HBB_ODOVI
ID HBB_ODOVI Reviewed; 145 AA.
AC P02074;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Hemoglobin subunit beta-3;
DE AltName: Full=Beta-3-globin;
DE AltName: Full=Hemoglobin beta-3 chain;
DE AltName: Full=Hemoglobin beta-III chain;
GN Name=HBB;
OS Odocoileus virginianus virginianus (Virginia white-tailed deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Odocoileinae; Odocoileus.
OX NCBI_TaxID=9875;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=6841126; DOI=10.3109/03630268309038399;
RA Shimizu K., Wong S.C., Wilson J.B., Lam H., Reynolds A.E., Singh P.,
RA Huisman T.H.J., Charles N.G., Amma E.L.;
RT "The primary sequence of the beta chain of Hb type III of the Virginia
RT white-tailed deer (Odocoilus Virginianus), a comparison with putative
RT sequences of the beta chains from four additional deer hemoglobins, types
RT II, IV, V, and VIII, and relationships between intermolecular contacts,
RT primary sequence and sickling of deer hemoglobins.";
RL Hemoglobin 7:15-45(1983).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH HEME.
RA Schmidt W.C. Jr., Girling R.L., Houston T.E., Sproul G.D., Amma E.L.,
RA Huisman T.H.J.;
RT "The structure of sickling deer type III hemoglobin by molecular
RT replacement.";
RL Acta Crystallogr. B 33:335-342(1977).
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: This chain is one of five beta chain alleles.
CC {ECO:0000305|PubMed:6841126}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A02393; HBDE3.
DR PDB; 1HDS; X-ray; 1.98 A; B/D=1-145.
DR PDBsum; 1HDS; -.
DR AlphaFoldDB; P02074; -.
DR SMR; P02074; -.
DR PRIDE; P02074; -.
DR EvolutionaryTrace; P02074; -.
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 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Oxygen transport; Phosphoprotein; S-nitrosylation;
KW Transport.
FT CHAIN 1..145
FT /note="Hemoglobin subunit beta-3"
FT /id="PRO_0000053039"
FT BINDING 62
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 /evidence="ECO:0000250|UniProtKB:P80044"
FT BINDING 91
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 /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1HDS"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 92
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:1HDS"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:1HDS"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1HDS"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:1HDS"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1HDS"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 99..117
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 123..142
FT /evidence="ECO:0007829|PDB:1HDS"
SQ SEQUENCE 145 AA; 15824 MW; F3875A54C4C84323 CRC64;
MLTAEEKAAV TGFWGKVNVD VVGAEALGRL LVVYPWTQRF FEHFGDLSSA GAVMGNPKVK
AHGKRVLDAF SEGLKHLDDL KGAFAELSEL HCNKLHVDPE NFRLLGNVLV VVLARNFGGE
FTPLVQADFQ KVVAGVANAL AHRYH
