HBB2_BORSA
ID HBB2_BORSA Reviewed; 147 AA.
AC Q1AGS6; P84608;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Hemoglobin subunit beta-2;
DE AltName: Full=Beta-2-globin;
DE AltName: Full=Hemoglobin beta-2 chain;
GN Name=hbb2;
OS Boreogadus saida (Polar cod) (Gadus saida).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Boreogadus.
OX NCBI_TaxID=44932;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAZ99825.1}
RP PROTEIN SEQUENCE OF 2-147, NUCLEOTIDE SEQUENCE [MRNA] OF 20-147, FUNCTION,
RP AND SUBUNIT.
RC TISSUE=Blood {ECO:0000269|PubMed:16717098}, and
RC Spleen {ECO:0000269|PubMed:16717098};
RX PubMed=16717098; DOI=10.1074/jbc.m513080200;
RA Verde C., Balestrieri M., de Pascale D., Pagnozzi D., Lecointre G.,
RA di Prisco G.;
RT "The oxygen transport system in three species of the boreal fish family
RT Gadidae. Molecular phylogeny of hemoglobin.";
RL J. Biol. Chem. 281:22073-22084(2006).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000269|PubMed:16717098, ECO:0000305}.
CC -!- SUBUNIT: Hb 3 is a heterotetramer of two alpha-2 and two beta-2 chains.
CC {ECO:0000269|PubMed:16717098}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MISCELLANEOUS: Hb 3 displays a Bohr effect, which is enhanced by
CC organophosphates, and a Root effect, which is enhanced by ATP.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; DQ125473; AAZ99825.1; -; mRNA.
DR AlphaFoldDB; Q1AGS6; -.
DR SMR; Q1AGS6; -.
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:16717098"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta-2"
FT /id="PRO_0000247583"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT CONFLICT 121..122
FT /note="SA -> TG (in Ref. 1; AAZ99825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16626 MW; F9ED2AD2745CD594 CRC64;
MVEWTDSERA IITSIFSNLD YEEIGRKSLC RCLIVYPWTQ RYFGAFGNLY NAETIMANPL
IAAHGTKILH GLDRALKNMD DIKNTYAELS LLHSDKLHVD PDNFRLLADC LTVVIAAKMG
SAFTVETQVA WQKFLSVVVS ALGRQYH
