HBA2_TELPE
ID HBA2_TELPE Reviewed; 137 AA.
AC P83113;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Hemoglobin subunit alpha-2;
DE AltName: Full=Alpha-2-globin;
DE AltName: Full=Hemoglobin alpha-2 chain;
DE Flags: Fragment;
OS Telmatobius peruvianus (Andean frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Ceratophryidae; Telmatobiinae;
OC Telmatobius.
OX NCBI_TaxID=170953 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RX PubMed=12376398; DOI=10.1152/ajpregu.00292.2002;
RA Weber R.E., Ostojic H., Fago A., Dewilde S., Van Hauwaert M.-L., Moens L.,
RA Monge C.;
RT "Novel mechanism for high-altitude adaptation in hemoglobin of the Andean
RT frog Telmatobius peruvianus.";
RL Am. J. Physiol. 283:R1052-R1060(2002).
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- PTM: The N-terminus of the mature protein is acetylated.
CC {ECO:0000269|PubMed:12376398}.
CC -!- SIMILARITY: Belongs to the globin family.
CC {ECO:0000250|UniProtKB:P01966, ECO:0000255|PROSITE-ProRule:PRU00238}.
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DR AlphaFoldDB; P83113; -.
DR SMR; P83113; -.
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..137
FT /note="Hemoglobin subunit alpha-2"
FT /id="PRO_0000052781"
FT BINDING 54
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:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 83
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:0000255|PROSITE-ProRule:PRU00238"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:12376398"
SQ SEQUENCE 137 AA; 15294 MW; 31D7D2E8C595B37A CRC64;
DDRSHILAIW PSVASHGADY GGEALYRLFL SNPQTKTYFP NFDFHKDSPQ IKAHGKKVVD
ALTEASKHLD NINGALSKLF DLHAFELRVD PGNFPLLAHH INVTIAVMFP DDKFDIAHHQ
LDKFLAAVGG SLTSKYR