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HBG_CARSF
ID   HBG_CARSF               Reviewed;         148 AA.
AC   P18436;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Hemoglobin subunit gamma;
DE   AltName: Full=Gamma-globin;
DE   AltName: Full=Hemoglobin gamma chain;
GN   Name=HBG;
OS   Carlito syrichta (Philippine tarsier) (Tarsius syrichta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC   Carlito.
OX   NCBI_TaxID=1868482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2488474; DOI=10.1093/oxfordjournals.molbev.a040574;
RA   Koop B.F., Tagle D.A., Goodman M., Slightom J.L.;
RT   "A molecular view of primate phylogeny and important systematic and
RT   evolutionary questions.";
RL   Mol. Biol. Evol. 6:580-612(1989).
CC   -!- FUNCTION: Gamma chains make up the fetal hemoglobin F, in combination
CC       with alpha chains.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two gamma chains in
CC       fetal hemoglobin (Hb F).
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; M33971; AAA36959.1; -; Genomic_DNA.
DR   PIR; I77330; I77330.
DR   AlphaFoldDB; P18436; -.
DR   SMR; P18436; -.
DR   STRING; 1868482.ENSTSYP00000002210; -.
DR   Proteomes; UP000189704; 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   Heme; Iron; Metal-binding; Oxygen transport; Reference proteome; Transport.
FT   CHAIN           1..148
FT                   /note="Hemoglobin subunit gamma"
FT                   /id="PRO_0000053269"
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"
SQ   SEQUENCE   148 AA;  16459 MW;  5AB48437FC21DD66 CRC64;
     MVHFTAEEKA IITSLWAKVN VEETGGEALG RLLVVYPWTQ RFFDNFGNLS SASAIMGNPK
     VKAHGKKVLS SLGEAVTHMD DLKDAFAHLS RLHCDELHVD PENFRVTPGK RAVIVLAHHF
     GREFTPQVQA AWKKLMSAVA IAMGHKYH
 
 
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