HBE_OTOCR
ID HBE_OTOCR Reviewed; 147 AA.
AC P19759;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Hemoglobin subunit epsilon;
DE AltName: Full=Epsilon-globin;
DE AltName: Full=Hemoglobin epsilon chain;
GN Name=HBE1;
OS Otolemur crassicaudatus (Brown greater galago) (Galago crassicaudatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=9463;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=3199442; DOI=10.1016/0022-2836(88)90011-3;
RA Tagle D.A., Koop B.F., Goodman M., Slightom J.L., Hess D.L., Jones R.T.;
RT "Embryonic epsilon and gamma globin genes of a prosimian primate (Galago
RT crassicaudatus). Nucleotide and amino acid sequences, developmental
RT regulation and phylogenetic footprints.";
RL J. Mol. Biol. 203:439-455(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=1639402; DOI=10.1016/0888-7543(92)90150-q;
RA Tagle D.A., Stanhope M.J., Siemieniak D.R., Benson P.J., Goodman M.,
RA Slightom J.L.;
RT "The beta globin gene cluster of the prosimian primate Galago
RT crassicaudatus: nucleotide sequence determination of the 41-kb cluster and
RT comparative sequence analyses.";
RL Genomics 13:741-760(1992).
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; M36304; AAA35446.1; -; Genomic_DNA.
DR EMBL; U60902; AAC50960.1; -; Genomic_DNA.
DR PIR; A42829; A42829.
DR PIR; S01375; HEGC.
DR AlphaFoldDB; P19759; -.
DR SMR; P19759; -.
DR PRIDE; P19759; -.
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_0000053210"
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; 16181 MW; BC17DD8AD2D67F0B CRC64;
MVHFTAEEKA IIMSLWGKVN IEEAGGEALG RLLVVYPWTQ RFFETFGNLS SASAIMGNPK
VKAHGKKVLT SFGEAVKNMD NLKGAFAKLS ELHCDKLHVD PENFKLLGNV MVIILATHFG
KEFTPDVQAA WQKLVSGVAT ALAHKYH
