HBA_APTFO
ID HBA_APTFO Reviewed; 142 AA.
AC P01980;
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 Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233;
RN [1]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=8158641; DOI=10.1006/jmbi.1994.1259;
RA Tamburrini M., Condo S.G., di Prisco G., Giardina B.;
RT "Adaptation to extreme environments: structure-function relationships in
RT Emperor penguin haemoglobin.";
RL J. Mol. Biol. 237:615-621(1994).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-142.
RA Schnek A.G., Paul C., Vandecasserie C.;
RL (In) Brush A.H. (eds.);
RL Chemical zoology, pp.10:359-381, Academic Press, New York and London
RL (1978).
RN [3]
RP PROTEIN SEQUENCE OF 2-46.
RX PubMed=4747605; DOI=10.1016/0014-5793(73)80344-8;
RA Monier C., Schnek A.G., Dirkx J., Leonis J.;
RT "Penguin hemoglobin (Aptenodytes forsteri). A 45 residue N-terminal
RT sequence.";
RL FEBS Lett. 36:93-95(1973).
CC -!- FUNCTION: Involved in oxygen transport from the lung 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 -!- SEQUENCE CAUTION:
CC Sequence=Ref.2; Type=Miscellaneous discrepancy; Note=Differs considerably from that shown in PubMed:8158641.; Evidence={ECO:0000305};
CC Sequence=Ref.3; Type=Miscellaneous discrepancy; Note=Differs considerably from that shown in PubMed:8158641.; Evidence={ECO:0000305};
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DR PIR; S46402; HAPN.
DR AlphaFoldDB; P01980; -.
DR SMR; P01980; -.
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 Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052555"
FT BINDING 59
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"
SQ SEQUENCE 142 AA; 15599 MW; 449A4508EC22B009 CRC64;
MVLSANDKSN VKSIFSKISS HAEEYGAETL ERMFTTYPQT KTYFPHFDLH HGSAQVKAHG
KKVAAALIEA ANHIDDIAGA LSKLSDLHAE KLRVDPVNFK LLGQCFMVVV AIHHPSALTP
EIHASLDKFL CAVGNVLTSK YR
