HBB_PHACA
ID HBB_PHACA Reviewed; 146 AA.
AC P10782;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3245897; DOI=10.1515/bchm3.1988.369.2.1251;
RA Huber K., Braunitzer G., Schneeganss D., Kosters J., Grimm F.;
RT "The primary structure of the hemoglobin of the Cormorant (Phalacrocorax
RT carbo, Pelecaniformes).";
RL Biol. Chem. Hoppe-Seyler 369:1251-1258(1988).
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 -!- MISCELLANEOUS: In pos. 135 of beta chain, other birds usually have Arg
CC (the positively charged AA contributes to the formation of the
CC phosphate-binding site). Here the non-polar Gly reduced phosphate
CC interactions, and oxygen affinity increased.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; S01805; HBCOG.
DR PDB; 3WR1; X-ray; 3.50 A; B=1-146.
DR PDBsum; 3WR1; -.
DR AlphaFoldDB; P10782; -.
DR SMR; P10782; -.
DR PRIDE; P10782; -.
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_0000053066"
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..16
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3WR1"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:3WR1"
SQ SEQUENCE 146 AA; 16109 MW; BB96A8E52E2CAD66 CRC64;
VHWTAEEKQL ITGLWGKVNV AECGAEALAR LLIVYPWTQR FFASFGNLSS ATAITGNPMV
RAHGKKVLTS FGEAVKNLDN IKATFAQLSE LHCDKLHVDP ENFRLLGDIL IIVLAAHFAK
DFTPECQAAW QKLVGAVAHA LARKYH
