HBB_GYMAC
ID HBB_GYMAC Reviewed; 147 AA.
AC P29625; Q71UP5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=hbb;
OS Gymnodraco acuticeps (Antarctic dragonfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Bathydraconidae; Gymnodraco.
OX NCBI_TaxID=8218;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9671736; DOI=10.1073/pnas.95.15.8670;
RA Bargelloni L., Marcato S., Patarnello T.;
RT "Antarctic fish hemoglobins: evidence for adaptive evolution at subzero
RT temperature.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8670-8675(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=1727645; DOI=10.1016/0003-9861(92)90082-8;
RA Tamburrini M., Brancaccio A., Ippoliti R., di Prisco G.;
RT "The amino acid sequence and oxygen-binding properties of the single
RT hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps.";
RL Arch. Biochem. Biophys. 292:295-302(1992).
CC -!- FUNCTION: Involved in oxygen transport from gills 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 EMBL; AF067568; AAC41386.1; -; mRNA.
DR PIR; S20271; S20271.
DR AlphaFoldDB; P29625; -.
DR SMR; P29625; -.
DR Proteomes; UP000515161; Unplaced.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1727645"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052967"
FT BINDING 64
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 93
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"
SQ SEQUENCE 147 AA; 16180 MW; 7BC8CBDE61B7199B CRC64;
MVNWTKTEKA TITDIFSHLD YDDIGPKALS RCLIVYPWTQ RYFSGFGNLY NAAAIIGNAK
VAEHGIKVLH GLDLGLKKMD NIEAAYADLS SLHSEKLHVD PDNFKLLSDC ITIVLAAKLG
SAFTAETQAT FQKFLGAVMS ALGKQYH