HBB_PSIKR
ID HBB_PSIKR Reviewed; 146 AA.
AC P21668;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Psittacula krameri (Rose-ringed parakeet).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Psittacula.
OX NCBI_TaxID=9228;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2803513; DOI=10.1007/bf01026432;
RA Islam A., Persson B., Zaidi Z.H., Joernvall H.;
RT "Primary structure of the hemoglobin beta-chain of rose-ringed parakeet
RT (Psittacula krameri).";
RL J. Protein Chem. 8:481-486(1989).
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 -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A34947; A34947.
DR PDB; 2ZFB; X-ray; 3.00 A; B=1-146.
DR PDBsum; 2ZFB; -.
DR AlphaFoldDB; P21668; -.
DR SMR; P21668; -.
DR EvolutionaryTrace; P21668; -.
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; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT CHAIN 1..146
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000053081"
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 HELIX 5..15
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 58..77
FT /evidence="ECO:0007829|PDB:2ZFB"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2ZFB"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:2ZFB"
SQ SEQUENCE 146 AA; 16192 MW; B589AFC40A8FAAA3 CRC64;
VHWSAEEKQL ITGLWGKVNV AECGAEALAR LLIVYPWTQR FFTSFGNLSS ASAVLGNPNV
RAHGKKVLTS FGEAVKNLDN IKNTFAQLSE LHCDKLHVDP ENFRLLGDIL IIVLAGHFGK
DFTPDCQAAW QKLVRAVAHA LARKYH
