HBG2_PANTR
ID HBG2_PANTR Reviewed; 147 AA.
AC P61921; P02096;
DT 21-JUL-1986, 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-2;
DE AltName: Full=Gamma-2-globin;
DE AltName: Full=Hemoglobin gamma-2 chain;
DE AltName: Full=Hemoglobin gamma-G chain;
GN Name=HBG2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3870867; DOI=10.1093/oxfordjournals.molbev.a040357;
RA Slightom J.L., Chang L.-Y.E., Koop B.F., Goodman M.;
RT "Chimpanzee fetal G gamma and A gamma globin gene nucleotide sequences
RT provide further evidence of gene conversions in hominine evolution.";
RL Mol. Biol. Evol. 2:370-389(1985).
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).
RN [3]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=11452387; DOI=10.1016/0005-2795(71)90105-x;
RA de Jong W.W.W.;
RT "Chimpanzee foetal haemoglobin: structure and heterogeneity of the gamma
RT chain.";
RL Biochim. Biophys. Acta 251:217-226(1971).
CC -!- FUNCTION: Gamma chains make up the fetal hemoglobin F, in combination
CC with alpha chains. {ECO:0000250|UniProtKB:P69892}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two gamma chains in
CC fetal hemoglobin (Hb F). {ECO:0000250|UniProtKB:P69892}.
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; X03109; CAA26891.1; -; Genomic_DNA.
DR EMBL; M92294; AAA35411.1; -; Genomic_DNA.
DR PIR; I36939; HGCZG.
DR RefSeq; NP_001065247.2; NM_001071779.2.
DR AlphaFoldDB; P61921; -.
DR SMR; P61921; -.
DR Ensembl; ENSPTRT00000066372; ENSPTRP00000057950; ENSPTRG00000043688.
DR GeneID; 450979; -.
DR KEGG; ptr:450979; -.
DR CTD; 3048; -.
DR GeneTree; ENSGT00940000154647; -.
DR InParanoid; P61921; -.
DR OMA; WRKVNVE; -.
DR OrthoDB; 1370439at2759; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000043688; Expressed in bone marrow and 11 other tissues.
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 Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Phosphoprotein; Reference proteome; S-nitrosylation;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P69892,
FT ECO:0000269|PubMed:11452387"
FT CHAIN 2..147
FT /note="Hemoglobin subunit gamma-2"
FT /id="PRO_0000053263"
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:P69892"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69892"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69892"
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:P69892"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69892"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69892"
SQ SEQUENCE 147 AA; 16126 MW; 8FCDC4441B416DDE CRC64;
MGHFTEEDKA TITSLWGKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGNLS SASAIMGNPK
VKAHGKKVLT SLGDAIKHLD DLKGTFAQLS ELHCDKLHVD PENFKLLGNV LVTVLAIHFG
KEFTPEVQAS WQKMVTGVAS ALSSRYH
