ID   HBE_ATEBE               Reviewed;         147 AA.
AC   P51438;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Hemoglobin subunit epsilon;
DE   AltName: Full=Epsilon-globin;
DE   AltName: Full=Hemoglobin epsilon chain;
GN   Name=HBE1;
OS   Ateles belzebuth (White-bellied spider monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae;
OC   Atelinae; Ateles.
OX   NCBI_TaxID=9507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Lymphocyte;
RX   PubMed=8136923; DOI=10.1006/mpev.1993.1022;
RA   Schneider H., Schneider M.P.C., Sampaio I., Harada M.L., Stanhope M.J.,
RA   Czekysbuaj J., Goodman M.;
RT   "Molecular phylogeny of the New World monkeys (Platyrrhini, primates).";
RL   Mol. Phylogenet. Evol. 2:225-242(1993).
CC   -!- FUNCTION: The epsilon chain is a beta-type chain of early mammalian
CC       embryonic hemoglobin.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two epsilon chains in
CC       early embryonic hemoglobin Gower-2; two zeta chains and two epsilon
CC       chains in early embryonic hemoglobin Gower-1.
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; L25369; AAA36925.1; -; Genomic_DNA.
DR   AlphaFoldDB; P51438; -.
DR   SMR; P51438; -.
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; Phosphoprotein; Transport.
FT   CHAIN           1..147
FT                   /note="Hemoglobin subunit epsilon"
FT                   /id="PRO_0000053187"
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         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02100"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02100"
SQ   SEQUENCE   147 AA;  16228 MW;  252E16BE1BFC2355 CRC64;
     MVHLTAEEKA AITSLWGKMN VEEAGGEALG RLLVVYPWTQ RFFDNFGNLS SPSAILGNPK
     VKAHGKKVLT SFGDAIKNMD NLKTTFAKLS ELHCDKLHVD PENFRLLGNV MVIILATHFG
     KEFTPEVQAA WQKLVSAVAI ALGHKYH