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HBB2_PSEUR
ID   HBB2_PSEUR              Reviewed;         146 AA.
AC   P83625;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Hemoglobin subunit beta-2;
DE   AltName: Full=Beta-2-globin;
DE   AltName: Full=Hemoglobin beta-2 chain;
GN   Name=hbb2;
OS   Pseudaphritis urvillii (Congolli) (Freshwater flathead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Pseudaphritis.
OX   NCBI_TaxID=56722;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBUNIT.
RC   TISSUE=Erythrocyte {ECO:0000269|PubMed:15340169};
RX   PubMed=15340169; DOI=10.1110/ps.04861504;
RA   Verde C., Howes B.D., De Rosa M.C., Raiola L., Smulevich G., Williams R.,
RA   Giardina B., Parisi E., Di Prisco G.;
RT   "Structure and function of the Gondwanian hemoglobin of Pseudaphritis
RT   urvillii, a primitive notothenioid fish of temperate latitudes.";
RL   Protein Sci. 13:2766-2781(2004).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Hb2 is a heterotetramer of two alpha chains and two beta-2
CC       chains. {ECO:0000269|PubMed:15340169}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P83625; -.
DR   SMR; P83625; -.
DR   GO; GO:0005833; C:hemoglobin complex; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0015671; P:oxygen transport; IDA:UniProtKB.
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-2"
FT                   /id="PRO_0000053080"
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:0000250|UniProtKB:P80044,
FT                   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:0000250|UniProtKB:P80044,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   146 AA;  16340 MW;  14A5458AE2A50E6F CRC64;
     VEWTDFERAT IKDIFSKIEY EVVGPAALAR CLVVYPWTQR YFGKFGNLYN AEAITGNPMI
     SKHGTTILHG LDRAVKNMDD IKNTYAELSV LHSETLHVDP DNFKLLSDCL TIVVAGQLGK
     DFTGEVQAAF QKFLAVVVSS LGRQYH
 
 
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