HBB_LATCH
ID HBB_LATCH Reviewed; 146 AA.
AC P23741;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1958318; DOI=10.1515/bchm3.1991.372.2.599;
RA Gorr T., Kleinschmidt T., Sgouros J.G., Kasang L.;
RT "A 'living fossil' sequence: primary structure of the coelacanth (Latimeria
RT chalumnae) hemoglobin -- evolutionary and functional aspects.";
RL Biol. Chem. Hoppe-Seyler 372:599-612(1991).
RN [2]
RP PHYLOGENETIC COMPARISONS.
RX PubMed=2034288; DOI=10.1038/351394a0;
RA Gorr T., Kleinschmidt T., Fricke H.;
RT "Close tetrapod relationships of the coelacanth Latimeria indicated by
RT haemoglobin sequences.";
RL Nature 351:394-397(1991).
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 (an
CC easy dimerization is also reported).
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; S15449; S15449.
DR AlphaFoldDB; P23741; -.
DR SMR; P23741; -.
DR STRING; 7897.ENSLACP00000005370; -.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P23741; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
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 Reference proteome; Transport.
FT CHAIN 1..146
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052985"
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: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:0000255|PROSITE-ProRule:PRU00238"
SQ SEQUENCE 146 AA; 16872 MW; E61EA7DBB67EFC52 CRC64;
VHWTETERAT IETVYQKLHL DEVGREALTR LFIVYPWTTR YFKSFGDLSS SKAIASNPKV
TEHGLKVMNK LTEAIHNLDH IKDLFHKLSE KHFHELHVDP QNFKLLSKCL IIVLATKLGK
QLTPDVQATW EKLLSVVVAA LSREYH