HBG1_PLEMO
ID HBG1_PLEMO Reviewed; 147 AA.
AC Q9GLX4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Hemoglobin subunit gamma-1;
DE AltName: Full=Gamma-1-globin;
DE AltName: Full=Hemoglobin gamma-1 chain;
GN Name=HBG1;
OS Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC Pitheciidae; Callicebinae; Plecturocebus.
OX NCBI_TaxID=9523;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9461379; DOI=10.1016/s0378-1119(97)00476-9;
RA Chiu C.-H., Schneider H., Slightom J.L., Gumucio D.L., Goodman M.;
RT "Dynamics of regulatory evolution in primate beta-globin gene clusters:
RT cis-mediated acquisition of simian gamma fetal expression patterns.";
RL Gene 205:47-57(1997).
CC -!- FUNCTION: Gamma chains make up the fetal hemoglobin F, in combination
CC with alpha chains. {ECO:0000250|UniProtKB:P69891}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two gamma chains in
CC fetal hemoglobin (Hb F). {ECO:0000250|UniProtKB:P69891}.
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; AF016986; AAG33928.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GLX4; -.
DR SMR; Q9GLX4; -.
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 2: Evidence at transcript level;
KW Acetylation; Heme; Iron; Metal-binding; Oxygen transport; Phosphoprotein;
KW S-nitrosylation; Transport.
FT CHAIN 1..147
FT /note="Hemoglobin subunit gamma-1"
FT /id="PRO_0000053240"
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"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69891"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69891"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69891"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 94
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69891"
SQ SEQUENCE 147 AA; 15954 MW; 899CA5C6D6E0FA14 CRC64;
MSNFTAEDKA AITSLWGKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGSLS SPSAIMGNPK
VKAHGVKVLT SLGEAIKNLD DLKGTFDQLS ELHCDKLHVD PENFRLLGNV LVTVLAILHG
KEFTPEVQAS RQKMVAGVAS ALGSRYH