ID   HBAC_CONCO              Reviewed;         143 AA.
AC   P83479;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Hemoglobin cathodic subunit alpha;
DE   AltName: Full=Hemoglobin cathodic alpha chain;
OS   Conger conger (Conger eel) (Muraena conger).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Congridae; Conger.
OX   NCBI_TaxID=82655;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-143, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP   ACETYLATION AT SER-2.
RC   TISSUE=Erythrocyte;
RX   PubMed=12646043; DOI=10.1042/bj20021865;
RA   Pellegrini M., Giardina B., Verde C., Carratore V., Olianas A., Sollai L.,
RA   Sanna M.T., Castagnola M., Di Prisco G.;
RT   "Structural-functional characterization of the cathodic haemoglobin of the
RT   conger eel Conger conger: molecular modelling study of an additional
RT   phosphate-binding site.";
RL   Biochem. J. 372:679-686(2003).
CC   -!- FUNCTION: Involved in oxygen transport from the gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:12646043}.
CC   -!- MASS SPECTROMETRY: Mass=15300; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12646043};
CC   -!- MISCELLANEOUS: This fish has two types of hemoglobin: one cathodic Hb
CC       and two major anodic Hbs. The cathodic Hb displays a small normal Bohr
CC       effect and a reverse Bohr effect in the presence and absence of
CC       phosphate respectively. In addition, the cathodic HB displays a large
CC       phosphate effect.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P83479; -.
DR   SMR; P83479; -.
DR   iPTMnet; P83479; -.
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; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12646043"
FT   CHAIN           2..143
FT                   /note="Hemoglobin cathodic subunit alpha"
FT                   /id="PRO_0000052606"
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         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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:12646043"
SQ   SEQUENCE   143 AA;  15279 MW;  92DD22E89997165D CRC64;
     MSLTAKDKTL VKTFWGKVKG KADAMGAEAL GRMLVVYPQT KTYFAHWSDQ SPGSEPVKHG
     KKTIMGAVGD AVGKIDNLLG GLSALSEVHA TKLAIDPGNF KLLSHCLLVT FAVNYPTDFT
     AEVHVAVDKF LAAVSAALAD KYR