HBE_CARSF
ID HBE_CARSF Reviewed; 147 AA.
AC P18435;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Hemoglobin subunit epsilon;
DE AltName: Full=Epsilon-globin;
DE AltName: Full=Hemoglobin epsilon chain;
GN Name=HBE1;
OS Carlito syrichta (Philippine tarsier) (Tarsius syrichta).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC Carlito.
OX NCBI_TaxID=1868482;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2488474; DOI=10.1093/oxfordjournals.molbev.a040574;
RA Koop B.F., Tagle D.A., Goodman M., Slightom J.L.;
RT "A molecular view of primate phylogeny and important systematic and
RT evolutionary questions.";
RL Mol. Biol. Evol. 6:580-612(1989).
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; M81411; AAA16712.1; -; Unassigned_DNA.
DR EMBL; M33970; AAA36958.1; -; Genomic_DNA.
DR PIR; I57442; I57442.
DR AlphaFoldDB; P18435; -.
DR SMR; P18435; -.
DR STRING; 1868482.ENSTSYP00000017765; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR Proteomes; UP000189704; Unplaced.
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;
KW Reference proteome; Transport.
FT CHAIN 1..147
FT /note="Hemoglobin subunit epsilon"
FT /id="PRO_0000053231"
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; 16178 MW; 4D8EBF3C3611E931 CRC64;
MVHLTAEEKS SVTSLWGKMN VDEAGGEALG RLLVVYPWTQ RFFDNFGNLS SSSAIMGNPK
VKAHGKKVLT SFGDAIKNMD NLKGAFAKLS ELHCDKLHVD PENFRLLGNV LVIILVTHFG
KDFTPEVQVA WQKLVSGVAT ALAHKYH