ID   HBG1_PONPY              Reviewed;         147 AA.
AC   P18995;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Hemoglobin subunit gamma-1;
DE   AltName: Full=Gamma-1-globin;
DE   AltName: Full=Hemoglobin gamma-1 chain;
GN   Name=HBG1;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3034897; DOI=10.1016/s0021-9258(18)47590-4;
RA   Slightom J.L., Theisen T.W., Koop B.F., Goodman M.;
RT   "Orangutan fetal globin genes. Nucleotide sequence reveal multiple gene
RT   conversions during hominid phylogeny.";
RL   J. Biol. Chem. 262:7472-7483(1987).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M16208; AAA36933.1; -; Genomic_DNA.
DR   EMBL; M92296; AAA36930.1; -; Genomic_DNA.
DR   PIR; A27800; A27800.
DR   AlphaFoldDB; P18995; -.
DR   SMR; P18995; -.
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   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_0000053265"
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;  16131 MW;  8854448B27A9C87E CRC64;
     MGHFTEEDKA TITSLWGKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGNLS SASAIMGNPK
     VKAHGKKVLT SLGDAIKNLD DLKGTFAQLS ELHCDKLHVD PENFRLLGNV LVTVLAIHFG
     KEFTPEVQAS WQKMVTGVAS ALSSRYH