ID   HBA1_NOTNE              Reviewed;         142 AA.
AC   P10777;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Hemoglobin subunit alpha-1;
DE   AltName: Full=Alpha-1-globin;
DE   AltName: Full=Hemoglobin alpha-1 chain;
GN   Name=hba1;
OS   Notothenia neglecta (Yellowbelly rockcod) (Notothenia coriiceps neglecta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Notothenia.
OX   NCBI_TaxID=202063;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX   PubMed=2920735; DOI=10.1111/j.1432-1033.1989.tb14604.x;
RA   D'Avino R., Caruso C., Romano M., Camardella L., Rutigliano B.,
RA   di Prisco G.;
RT   "Hemoglobin from the Antarctic fish Notothenia coriiceps neglecta. 2. Amino
RT   acid sequence of the alpha chain of Hb1.";
RL   Eur. J. Biochem. 179:707-713(1989).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=2737301; DOI=10.1016/0014-5793(89)80683-0;
RA   D'Avino R., Caruso C., Schinina M.E., Rutigliano B., Romano M.,
RA   Camardella L., Bosa F., Barra D., di Prisco G.;
RT   "The amino acid sequence of the alpha- and beta-chains of the two
RT   hemoglobins of the Antarctic fish Notothenia coriiceps neglecta.";
RL   FEBS Lett. 250:53-56(1989).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Hb1 is a heterotetramer of two alpha-2 chains and two beta
CC       chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: This fish has two hemoglobins: Hb1 and Hb2.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; S02816; S02816.
DR   AlphaFoldDB; P10777; -.
DR   SMR; P10777; -.
DR   iPTMnet; P10777; -.
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   CHAIN           1..142
FT                   /note="Hemoglobin subunit alpha-1"
FT                   /id="PRO_0000052703"
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:2920735"
SQ   SEQUENCE   142 AA;  15495 MW;  C4BA34C216D2B412 CRC64;
     SLSDKDKAAV KALWSKIGKS ADAIGNDALS RMIVVYPQTK TYFSHWPSVT PGHPDIKAHG
     KKVMGGLAIA VSKINDLKAG LSNLSQQHAY KLRVDPANFK ILNHCILVVI STMFPKNFTP
     QAHVSLNKFL SGVALALAQR YR