位置:首页 > 蛋白库 > HBA1_TRENE
HBA1_TRENE
ID   HBA1_TRENE              Reviewed;         142 AA.
AC   P45718;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Hemoglobin subunit alpha-1;
DE   AltName: Full=Alpha-1-globin;
DE   AltName: Full=Hemoglobin alpha-1 chain;
GN   Name=hba1;
OS   Trematomus newnesi (Dusky notothen).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Trematomus.
OX   NCBI_TaxID=35730;
RN   [1]
RP   PROTEIN SEQUENCE, ACETYLATION AT SER-1, FUNCTION, AND SUBUNIT.
RX   PubMed=8144556; DOI=10.1016/s0021-9258(17)36935-1;
RA   D'Avino R., Caruso C., Tamburrini M., Romano M., Rutigliano B.,
RA   Polverino de Laureto P., Camardella L., Carratore V., di Prisco G.;
RT   "Molecular characterization of the functionally distinct hemoglobins of the
RT   Antarctic fish Trematomus newnesi.";
RL   J. Biol. Chem. 269:9675-9681(1994).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000269|PubMed:8144556}.
CC   -!- SUBUNIT: Hb1 is a heterotetramer of two alpha-1 chains and two beta
CC       chains. HbC is a heterotetramer of two alpha-1 chains and two beta-C
CC       chains. {ECO:0000269|PubMed:8144556}.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: This fish has three hemoglobins: Hb1 (major, about 65-
CC       70% of the total), Hb2 (about 5% of the total) and HbC (about 20-25% of
CC       the total). Hb1 and Hb2 display a very weak Bohr effect and no Root
CC       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   PIR; A54403; A54403.
DR   PDB; 1LA6; X-ray; 2.00 A; A=1-142.
DR   PDB; 1T1N; X-ray; 2.20 A; A=1-142.
DR   PDB; 2AA1; X-ray; 1.80 A; A/C=1-142.
DR   PDB; 3D1K; X-ray; 1.25 A; A=1-142.
DR   PDB; 3NFE; X-ray; 2.01 A; A/C=1-142.
DR   PDB; 3NG6; X-ray; 2.20 A; A/C=1-142.
DR   PDB; 5LFG; X-ray; 1.94 A; A/C=1-142.
DR   PDBsum; 1LA6; -.
DR   PDBsum; 1T1N; -.
DR   PDBsum; 2AA1; -.
DR   PDBsum; 3D1K; -.
DR   PDBsum; 3NFE; -.
DR   PDBsum; 3NG6; -.
DR   PDBsum; 5LFG; -.
DR   AlphaFoldDB; P45718; -.
DR   SMR; P45718; -.
DR   MINT; P45718; -.
DR   iPTMnet; P45718; -.
DR   EvolutionaryTrace; P45718; -.
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   3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW   Metal-binding; Oxygen transport; Transport.
FT   CHAIN           1..142
FT                   /note="Hemoglobin subunit alpha-1"
FT                   /id="PRO_0000052787"
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:8144556"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           37..43
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           54..72
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           77..90
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           99..113
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           120..137
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:3D1K"
SQ   SEQUENCE   142 AA;  15653 MW;  470CD779E9334A89 CRC64;
     SLSDKDKAAV RALWSKIGKS SDAIGNDALS RMIVVYPQTK IYFSHWPDVT PGSPNIKAHG
     KKVMGGIALA VSKIDDLKTG LMELSEQHAY KLRVDPSNFK ILNHCILVVI STMFPKEFTP
     EAHVSLDKFL SGVALALAER YR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024