HBA1_LIPTU
ID HBA1_LIPTU Reviewed; 143 AA.
AC P85081;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Hemoglobin subunit alpha-1;
DE AltName: Full=Alpha-1-globin;
DE AltName: Full=Hemoglobin alpha-1 chain;
GN Name=hba1 {ECO:0000250|UniProtKB:P45718, ECO:0000303|PubMed:17618067};
OS Liparis tunicatus (Kelp snailfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Cottales; Liparidae; Liparis.
OX NCBI_TaxID=420949;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-143, FUNCTION, SUBUNIT, AND ACETYLATION AT SER-2.
RC TISSUE=Blood {ECO:0000269|PubMed:17618067};
RX PubMed=17618067; DOI=10.1016/j.gene.2007.06.002;
RA Giordano D., Vergara A., Lee H.C., Peisach J., Balestrieri M.,
RA Mazzarella L., Parisi E., Prisco G., Verde C.;
RT "Hemoglobin structure/function and globin-gene evolution in the Arctic fish
RT Liparis tunicatus.";
RL Gene 406:58-68(2007).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000269|PubMed:17618067, ECO:0000305}.
CC -!- SUBUNIT: Hb1 is a heterotetramer of two alpha-1 chains and two beta-1
CC chains. {ECO:0000269|PubMed:17618067}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MISCELLANEOUS: This fish has two hemoglobins: Hb1 (major) and Hb2. Hb1
CC has low oxygen affinity, it displays a pronounced Bohr effect, which is
CC enhanced by ATP, and a pronounced Root effect.
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; P85081; -.
DR SMR; P85081; -.
DR iPTMnet; P85081; -.
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:17618067"
FT CHAIN 2..143
FT /note="Hemoglobin subunit alpha-1"
FT /evidence="ECO:0000269|PubMed:17618067"
FT /id="PRO_0000312764"
FT BINDING 60
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:P45718,
FT 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:0000250|UniProtKB:P45718,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:17618067"
SQ SEQUENCE 143 AA; 15770 MW; 905A8E9806E4102D CRC64;
MSLSTKDKET VKDLWGHISA SADAIGADAL GRLLVVYPQT KIYFLHWPDL SPNSPSVKNH
GKNIMSGIAL AVTKIDDLKS GLNALSEQHA FQLRVDPANF KLLSHCILVV LAIRFPHEFT
PEAHVAMDKF FCGVSLALAE KYR
