ID   HBB1_PAGBO              Reviewed;         147 AA.
AC   O93348; P82346;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Hemoglobin subunit beta-1;
DE   AltName: Full=Beta-1-globin;
DE   AltName: Full=Hb 1;
DE   AltName: Full=Hemoglobin beta-1 chain;
GN   Name=hbb1;
OS   Pagothenia borchgrevinki (Bald rockcod) (Trematomus borchgrevinki).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Pagothenia.
OX   NCBI_TaxID=8213;
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.
RC   TISSUE=Blood;
RA   Riccio A., Tamburrini M., Carratore V., di Prisco G.;
RT   "Functionally distinct haemoglobins of the cryopelagic antarctic teleost
RT   Pagothenia borchgrevinki.";
RL   J. Fish Biol. 57:20-32(2000).
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   -!- MISCELLANEOUS: This fish has five hemoglobins: Hb C, Hb O, Hb 1, Hb 2
CC       and Hb 3. Hb 0 presents the strongest Bohr effect while Hb 1 presents
CC       the weakest Bohr effect.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; AF067567; AAC41385.1; -; mRNA.
DR   AlphaFoldDB; O93348; -.
DR   SMR; O93348; -.
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|Ref.2"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta-1"
FT                   /id="PRO_0000053049"
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        88
FT                   /note="D -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   147 AA;  16335 MW;  251E8D31EC83321C CRC64;
     MVEWTDKERS IISDIFSHLD YEDIGPKALS RCLIVYPWTQ RHFSGFGNLY NAESIIGNAN
     VAAHGIKVLH GLDRGLKNMD NIEATYADLS TLHSEKLHVD PDNFKLLADC ITIVLAAKMG
     QAFTAEIQGA FQKFLAVVVS ALGKQYH