HBE_SAIBB
ID HBE_SAIBB Reviewed; 147 AA.
AC P68029; P51444; Q29409;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Hemoglobin subunit epsilon;
DE AltName: Full=Epsilon-globin;
DE AltName: Full=Hemoglobin epsilon chain;
GN Name=HBE1;
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphocyte;
RX PubMed=8845968; DOI=10.1006/mpev.1995.1029;
RA Harada M.L., Schneider H., Schneider M.P.C., Sampaio I., Czelusniak J.,
RA Goodman M.;
RT "DNA evidence on the phylogenetic systematics of New World monkeys: support
RT for the sister-grouping of Cebus and Saimiri from two unlinked nuclear
RT genes.";
RL Mol. Phylogenet. Evol. 4:331-349(1995).
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; U18616; AAB40983.1; -; Genomic_DNA.
DR RefSeq; XP_003923417.1; XM_003923368.2.
DR AlphaFoldDB; P68029; -.
DR SMR; P68029; -.
DR STRING; 39432.ENSSBOP00000022178; -.
DR Ensembl; ENSSBOT00000039025; ENSSBOP00000022178; ENSSBOG00000027626.
DR GeneID; 101035846; -.
DR KEGG; sbq:101035846; -.
DR CTD; 3046; -.
DR GeneTree; ENSGT00940000157809; -.
DR OMA; INGLWSK; -.
DR OrthoDB; 1370439at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005833; C:hemoglobin complex; IEA:Ensembl.
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;
KW Reference proteome; Transport.
FT CHAIN 1..147
FT /note="Hemoglobin subunit epsilon"
FT /id="PRO_0000053228"
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; 16292 MW; 89AD775A06314E30 CRC64;
MVHFTAEEKA AITSLWSKMN VEEAGGEALG RLLVVYPWTQ RFFDNFGNLS SPSAILGNPK
VKAHGKKVLT SFGDAIKNMD NLKTTFAKLS ELHCDKLHVD PENFRLLGNV MVIILATHFG
KEFTPEVQAA WQKLVSAVAI ALGHKYH
