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Hemoglobin subunit gamma-1 (Gamma-1-globin) (Hemoglobin gamma-1 chain) (Hemoglobin gamma-A chain)

 HBG1_PANTR              Reviewed;         147 AA.
P61920; P02096;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 85.
RecName: Full=Hemoglobin subunit gamma-1;
AltName: Full=Gamma-1-globin;
AltName: Full=Hemoglobin gamma-1 chain;
AltName: Full=Hemoglobin gamma-A chain;
Name=HBG1;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3870867;
Slightom J.L., Chang L.-Y.E., Koop B.F., Goodman M.;
"Chimpanzee fetal G gamma and A gamma globin gene nucleotide sequences
provide further evidence of gene conversions in hominine evolution.";
Mol. Biol. Evol. 2:370-389(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1342932; DOI=10.1016/1055-7903(92)90024-B;
Bailey W.J., Hayasaka K., Skinner C.G., Kehoe S., Sieu L.C.,
Slightom J.L., Goodman M.;
"Reexamination of the African hominoid trichotomy with additional
sequences from the primate beta-globin gene cluster.";
Mol. Phylogenet. Evol. 1:97-135(1992).
[3]
PROTEIN SEQUENCE OF 2-147.
PubMed=11452387;
de Jong W.W.W.;
"Chimpanzee foetal haemoglobin: structure and heterogeneity of the
gamma chain.";
Biochim. Biophys. Acta 251:217-226(1971).
-!- FUNCTION: Gamma chains make up the fetal hemoglobin F, in
combination with alpha chains.
-!- SUBUNIT: Heterotetramer of two alpha chains and two gamma chains
in fetal hemoglobin (Hb F). The ratio of gamma-G to gamma-A chains
in is approximately 2:1 in infant chimpanzee, and 1:2 in the
adult.
-!- TISSUE SPECIFICITY: Red blood cells.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
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EMBL; X03110; CAA26892.1; -; Genomic_DNA.
EMBL; M92294; AAA35410.1; -; Genomic_DNA.
PIR; I36940; HGCZA.
RefSeq; NP_001129303.1; NM_001135831.1.
UniGene; Ptr.6100; -.
UniGene; Ptr.6101; -.
ProteinModelPortal; P61920; -.
SMR; P61920; -.
STRING; 9598.ENSPTRP00000048283; -.
PaxDb; P61920; -.
PRIDE; P61920; -.
GeneID; 736917; -.
KEGG; ptr:736917; -.
CTD; 3047; -.
eggNOG; KOG3378; Eukaryota.
eggNOG; COG1018; LUCA.
HOGENOM; HOG000036868; -.
HOVERGEN; HBG009709; -.
InParanoid; P61920; -.
KO; K13824; -.
Proteomes; UP000002277; Unplaced.
GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
CDD; cd08925; Hb-beta_like; 1.
Gene3D; 1.10.490.10; -; 1.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like_sf.
InterPro; IPR012292; Globin/Proto.
InterPro; IPR002337; Haemoglobin_b.
Pfam; PF00042; Globin; 1.
PRINTS; PR00814; BETAHAEM.
SUPFAM; SSF46458; SSF46458; 1.
PROSITE; PS01033; GLOBIN; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing; Heme; Iron;
Metal-binding; Oxygen transport; Phosphoprotein; Reference proteome;
S-nitrosylation; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P69891,
ECO:0000269|PubMed:11452387}.
CHAIN 2 147 Hemoglobin subunit gamma-1.
/FTId=PRO_0000053262.
METAL 64 64 Iron (heme distal ligand).
{ECO:0000255|PROSITE-ProRule:PRU00238}.
METAL 93 93 Iron (heme proximal ligand).
{ECO:0000255|PROSITE-ProRule:PRU00238}.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000250|UniProtKB:P69891}.
MOD_RES 13 13 Phosphothreonine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:P69891}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000250|UniProtKB:P69891}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000250|UniProtKB:P69891}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 83 83 N6-acetyllysine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 94 94 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000250|UniProtKB:P69891}.
SEQUENCE 147 AA; 16140 MW; 8FCDC3DA1B416DDE CRC64;
MGHFTEEDKA TITSLWGKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGNLS SASAIMGNPK
VKAHGKKVLT SLGDAIKHLD DLKGTFAQLS ELHCDKLHVD PENFKLLGNV LVTVLAIHFG
KEFTPEVQAS WQKMVTAVAS ALSSRYH


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