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HBB1_TORMA
ID   HBB1_TORMA              Reviewed;         142 AA.
AC   P20246;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Hemoglobin subunit beta-1;
DE   AltName: Full=Beta-1-globin;
DE   AltName: Full=Hemoglobin beta-1 chain;
GN   Name=HBB1;
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   AlphaFoldDB; P20246; -.
DR   SMR; P20246; -.
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   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-1"
FT                   /id="PRO_0000053131"
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;  16131 MW;  18976431996B8046 CRC64;
     VSLTDEEIRL IQHIWSNVNV VEITAKALER VFYVYPWTTR LFTSFNHNFK ASDKQVHDHA
     VNVSNAISAA IGDLHDINKN FSALSTKHQK KLGVDTSNFM LLGQAFLVEL AALEKDKFTP
     QYHKAALKLF EVVTEALSCQ YH
 
 
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