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HBG_MACMU
ID   HBG_MACMU               Reviewed;         147 AA.
AC   P68077; P02098;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Hemoglobin subunit gamma;
DE   AltName: Full=Gamma-globin;
DE   AltName: Full=Hemoglobin gamma chain;
GN   Name=HBG;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3410846; DOI=10.1016/s0021-9258(18)37773-1;
RA   Slightom J.L., Koop B.F., Xu P., Goodman M.;
RT   "Rhesus fetal globin genes. Concerted gene evolution in the descent of
RT   higher primates.";
RL   J. Biol. Chem. 263:12427-12438(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-147.
RX   PubMed=6157408; DOI=10.1021/bi00560a009;
RA   Mahoney W.C., Nute P.E.;
RT   "Fetal hemoglobin of the rhesus monkey, Macaca mulatta: complete primary
RT   structure of the gamma chain.";
RL   Biochemistry 19:4436-4442(1980).
CC   -!- FUNCTION: Gamma chains make up the fetal hemoglobin F, in combination
CC       with alpha chains.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two gamma chains in
CC       fetal hemoglobin (Hb F).
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; M19434; AAA36846.1; -; Genomic_DNA.
DR   PIR; A31109; HGMQR.
DR   AlphaFoldDB; P68077; -.
DR   SMR; P68077; -.
DR   STRING; 9544.ENSMMUP00000031232; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   InParanoid; P68077; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR   GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0031721; F:hemoglobin alpha binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR   GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR   GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR   GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6157408"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit gamma"
FT                   /id="PRO_0000053259"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   147 AA;  16101 MW;  8854449B26A9C87E CRC64;
     MGHFTEEDKA TITSLWGKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGNLS SASAIMGNPK
     VKAHGKKVLT SLGDAIKNLD DLKGTFAQLS ELHCDKLHVD PENFRLLGNV LVTVLAIHFG
     KEFTPEVQAS WQKMVAGVAS ALSSRYH
 
 
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