HBA_LYCRE
ID HBA_LYCRE Reviewed; 142 AA.
AC P86882;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Hemoglobin subunit alpha {ECO:0000303|PubMed:21491556};
DE AltName: Full=Alpha-globin {ECO:0000250|UniProtKB:P56250};
DE AltName: Full=Hemoglobin alpha chain {ECO:0000250|UniProtKB:P56250};
GN Name=hba {ECO:0000250|UniProtKB:P56250};
OS Lycodes reticulatus (Arctic eelpout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Zoarcales; Zoarcidae; Lycodinae;
OC Lycodes.
OX NCBI_TaxID=215418;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND ACETYLATION AT
RP SER-1.
RC TISSUE=Blood {ECO:0000269|PubMed:21491556};
RX PubMed=21491556; DOI=10.1002/iub.450;
RA Riccio A., Mangiapia G., Giordano D., Flagiello A., Tedesco R., Bruno S.,
RA Vergara A., Mazzarella L., di Prisco G., Pucci P., Paduano L., Verde C.;
RT "Polymerization of hemoglobins in Arctic fish: Lycodes reticulatus and
RT Gadus morhua.";
RL IUBMB Life 63:346-354(2011).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000250|UniProtKB:P56250,
CC ECO:0000269|PubMed:21491556}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC {ECO:0000303|PubMed:21491556}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=15663.3; Mass_error=0.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21491556};
CC -!- MISCELLANEOUS: This fish has just a single hemoglobin. It displays a
CC weak Bohr effect that is not effector-enhanced and shows a propensity
CC to form disulfide-linked polymers in vitro.
CC {ECO:0000269|PubMed:21491556}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P86882; -.
DR SMR; P86882; -.
DR iPTMnet; P86882; -.
DR GO; GO:0005833; C:hemoglobin complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0015671; P:oxygen transport; ISS:UniProtKB.
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"
FT /id="PRO_0000419015"
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:0000250|UniProtKB:P56250,
FT 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:0000250|UniProtKB:P56250,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:21491556"
SQ SEQUENCE 142 AA; 15622 MW; 4F312EDF210B804F CRC64;
SLSDKDKAAV KAIWNKISKS ADVIGADAMG RMLVVYPQTK TYFSHWSDLS PNSAPVKNHG
KTVMTGVALA VSNIDDMTTG LKALSEKHAF QLRVDPSNFK ILSHCILVVI AMMYPKDFTP
EAHVSMDKFF CGLSLALAEK YR
