HBA1_TACAC
ID HBA1_TACAC Reviewed; 141 AA.
AC P01977;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Hemoglobin subunit alpha-1;
DE AltName: Full=Alpha-1-globin;
DE AltName: Full=Hemoglobin alpha-1 chain;
OS Tachyglossus aculeatus aculeatus (Southeast Australian short-beaked
OS echidna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Tachyglossidae; Tachyglossus.
OX NCBI_TaxID=49271;
RN [1]
RP PROTEIN SEQUENCE (VARIANT B).
RX PubMed=4748330; DOI=10.1071/bi9730877;
RA Whittaker R.G., Fisher W.K., Thompson E.O.P.;
RT "Studies on monotreme proteins. II. Amino acid sequence of the alpha-chain
RT in haemoglobin from the echidna, Tachyglossus aculeatus aculeatus.";
RL Aust. J. Biol. Sci. 26:877-888(1973).
RN [2]
RP PROTEIN SEQUENCE (VARIANT A).
RX PubMed=4415942; DOI=10.1071/bi9740111;
RA Dodgson S.J., Fisher W.K., Thompson E.O.P.;
RT "Studies on monotreme proteins. IV. Amino acid sequence of haemoglobin-IA
RT of the echidna; a comparison of major haemoglobins from two geographical
RT groups of echidnas.";
RL Aust. J. Biol. Sci. 27:111-115(1974).
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 -!- MISCELLANEOUS: Echidnas have a major hemoglobin I (with alpha-1 chain
CC variants A, B, and C) and a minor hemoglobin II (with alpha-2 chain
CC variants A and B). All hemoglobins may have the same beta chain. The
CC sequences of both alpha-1 A and B variants differ from that of the
CC alpha-2 A variant at nine positions.
CC -!- MISCELLANEOUS: The sequence shown is that of alpha-1 B.
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 PIR; A90089; HATG.
DR AlphaFoldDB; P01977; -.
DR SMR; P01977; -.
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 CHAIN 1..141
FT /note="Hemoglobin subunit alpha-1"
FT /id="PRO_0000052773"
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 87
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 VARIANT 12
FT /note="S -> G (in alpha-1 A variant)"
FT VARIANT 78
FT /note="S -> N (in alpha-1 A variant)"
FT VARIANT 102
FT /note="A -> S (in alpha-1 A variant)"
FT VARIANT 115
FT /note="A -> E (in alpha-1 A variant)"
SQ SEQUENCE 141 AA; 15462 MW; D8D0FF702686A0F6 CRC64;
VLTDAEKKEV TSLWGKASGH AEEYGAEALE RLFLSFPTTK TYFSHMDLSK GSAQVKAHGK
RVADALTTAA GHFNDMDSAL SALSDLHAHK LRVDPVNFKL LAHCFLVVLA RHHPAEFTPS
AHAAMDKFLS RVATVLTSKY R