ID   HBE_GORGO               Reviewed;         147 AA.
AC   Q6LDH0;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Hemoglobin subunit epsilon;
DE   AltName: Full=Epsilon-globin;
DE   AltName: Full=Hemoglobin epsilon chain;
GN   Name=HBE1;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=1301735; DOI=10.1126/science.1301735;
RA   Bailey W.J., Slightom J.L., Goodman M.;
RT   "Rejection of the 'flying primate' hypothesis by phylogenetic evidence from
RT   the epsilon-globin gene.";
RL   Science 256:86-89(1992).
RN   [2]
RP   ERRATUM OF PUBMED:1301735.
RA   Bailey W.J., Slightom J.L., Goodman M.;
RL   Science 260:605-605(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; M81363; AAA70223.1; -; Genomic_DNA.
DR   RefSeq; XP_004050587.1; XM_004050539.2.
DR   AlphaFoldDB; Q6LDH0; -.
DR   SMR; Q6LDH0; -.
DR   STRING; 9593.ENSGGOP00000026114; -.
DR   PRIDE; Q6LDH0; -.
DR   Ensembl; ENSGGOT00000031529; ENSGGOP00000026114; ENSGGOG00000024137.
DR   GeneID; 101151732; -.
DR   KEGG; ggo:101151732; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   GeneTree; ENSGT00940000157809; -.
DR   HOGENOM; CLU_003827_10_0_1; -.
DR   InParanoid; Q6LDH0; -.
DR   OrthoDB; 1370439at2759; -.
DR   Proteomes; UP000001519; Chromosome 11.
DR   Bgee; ENSGGOG00000024137; Expressed in liver and 2 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   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Oxygen transport; Phosphoprotein;
KW   Reference proteome; Transport.
FT   CHAIN           1..147
FT                   /note="Hemoglobin subunit epsilon"
FT                   /id="PRO_0000053211"
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;  16203 MW;  223388816EDDE8D5 CRC64;
     MVHFTAEEKA AVTSLWSKMN VEEAGGEALG RLLVVYPWTQ RFFDSFGNLS SPSAILGNPK
     VKAHGKKVLT SFGDAIKNMD NLKPAFAKLS ELHCDKLHVD PENFKLLGNV MVIILATHFG
     KEFTPEVQAA WQKLVSAVAI ALAHKYH