HBE_CEBAL
ID HBE_CEBAL Reviewed; 147 AA.
AC Q28220;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Hemoglobin subunit epsilon;
DE AltName: Full=Epsilon-globin;
DE AltName: Full=Hemoglobin epsilon chain;
GN Name=HBE1;
OS Cebus albifrons (White-fronted capuchin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Cebus.
OX NCBI_TaxID=9514;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8276414; DOI=10.1006/geno.1993.1422;
RA Hayasaka K., Skinner C.G., Goodman M., Slightom J.L.;
RT "The gamma-globin genes and their flanking sequences in primates: findings
RT with nucleotide sequences of capuchin monkey and tarsier.";
RL Genomics 18:20-28(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; M81409; AAA19702.1; -; Unassigned_DNA.
DR AlphaFoldDB; Q28220; -.
DR SMR; Q28220; -.
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_0000053200"
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; 16306 MW; 5EF74AC3FDAF3F67 CRC64;
MVHFTADEKV AITSLWSKMN VEEAGGEALG RLLVVYPWTQ RFFDNFGNLS SPSAILGNPK
VKAHGKKVLT SFGDAIKNMD NLKTTFAKLS ELHCDKLHVD PENFRLLGNV MVIILATHFG
KEFTPEVQAA WQKLVSAVAI ALGHKYH