HBA_CATCL
ID HBA_CATCL Reviewed; 142 AA.
AC P02017;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
GN Name=hba;
OS Catostomus clarkii (Desert sucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Catostomoidei; Catostomidae; Catostomus.
OX NCBI_TaxID=7970;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX PubMed=4672861; DOI=10.1016/s0021-9258(19)44747-9;
RA Powers D.A., Edmundson A.B.;
RT "Multiple hemoglobins of catostomid fish. II. The amino acid sequence of
RT the major alpha chain from Catostomus clarkii hemoglobins.";
RL J. Biol. Chem. 247:6694-6707(1972).
RN [2]
RP SUBUNIT.
RX PubMed=5076774; DOI=10.1016/s0021-9258(19)44746-7;
RA Powers D.A., Edmundson A.B.;
RT "Multiple hemoglobins of catostomid fish. I. Isolation and characterization
RT of the isohemoglobins from Catostomus clarkii.";
RL J. Biol. Chem. 247:6686-6693(1972).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC {ECO:0000269|PubMed:5076774}.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- MISCELLANEOUS: This fish has ten hemoglobins, 8 of which are anodal and
CC 2 cathodal. The cathodal tetramers do not exhibit the Bohr effect, due
CC to lack of the C-terminal His in the beta chains and to blocking of the
CC alpha-amino group on the N-terminal residue of the alpha chains. The
CC possession of both anodal and cathodal hemoglobins may be a
CC physiological advantage for fish living in fast-moving water habitats.
CC -!- MISCELLANEOUS: This fish possesses 6 types of hemoglobin chains,
CC including a major alpha chain, a minor alpha chain, two major beta
CC chains, and two minor beta chains.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A92116; HACC1.
DR AlphaFoldDB; P02017; -.
DR SMR; P02017; -.
DR iPTMnet; P02017; -.
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; Transport.
FT CHAIN 1..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052588"
FT BINDING 58
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 BINDING 88
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 MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:4672861"
SQ SEQUENCE 142 AA; 15431 MW; 6CE93FDFAF90E451 CRC64;
SLSDKDKADV KIAWAKISPR ADEIGAEALG RMLTVYPQTK TYFAHWADLS PGSGPVKHGK
KVIMGAIGDA VTKFDDLLGG LASLSELHAS KLRVDPSNFK ILANCITVVI MFYLPGDFPP
EVHASVDKFF QNLALALGQK YR
