ID   HBB_BATEA               Reviewed;         141 AA.
AC   P84217;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Bathyraja eatonii (Eaton's skate) (Raja eatonii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Rajiformes; Bathyraja.
OX   NCBI_TaxID=298348;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Erythrocyte;
RX   PubMed=15807670; DOI=10.1042/bj20050305;
RA   Verde C., De Rosa M.C., Giordano D., Mosca D., De Pascale D., Raiola L.,
RA   Cocca E., Carratore V., Giardina B., Di Prisco G.;
RT   "Structure, function and molecular adaptations of haemoglobins of the polar
RT   cartilaginous fish Bathyraja eatonii and Raja hyperborea.";
RL   Biochem. J. 389:297-306(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P84217; -.
DR   SMR; P84217; -.
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   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..141
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052887"
FT   BINDING         59
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         88
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   141 AA;  15647 MW;  78020F5BBD812E90 CRC64;
     VKITDKKAAY ITGIWSKLDK KVTTAHALER VFTVYPWTTR LFKSFNGHFK AGDSGVQGHA
     EKVVGALDTA VLHLHDIDAG YKKLSEKHQL IGVDTQNFKL LGQAFLVELA ILFKEGFTPE
     LHEAAYKFFL AVAGGLSSQY H