ID   HBE_PIG                 Reviewed;         147 AA.
AC   P02101; Q29039;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Hemoglobin subunit epsilon;
DE   AltName: Full=Epsilon-globin;
DE   AltName: Full=Hemoglobin epsilon chain;
GN   Name=HBE1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sharma A., Parson C.T., Midha S., Okabe J., Yerle M., Pinton P., Logan J.,
RA   Kumar L.R.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-147.
RX   PubMed=6724525;
RA   Bieber F.A., Braunitzer G.;
RT   "Pre- and perinatal oxygen transport in mammals: the embryonic hemoglobins
RT   of the domestic pig (Sus scrofa domestica).";
RL   Hoppe-Seyler's Z. Physiol. Chem. 365:321-334(1984).
CC   -!- FUNCTION: Hemoglobin epsilon chain is a beta-type chain found in early
CC       embryos.
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; X86792; CAA60491.1; -; Genomic_DNA.
DR   PIR; A02421; HEPG.
DR   RefSeq; NP_999612.1; NM_214447.1.
DR   AlphaFoldDB; P02101; -.
DR   SMR; P02101; -.
DR   STRING; 9823.ENSSSCP00000015648; -.
DR   PaxDb; P02101; -.
DR   PeptideAtlas; P02101; -.
DR   GeneID; 407067; -.
DR   KEGG; ssc:407067; -.
DR   CTD; 3046; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   InParanoid; P02101; -.
DR   OrthoDB; 1370439at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Phosphoprotein; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6724525"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit epsilon"
FT                   /id="PRO_0000053222"
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         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02100"
FT   CONFLICT        10
FT                   /note="S -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17..18
FT                   /note="GK -> SR (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="A -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="G -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   147 AA;  16095 MW;  38B1E1D8AE2E6A9E CRC64;
     MVHFTAEEKS VITGLWGKVN VEETGGQAVG RLLVVYPWTQ RFFDSFGNMS SPSAIMGNPK
     VKAHGKKVLT AFGDAVKNMD NLKGTFAKLS ELHCDKLHVD PENFRLLGNM IVIILASHFG
     GEFTPEVQAA WQKLVAGVAT ALAHKYH