HBA_DISEL
ID HBA_DISEL Reviewed; 135 AA.
AC C0HJT8;
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 alpha {ECO:0000303|Ref.1};
DE AltName: Full=Alpha-globin {ECO:0000250|UniProtKB:P80043};
DE AltName: Full=Hemoglobin alpha chain {ECO:0000250|UniProtKB:P80043};
DE Flags: Fragment;
GN Name=hba {ECO:0000250|UniProtKB:P80043};
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 PROTEIN SEQUENCE, FUNCTION, SUBUNIT, PTM, 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. 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 -!- PTM: The N-terminus is blocked. {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; C0HJT8; -.
DR SMR; C0HJT8; -.
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; cd08927; Hb-alpha-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; IPR002338; Hemoglobin_a-typ.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
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..135
FT /note="Hemoglobin subunit alpha"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000433393"
FT BINDING 52
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 81
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"
FT NON_TER 1
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 135 AA; 14770 MW; 5F7149E6C47BA971 CRC64;
AAVVALWGKI GKSADVIGND ALSRMIVVYP ETKTYFSHWP DLAPGSPHIK AHGKKVMGGI
ALAVTKIDDL KAGLFDLSEQ HAYKLRVDPS NFKILNHCIL VVISIMFPKE FTPEAHVSLD
KFLSGVALAL AERYK
