HBB2_TORMA
ID HBB2_TORMA Reviewed; 142 AA.
AC P20247;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Hemoglobin subunit beta-2;
DE AltName: Full=Beta-2-globin;
DE AltName: Full=Hemoglobin beta-2 chain;
GN Name=HBB2;
OS Torpedo marmorata (Marbled electric ray).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX NCBI_TaxID=7788;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2590465; DOI=10.1515/bchm3.1989.370.2.831;
RA Huber F., Braunitzer G.;
RT "The primary structure of electric ray hemoglobin (Torpedo marmorata). Bohr
RT effect and phosphate interaction.";
RL Biol. Chem. Hoppe-Seyler 370:831-838(1989).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; S05421; HBRYM.
DR AlphaFoldDB; P20247; -.
DR SMR; P20247; -.
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 Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR Pfam; PF00042; Globin; 1.
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..142
FT /note="Hemoglobin subunit beta-2"
FT /id="PRO_0000053132"
FT BINDING 59
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 88
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 142 AA; 16089 MW; AE188F91D94D1CEE CRC64;
VSLTDEEKHL IQHIWSNVNV VEITAKALER VFYVYPWTTR LFTSFNHNFK ASDKGVHDHA
VNVSKALSAA IGDLHNVNKN FSALSTKHQK KLGVDTSNFM LLGQAFLVEL AAFEKDKFTP
QYHKAALKLF EVVTEALSCQ YH