位置:首页 > 蛋白库 > HBA_PALPA
HBA_PALPA
ID   HBA_PALPA               Reviewed;         141 AA.
AC   C0HJE0;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Hemoglobin subunit alpha {ECO:0000303|PubMed:23720132};
DE   AltName: Full=Alpha-globin {ECO:0000250|UniProtKB:P01966};
DE   AltName: Full=Hemoglobin alpha chain {ECO:0000250|UniProtKB:P01966};
GN   Name=HBA {ECO:0000250|UniProtKB:P01966};
OS   Paleosuchus palpebrosus (Cuvier's smooth-fronted caiman) (Dwarf caiman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Caimaninae;
OC   Paleosuchus.
OX   NCBI_TaxID=84099;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBUNIT.
RC   TISSUE=Erythrocyte {ECO:0000269|PubMed:23720132};
RX   PubMed=23720132; DOI=10.1152/ajpregu.00014.2013;
RA   Weber R.E., Fago A., Malte H., Storz J.F., Gorr T.A.;
RT   "Lack of conventional oxygen-linked proton and anion binding sites does not
RT   impair allosteric regulation of oxygen binding in dwarf caiman
RT   hemoglobin.";
RL   Am. J. Physiol. 305:R300-R312(2013).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues. {ECO:0000305}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains. When
CC       oxygenated in vitro, exists virtually only in polymeric form. When
CC       deoxygenated, forms tetramers, octamers and larger polymers.
CC       {ECO:0000269|PubMed:23720132}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Displays a pronounced Bohr effect despite the lack of
CC       the His at position 146 conserved in the beta subunit in most other
CC       vertebrates. Shows chloride-dependent sensitivity to organophosphates
CC       like ATP and 2,3-diphosphoglycerate (DPG) but not to inositol
CC       hexaphosphate (IHP). Binds molecular CO(2), not bicarbonate as reported
CC       for other crocodilians. {ECO:0000269|PubMed:23720132}.
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; C0HJE0; -.
DR   SMR; C0HJE0; -.
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   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Transport.
FT   CHAIN           1..141
FT                   /note="Hemoglobin subunit alpha"
FT                   /id="PRO_0000424533"
FT   BINDING         58
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:P01966,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         87
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:P01966,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   141 AA;  15748 MW;  9C46F00E38BEBD8E CRC64;
     VLSEADKSNV KGIWSKACCH LEDYGAETLE RLFFVYPQTK IYFPHFDLTH NSAQIRGHGK
     KVFLALHDAV NHIDDLSGAL SRLSDLHAHN LRVDPVNFKL LSQCVLVVFG VHHPGALTPE
     VHASLDKFLC AVSTVLTSKY R
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024