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HBB4_ONCMY
ID   HBB4_ONCMY              Reviewed;         148 AA.
AC   P02141; Q91199;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Hemoglobin subunit beta-4;
DE   AltName: Full=Beta-4-globin;
DE   AltName: Full=Hemoglobin beta-4 chain;
DE   AltName: Full=Hemoglobin beta-IV chain;
GN   Name=hbb4;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yoshizaki G., Kang J.-H., Sakuma K., Aoki T., Takashima F.;
RT   "Cloning and sequencing of rainbow trout beta-globin cDNA.";
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-148.
RA   Petruzzelli R., Barra D., Goffredo B.M., Bossa F., Coletta M., Brunori M.;
RT   "Amino-acid sequence of beta-chain of hemoglobin IV from trout (Salmo
RT   irideus).";
RL   Biochim. Biophys. Acta 789:69-73(1984).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-42 AND 46-86.
RX   PubMed=1269767; DOI=10.1016/0014-5793(76)80253-0;
RA   Bossa F., Barra D., Coletta M., Martini F., Liverzani A., Petruzzelli R.,
RA   Bonaventura J., Brunori M.;
RT   "Primary structure of hemoglobins from trout (Salmo irideus). Partial
RT   determination of amino acid sequence of HB trout IV.";
RL   FEBS Lett. 64:76-80(1976).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; D82926; BAA11632.1; -; mRNA.
DR   PIR; A02461; HBTR4.
DR   RefSeq; NP_001118017.1; NM_001124545.1.
DR   PDB; 2R1H; X-ray; 1.90 A; B/D=2-148.
DR   PDB; 3BOM; X-ray; 1.35 A; B/D=2-148.
DR   PDBsum; 2R1H; -.
DR   PDBsum; 3BOM; -.
DR   AlphaFoldDB; P02141; -.
DR   SMR; P02141; -.
DR   GeneID; 100136291; -.
DR   KEGG; omy:100136291; -.
DR   OrthoDB; 1370439at2759; -.
DR   EvolutionaryTrace; P02141; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1269767, ECO:0000269|Ref.2"
FT   CHAIN           2..148
FT                   /note="Hemoglobin subunit beta-4"
FT                   /id="PRO_0000053101"
FT   BINDING         64
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         93
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   CONFLICT        7
FT                   /note="P -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78..81
FT                   /note="NLDD -> DLBB (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87..88
FT                   /note="TA -> AT (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..18
FT                   /evidence="ECO:0007829|PDB:3BOM"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:3BOM"
FT   HELIX           37..42
FT                   /evidence="ECO:0007829|PDB:3BOM"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:3BOM"
FT   HELIX           52..56
FT                   /evidence="ECO:0007829|PDB:3BOM"
FT   HELIX           59..77
FT                   /evidence="ECO:0007829|PDB:3BOM"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:2R1H"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:3BOM"
FT   HELIX           87..95
FT                   /evidence="ECO:0007829|PDB:3BOM"
FT   HELIX           102..123
FT                   /evidence="ECO:0007829|PDB:3BOM"
FT   HELIX           126..144
FT                   /evidence="ECO:0007829|PDB:3BOM"
SQ   SEQUENCE   148 AA;  16140 MW;  B8F24E8618DEB936 CRC64;
     MVDWTDPERS AIVGLWGKIS VDEIGPQALA RLLIVSPWTQ RHFSTFGNLS TPAAIMGNPA
     VAKHGKTVMH GLDRAVQNLD DIKNTYTALS VMHSEKLHVD PDNFRLLADC ITVCVAAKLG
     PAVFSADTQE AFQKFLAVVV SALGRQYH
 
 
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