ID   HBAC_HOPLI              Reviewed;         142 AA.
AC   P82315;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Hemoglobin cathodic subunit alpha;
DE   AltName: Full=Hemoglobin cathodic alpha chain;
DE            Short=Hb(Ca) alpha chain;
OS   Hoplosternum littorale (Hassar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Callichthyidae; Hoplosternum.
OX   NCBI_TaxID=114109;
RN   [1]
RP   PROTEIN SEQUENCE, ACETYLATION AT SER-1, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Blood;
RX   PubMed=10747999; DOI=10.1074/jbc.m001209200;
RA   Weber R.E., Fago A., Val A.L., Bang A., Van Hauwaert M.-L., Dewilde S.,
RA   Zal F., Moens L.;
RT   "Isohemoglobin differentiation in the bimodal-breathing amazon catfish
RT   Hoplosternum littorale.";
RL   J. Biol. Chem. 275:17297-17305(2000).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000250}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC       {ECO:0000269|PubMed:10747999}.
CC   -!- MASS SPECTROMETRY: Mass=15542; Mass_error=0.2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10747999};
CC   -!- MISCELLANEOUS: This fish has two hemoglobins: cathodic and anodic. The
CC       cathodic Hb and anodic Hb display small and large Bohr effects
CC       respectively. In addition, the cathodic Hb displays a reverse Bohr
CC       effect and appreciable phosphate effects.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P82315; -.
DR   SMR; P82315; -.
DR   iPTMnet; P82315; -.
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..142
FT                   /note="Hemoglobin cathodic subunit alpha"
FT                   /id="PRO_0000052651"
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"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:10747999"
SQ   SEQUENCE   142 AA;  15545 MW;  F4139EAE0C7407C9 CRC64;
     SLTAKDKALV KAFFGKIAGK ADAVGHEALV RMLVVYPQTK TYFAHWPDLS PSSEEVKKHG
     KTIMAAVKEA VGKIDDLVGG MAQLSDLHAF KMRVDPSNFK ILSHNILVTC AVHFPDDFTP
     EVHVSFDKFL AALSSTAADK YR