HBA2_COTGO
ID HBA2_COTGO Reviewed; 143 AA.
AC P85083;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Hemoglobin subunit alpha-2 {ECO:0000250|UniProtKB:P45719};
DE AltName: Full=Alpha-2-globin {ECO:0000250|UniProtKB:P45719};
DE AltName: Full=Hemoglobin alpha-2 chain {ECO:0000303|PubMed:19292863};
GN Name=hba2 {ECO:0000250|UniProtKB:P45719};
OS Cottoperca gobio (Frogmouth) (Aphritis gobio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Bovichtidae; Cottoperca.
OX NCBI_TaxID=56716;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-143, SUBUNIT, AND ACETYLATION AT SER-2.
RC TISSUE=Blood {ECO:0000269|PubMed:19292863};
RX PubMed=19292863; DOI=10.1111/j.1742-4658.2009.06954.x;
RA Giordano D., Boechi L., Vergara A., Marti M.A., Samuni U., Dantsker D.,
RA Grassi L., Estrin D.A., Friedman J.M., Mazzarella L., di Prisco G.,
RA Verde C.;
RT "The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically
RT basal species--oxygen-binding equilibria, kinetics and molecular
RT dynamics.";
RL FEBS J. 276:2266-2277(2009).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000305}.
CC -!- SUBUNIT: Hb 2 is a heterotetramer of two alpha-2 and two beta chains.
CC {ECO:0000269|PubMed:19292863}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MISCELLANEOUS: This fish has two hemoglobins: Hb1 and Hb2. They display
CC the Bohr and root effects. {ECO:0000269|PubMed:19292863}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR AlphaFoldDB; P85083; -.
DR SMR; P85083; -.
DR iPTMnet; P85083; -.
DR Ensembl; ENSCGOT00000032239; ENSCGOP00000030030; ENSCGOG00000013969.
DR Proteomes; UP000504630; Genome assembly.
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 Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19292863"
FT CHAIN 2..143
FT /note="Hemoglobin subunit alpha-2"
FT /evidence="ECO:0000269|PubMed:19292863"
FT /id="PRO_0000389529"
FT BINDING 60
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:P45719,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 89
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:P45719,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:19292863"
SQ SEQUENCE 143 AA; 15764 MW; F59F11C11BA08B39 CRC64;
MSLSTKDKDT VTAFWGKVSC KAGDIGTDAL SRMLVVYPQT KTYFSHWKEL GPGSPPVQKH
GMTVMKGVGE AVAKIDDLTA GLLNLSELHA FTLRVDPANF KILSHNILVV FAIMFPHDFT
PEVHVSMDKF LAALARALSE KYR
