HBA_CYPCA
ID HBA_CYPCA Reviewed; 143 AA.
AC P02016;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
GN Name=hba;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6548931; DOI=10.1016/0167-4781(84)90037-x;
RA Takeshita S., Aoki T., Fukumaki Y., Takagi Y.;
RT "Cloning and sequence analysis of a cDNA for the alpha-globin mRNA of carp,
RT Cyprinus carpio.";
RL Biochim. Biophys. Acta 783:265-271(1984).
RN [2]
RP PROTEIN SEQUENCE OF 2-143, AND ACETYLATION AT SER-2.
RX PubMed=4875309;
RA Hilse K., Braunitzer G.;
RT "Hemoglobin, XVI. Amino acid sequence of the alpha-chain of both main
RT components of carp hemoglobin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 349:433-450(1968).
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 -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M25643; AAA49202.1; -; mRNA.
DR PIR; I50491; HACA.
DR AlphaFoldDB; P02016; -.
DR SMR; P02016; -.
DR iPTMnet; P02016; -.
DR Proteomes; UP000694384; Unplaced.
DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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 InterPro; IPR002339; Hemoglobin_pi.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
DR PRINTS; PR00815; PIHAEM.
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:4875309"
FT CHAIN 2..143
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052615"
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 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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:4875309"
FT CONFLICT 13..14
FT /note="GL -> IA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59..61
FT /note="KHG -> HGK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="F -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..115
FT /note="HNVIVVIGMLY -> NHIVVGIMFYL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 143 AA; 15447 MW; 19D963BC7E6AEB25 CRC64;
MSLSDKDKAA VKGLWAKISP KADDIGAEAL GRMLTVYPQT KTYFAHWADL SPGSGPVKKH
GKVIMGAVGD AVSKIDDLVG GLAALSELHA FKLRVDPANF KILAHNVIVV IGMLYPGDFP
PEVHMSVDKF FQNLALALSE KYR