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HBB_TRENE
ID   HBB_TRENE               Reviewed;         146 AA.
AC   P45720;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Hemoglobin subunit beta-1/2;
DE   AltName: Full=Beta-1/2-globin;
DE   AltName: Full=Hemoglobin beta-1/2 chain;
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, 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).
RN   [2] {ECO:0007744|PDB:1LA6}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=12093902; DOI=10.1073/pnas.132182099;
RA   Riccio A., Vitagliano L., di Prisco G., Zagari A., Mazzarella L.;
RT   "The crystal structure of a tetrameric hemoglobin in a partial hemichrome
RT   state.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9801-9806(2002).
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. Hb2 is a heterotetramer of two alpha-2 chains and two beta
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}.
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DR   PIR; C54403; C54403.
DR   PDB; 1LA6; X-ray; 2.00 A; B=1-146.
DR   PDB; 1T1N; X-ray; 2.20 A; B=1-146.
DR   PDB; 3D1K; X-ray; 1.25 A; B=1-146.
DR   PDB; 3NFE; X-ray; 2.01 A; B/D=1-146.
DR   PDB; 3NG6; X-ray; 2.20 A; B/D=1-146.
DR   PDB; 5LFG; X-ray; 1.94 A; B/D=1-146.
DR   PDBsum; 1LA6; -.
DR   PDBsum; 1T1N; -.
DR   PDBsum; 3D1K; -.
DR   PDBsum; 3NFE; -.
DR   PDBsum; 3NG6; -.
DR   PDBsum; 5LFG; -.
DR   AlphaFoldDB; P45720; -.
DR   SMR; P45720; -.
DR   MINT; P45720; -.
DR   EvolutionaryTrace; P45720; -.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd08925; Hb-beta-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; IPR002337; Hemoglobin_b.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta-1/2"
FT                   /id="PRO_0000053135"
FT   BINDING         63
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:0000269|PubMed:12093902,
FT                   ECO:0007744|PDB:1LA6"
FT   BINDING         92
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:0000269|PubMed:12093902,
FT                   ECO:0007744|PDB:1LA6, ECO:0007744|PDB:1T1N,
FT                   ECO:0007744|PDB:3D1K, ECO:0007744|PDB:3NFE,
FT                   ECO:0007744|PDB:3NG6"
FT   HELIX           5..17
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           20..34
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           36..42
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:5LFG"
FT   HELIX           51..56
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           58..70
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           72..76
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           101..118
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:3D1K"
FT   HELIX           124..142
FT                   /evidence="ECO:0007829|PDB:3D1K"
SQ   SEQUENCE   146 AA;  16226 MW;  32BCB8DCFA143169 CRC64;
     VEWTDKERSI ISDIFSHMDY DDIGPKALSR CLVVYPWTQR YFSGFGNLYN AEGIMSNANV
     AAHGIKVLHG LDRGMKNMDN IADAYTDLST LHSEKLHVDP DNFKLLSDCI TIVLAAKMGH
     AFTAETQGAF QKFLAAVVSA LGKQYH
 
 
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