HBG2_SAPAP
ID HBG2_SAPAP Reviewed; 147 AA.
AC P68257; Q28225; Q29434;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Hemoglobin subunit gamma-2;
DE AltName: Full=Gamma-2-globin;
DE AltName: Full=Hemoglobin gamma-2 chain;
GN Name=HBG2;
OS Sapajus apella (Brown-capped capuchin) (Cebus apella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Sapajus.
OX NCBI_TaxID=9515;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8692846; DOI=10.1073/pnas.93.13.6510;
RA Chiu C.-H., Schneider H., Schneider M.P.C., Sampaio I., Meireles C.M.,
RA Slightom J.L., Gumucio D.L., Goodman M.;
RT "Reduction of two functional gamma-globin genes to one: an evolutionary
RT trend in New World monkeys (infraorder Platyrrhini).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6510-6515(1996).
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; U57045; AAC50636.1; -; Genomic_DNA.
DR PIR; G00015; G00015.
DR AlphaFoldDB; P68257; -.
DR SMR; P68257; -.
DR Proteomes; UP000504640; 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 CHAIN 1..147
FT /note="Hemoglobin subunit gamma-2"
FT /id="PRO_0000053245"
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 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69892"
SQ SEQUENCE 147 AA; 15936 MW; 8A7CB81F98E85D03 CRC64;
MSNFTAEDKA AITSLWAKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGSLS SPSAIMGNPK
VKAHGAKVLT SLGEAIKNLD DLKGTFGQLS ELHCDKLHVD PENFRLLGNV LVTVLAIHHG
KEFTPEVQAS WQKMVAGVAS ALGSRYH
