HBB_PALPA
ID HBB_PALPA Reviewed; 146 AA.
AC C0HJE1;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Hemoglobin subunit beta {ECO:0000303|PubMed:23720132};
DE AltName: Full=Beta-globin {ECO:0000250|UniProtKB:P02070};
DE AltName: Full=Hemoglobin beta chain {ECO:0000250|UniProtKB:P02070};
GN Name=HBB {ECO:0000250|UniProtKB:P02070};
OS Paleosuchus palpebrosus (Cuvier's smooth-fronted caiman) (Dwarf caiman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Caimaninae;
OC Paleosuchus.
OX NCBI_TaxID=84099;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND SUBUNIT.
RC TISSUE=Erythrocyte {ECO:0000269|PubMed:23720132};
RX PubMed=23720132; DOI=10.1152/ajpregu.00014.2013;
RA Weber R.E., Fago A., Malte H., Storz J.F., Gorr T.A.;
RT "Lack of conventional oxygen-linked proton and anion binding sites does not
RT impair allosteric regulation of oxygen binding in dwarf caiman
RT hemoglobin.";
RL Am. J. Physiol. 305:R300-R312(2013).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. {ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains. When
CC oxygenated in vitro, exists virtually only in polymeric form. When
CC deoxygenated, forms tetramers, octamers and larger polymers.
CC {ECO:0000269|PubMed:23720132}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MISCELLANEOUS: Displays a pronounced Bohr effect despite the lack of
CC the His at position 146 conserved in the beta subunit in most other
CC vertebrates. Shows chloride-dependent sensitivity to organophosphates
CC like ATP and 2,3-diphosphoglycerate (DPG) but not to inositol
CC hexaphosphate (IHP). Binds molecular CO(2), not bicarbonate as reported
CC for other crocodilians. {ECO:0000269|PubMed:23720132}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR AlphaFoldDB; C0HJE1; -.
DR SMR; C0HJE1; -.
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"
FT /id="PRO_0000424534"
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 /evidence="ECO:0000250|UniProtKB:P02070,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
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 /evidence="ECO:0000250|UniProtKB:P02070,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
SQ SEQUENCE 146 AA; 16745 MW; 353F8C159D39DFB3 CRC64;
SPFSAHEEKL ILDLWAKVNV AACGGDALSR LLIIYPWKRR YFEHFGKMAT DQDVLHNEKI
QEHGKKVLAS FGEAVKHLDN IQGHFAHLSK LHYEKFHVDC ENFKLLGNII IVVLGMHHPK
EFTMETHAAF QKLARHVAAA LSVEYY
