ID   HBG1_PANPA              Reviewed;         147 AA.
AC   Q28779;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
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   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
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) (By similarity). The ratio of gamma-G to gamma-
CC       A chains in is approximately 2:1 in infant chimpanzee, and 1:2 in the
CC       adult (PubMed:1342932). {ECO:0000250|UniProtKB:P69891,
CC       ECO:0000269|PubMed:1342932}.
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; M93716; AAA72113.1; -; Unassigned_DNA.
DR   PIR; I37002; I37002.
DR   AlphaFoldDB; Q28779; -.
DR   SMR; Q28779; -.
DR   STRING; 9597.XP_008970670.1; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   Proteomes; UP000240080; Unplaced.
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   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_0000053261"
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;  16168 MW;  8FCDDD1527AC6DDE CRC64;
     MGHFTEEDKA TITSLWGKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGNLS SASAIMGNPK
     VKAHGKKVLT SLGDAIKHLD DLKGTFAQLS ELHCDKLHVD PENFRLLGNV LVTVLAIHFG
     KEFTPEVQAS WQKMVTAVAS ALSSRYH