ID   HBB1_CYGMA              Reviewed;         147 AA.
AC   P23017; O93347;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Hemoglobin subunit beta-1;
DE   AltName: Full=Beta-1-globin;
DE   AltName: Full=Hemoglobin beta-1 chain;
GN   Name=hbb1;
OS   Cygnodraco mawsoni (Antarctic dragonfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Bathydraconidae; Cygnodraco.
OX   NCBI_TaxID=8216;
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=2065095; DOI=10.1016/0167-4838(91)90569-l;
RA   Caruso C., Rutigliano B., Romano M., di Prisco G.;
RT   "The hemoglobins of the cold-adapted Antarctic teleost Cygnodraco
RT   mawsoni.";
RL   Biochim. Biophys. Acta 1078:273-282(1991).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Hb1 is a heterotetramer of two alpha chains and two beta-1
CC       chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: This fish has two hemoglobins: Hb1 (major) and Hb2
CC       (about 5% of the total). They display the Bohr and root effects.
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   EMBL; AF067566; AAC41384.1; -; mRNA.
DR   PIR; S16370; S16370.
DR   AlphaFoldDB; P23017; -.
DR   SMR; P23017; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2065095"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta-1"
FT                   /id="PRO_0000052939"
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"
FT   CONFLICT        135
FT                   /note="M -> L (in Ref. 1; AAC41384)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   147 AA;  16290 MW;  24035DCBD318377D CRC64;
     MVKWSKTELT IINDIFSHLD YDDIGPKALS RCLIVYPWTQ RHFSGFGNLY NAEAIIGNAN
     VAAHGIKVLH GLDRGLKNMD NIVDAYAELS TLHSEKLHVD PDNFKLLSDC ITIVLAAKLG
     KAFTAETQAA FQKFMAVVVS ALGKQYH