HBB1_DISEL
ID HBB1_DISEL Reviewed; 146 AA.
AC C0HJT6;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Hemoglobin subunit beta-1 {ECO:0000303|Ref.1};
DE AltName: Full=Beta-1-globin {ECO:0000250|UniProtKB:P84610};
DE AltName: Full=Hemoglobin beta-1 chain {ECO:0000250|UniProtKB:P84610};
GN Name=hbb1 {ECO:0000250|UniProtKB:P84610};
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: Hb1 is a heterotetramer of two alpha chains and two beta-1
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 AlphaFoldDB; C0HJT6; -.
DR SMR; C0HJT6; -.
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-1"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000433394"
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; 16243 MW; 9849543739D1C954 CRC64;
VHWTEKERTI ITGIFSHMDY EDIGPKALSR CLIVYPWTQR HFSCFGNLYN AEAIMGNANV
AAHGIKVLHG LDRGVKNMDN IVATYAELSI LHSEKLHVDP DNFKLLSDCI TIVVAAKMGH
AFTGETQAAF QKFLAVVVSA LGKQYH
