
AC   P18993;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   03-AUG-2022, entry version 90.
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   Varanus albigularis (White-throated monitor) (Varanus exanthematicus
OS   albigularis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Anguimorpha; Paleoanguimorpha; Varanoidea; Varanidae; Varanus.
OX   NCBI_TaxID=8558;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1930730; DOI=10.1515/bchm3.1991.372.2.473;
RA   Abbasi A., Braunitzer G.;
RT   "Primary structure of hemoglobin from monitor lizard (Varanus
RT   exanthematicus albigularis -- Squamata).";
RL   Biol. Chem. Hoppe-Seyler 372:473-479(1991).
RN   [2]
RP   PROTEIN SEQUENCE.
RA   Abbasi A., Braunitzer G.;
RT   "Hemoglobin -- structure, physiology and evolution.";
RL   (In) Zaidi Z.H. (eds.);
RL   Protein structure-function relationship, pp.1-13, Elsevier, Amsterdam
RL   (1988).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: The major hemoglobin component (HbIII) is a tetramer of two
CC       alpha-2 chains and two beta-1 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   PIR; S16367; HBLZC.
DR   AlphaFoldDB; P18993; -.
DR   SMR; P18993; -.
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   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Transport.
FT   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta-1"
FT                   /id="PRO_0000053150"
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"
SQ   SEQUENCE   146 AA;  16193 MW;  1D73BBFF3EAE04B7 CRC64;
     VHWTAEEKQL ICSLWGKIDV GLIGGETLAG LLVIYPWTQR QFSHFGNLSS PTAIAGNPRV
     KAHGKKVLTS FGDAIKNLDN IKDTFAKLSE LHCDKLHVDP TNFKLLGNVL VIVLADHHGK
     EFTPAHHAAY QKLVNVVSHS LARRYH