HBB1_ANAMI
ID HBB1_ANAMI Reviewed; 146 AA.
AC P83272;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Hemoglobin subunit beta-1;
DE AltName: Full=Beta-1-globin;
DE AltName: Full=Hemoglobin beta-1 chain;
GN Name=hbb1;
OS Anarhichas minor (Arctic spotted wolffish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Zoarcales; Anarhichadidae; Anarhichas.
OX NCBI_TaxID=65739;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12118003; DOI=10.1074/jbc.m202474200;
RA Verde C., Carratore V., Riccio A., Tamburrini M., Parisi E., Di Prisco G.;
RT "The functionally distinct hemoglobins of the Arctic spotted wolffish
RT Anarhichas minor.";
RL J. Biol. Chem. 277:36312-36320(2002).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000269|PubMed:12118003}.
CC -!- SUBUNIT: Hb1 is a heterotetramer of two alpha-1 chains and two beta-1
CC chains; Hb2 is a heterotetramer of two alpha-2 chains and two beta-1
CC chains.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:12118003}.
CC -!- MISCELLANEOUS: Hb1 and Hb2 display a low, effector-enhanced Bohr effect
CC and no Root effect.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR AlphaFoldDB; P83272; -.
DR SMR; P83272; -.
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 CHAIN 1..146
FT /note="Hemoglobin subunit beta-1"
FT /id="PRO_0000052866"
FT BINDING 63
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 92
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 146 AA; 16033 MW; 365699BB5CFF3E08 CRC64;
VKWSDKERAV IISIFAGLDY EDIGPKALSR CLIVYPWTQR YFGSFGNLST PAAIMGNPKI
AAHGIKVLHG LDRGVKNMDN IKDAYTELSI LHSETLHVDP DNFKLLADCL TIVVAAKMGC
AFTPDTQLAF QKFLAVVVSA LGKQYC