HBG1_GORGO
ID HBG1_GORGO Reviewed; 147 AA.
AC P62741; P06641;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Hemoglobin subunit gamma-1;
DE AltName: Full=Gamma-1-globin;
DE AltName: Full=Hemoglobin gamma-1 chain;
DE AltName: Full=Hemoglobin gamma-A chain;
GN Name=HBG1;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6599972; DOI=10.1093/oxfordjournals.molbev.a040325;
RA Scott A.F., Heath P., Trusko S., Boyer S.H., Prass W., Goodman M.,
RA Czelusniak J., Chang L.-Y.E., Slightom J.L.;
RT "The sequence of the gorilla fetal globin genes: evidence for multiple gene
RT conversions in human evolution.";
RL Mol. Biol. Evol. 1:371-389(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1342932; DOI=10.1016/1055-7903(92)90024-b;
RA Bailey W.J., Hayasaka K., Skinner C.G., Kehoe S., Sieu L.C., Slightom J.L.,
RA Goodman M.;
RT "Reexamination of the African hominoid trichotomy with additional sequences
RT from the primate beta-globin gene cluster.";
RL Mol. Phylogenet. Evol. 1:97-135(1992).
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; X03112; CAA26894.1; -; Genomic_DNA.
DR EMBL; M92295; AAA35466.1; -; Genomic_DNA.
DR PIR; I37022; I37022.
DR AlphaFoldDB; P62741; -.
DR SMR; P62741; -.
DR InParanoid; P62741; -.
DR Proteomes; UP000001519; 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 2: Evidence at transcript level;
KW Acetylation; Heme; Iron; Metal-binding; Oxygen transport; Phosphoprotein;
KW Reference proteome; S-nitrosylation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P69891"
FT CHAIN 2..147
FT /note="Hemoglobin subunit gamma-1"
FT /id="PRO_0000053251"
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 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P69891"
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; 16110 MW; 8FCE11DA2460A2DE CRC64;
MGHFTEEDKA TITSLWGKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGNLS SASAIMGNPK
VKAHGKKVLT SLGGAIKHLD DLKGTFAQLS ELHCDKLHVD PENFRLLGNV LVTVLAIHFG
KEFTPEVQAS WQKMVTAVAS ALSSRYH
