ID   HBAC_LITCT              Reviewed;         142 AA.
AC   P55267;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Hemoglobin subunit alpha-C;
DE   AltName: Full=Alpha-C-globin;
DE   AltName: Full=Hemoglobin alpha-C chain;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-142, PARTIAL PROTEIN SEQUENCE, AND
RP   ACETYLATION AT ALA-2.
RC   STRAIN=Shaw; TISSUE=Erythroid cell;
RX   PubMed=8262931; DOI=10.1016/s0021-9258(19)74204-5;
RA   Smith D.J., Zhu H., Kolatkar P.R., Tam L.-T., Baldwin T.O., Roe B.A.,
RA   Broyles R.H., Riggs A.F.;
RT   "The hemoglobins of the bullfrog, Rana catesbeiana. The cDNA-derived amino
RT   acid sequences of the alpha chains of adult hemoglobins B and C: their
RT   roles in deoxygenation-induced aggregation.";
RL   J. Biol. Chem. 268:26961-26971(1993).
CC   -!- FUNCTION: The alpha-C chain is a component of adult hemoglobin C.
CC   -!- SUBUNIT: Heterotetramer of either two alpha-B chains or two alpha-C
CC       chains and two beta chains. The two major hemoglobins, B and C,
CC       associate upon deoxygenation to form a trimer of tetramers, BC2, that
CC       has a much lower affinity for oxygen than either component alone.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; L19191; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; B49296; B49296.
DR   AlphaFoldDB; P55267; -.
DR   SMR; P55267; -.
DR   iPTMnet; P55267; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8262931"
FT   CHAIN           2..142
FT                   /note="Hemoglobin subunit alpha-C"
FT                   /id="PRO_0000052748"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:8262931"
SQ   SEQUENCE   142 AA;  15912 MW;  2E799EBA5DEC3312 CRC64;
     MALNCDDKAH IRAIWPCLAS HAEQYGAEAL HRMFLCHPQT KTYFPNFDFH ANSAHLKNHG
     KKVMNALTDA VKHLDHPEAS LSSLSDLHAF TLRVDPGNFA LLSNNILVVV AVHHSDKLSY
     ETHQALDKFL NVVSGLLTSK YR