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HBB2_DISEL
ID   HBB2_DISEL              Reviewed;         146 AA.
AC   C0HJT7;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Hemoglobin subunit beta-2 {ECO:0000303|Ref.1};
DE   AltName: Full=Beta-2-globin {ECO:0000250|UniProtKB:P84611};
DE   AltName: Full=Hemoglobin beta-2 chain {ECO:0000250|UniProtKB:P84611};
GN   Name=hbb2 {ECO:0000250|UniProtKB:P84611};
OS   Dissostichus eleginoides (Patagonian toothfish) (Dissostichus amissus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Dissostichus.
OX   NCBI_TaxID=100907 {ECO:0000303|Ref.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Erythrocyte {ECO:0000303|Ref.1};
RX   DOI=10.1007/s10750-015-2439-2;
RA   Coppola D., Giordano D., Abbruzzetti S., Marchesani F., Balestrieri M.,
RA   di Prisco G., Viappiani C., Bruno S., Verde C.;
RT   "Functional characterisation of the haemoglobins of the migratory
RT   notothenioid fish Dissostichus eleginoides.";
RL   Hydrobiologia 761:315-333(2015).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000269|Ref.1}.
CC   -!- SUBUNIT: Hb2 is a heterotetramer of two alpha chains and two beta-2
CC       chains. {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|Ref.1}.
CC   -!- MISCELLANEOUS: This fish has 2 hemoglobins: Hb1 (major) and the minor
CC       Hb2 which constitutes about 5% of the total. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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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-2"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000433395"
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;  16343 MW;  63258702B1167725 CRC64;
     VEWTDFERAT IKDIFSKIEY DVVGPATLAR CLVVYPWTQR YFGKFGNLYN AAGIAENAMV
     SKHGITILHG LDRAVKNMDD IKNTYAELSV LHSEKLHVDP DNFKLLADCL TIVVAXRFGN
     GFTGEVQAAF QKFMAVVVSS LGKQYH
 
 
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