HBB1_ELEMC
ID HBB1_ELEMC Reviewed; 146 AA.
AC K7N5M6; P86714;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Hemoglobin subunit beta-1 {ECO:0000250|UniProtKB:P83624};
DE AltName: Full=Beta-1-globin {ECO:0000250|UniProtKB:P83624};
DE AltName: Full=Hemoglobin beta-1 chain {ECO:0000303|PubMed:23086282};
GN Name=hbb1 {ECO:0000250|UniProtKB:P83624};
OS Eleginops maclovinus (Patagonian blennie) (Eleginus maclovinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Eleginopidae; Eleginops.
OX NCBI_TaxID=56733 {ECO:0000312|PDB:4ESA};
RN [1] {ECO:0000312|PDB:4ESA}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (1.45
RP ANGSTROMS) IN COMPLEX WITH HEME AND CARBON MONOXIDE.
RC TISSUE=Blood {ECO:0000303|PubMed:23086282};
RX PubMed=23086282; DOI=10.1039/c2mb25210d;
RA Coppola D., Abbruzzetti S., Nicoletti F., Merlino A., Gambacurta A.,
RA Giordano D., Howes B.D., De Sanctis G., Vitagliano L., Bruno S.,
RA di Prisco G., Mazzarella L., Smulevich G., Coletta M., Viappiani C.,
RA Vergara A., Verde C.;
RT "ATP regulation of the ligand-binding properties in temperate and cold-
RT adapted haemoglobins. X-ray structure and ligand-binding kinetics in the
RT sub-Antarctic fish Eleginops maclovinus.";
RL Mol. Biosyst. 8:3295-3304(2012).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000303|PubMed:23086282}.
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. HbC is a heterotetramer of two alpha-1 chains and two beta-2
CC chains. {ECO:0000269|PubMed:23086282}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MISCELLANEOUS: This fish has three hemoglobins: Hb1, Hb2 and HbC
CC accounting for about 70%, 5% and 25% of the total, respectively. Hb1
CC has high oxygen affinity and displays strong Bohr, Root and phosphate
CC effects. {ECO:0000269|PubMed:23086282}.
CC -!- SIMILARITY: Belongs to the globin family.
CC {ECO:0000255|RuleBase:RU000356}.
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DR PDB; 4ESA; X-ray; 1.45 A; B/D=1-146.
DR PDB; 6RP5; X-ray; 1.49 A; B=1-144.
DR PDBsum; 4ESA; -.
DR PDBsum; 6RP5; -.
DR AlphaFoldDB; K7N5M6; -.
DR SMR; K7N5M6; -.
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 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT CHAIN 1..146
FT /note="Hemoglobin subunit beta-1"
FT /id="PRO_0000430574"
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:0000269|PubMed:23086282"
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:0000269|PubMed:23086282"
FT HELIX 5..16
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4ESA"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:4ESA"
SQ SEQUENCE 146 AA; 16133 MW; B7C5682F50A58332 CRC64;
VEWTDQERAT ISSIFGSLDY DDIGPKALSR CLIVYPWTQR HFGSFGNLYN AEAIIGNQKV
AAHGIKVLHG LDRAVKNMDN IKEIYAELSI LHSEKLHVDP DNFKLLADCL TIVVAAKMGS
GFNPGTQATF QKFLAVVVSA LGKQYH
