ID   ERD2_ENTHI              Reviewed;         215 AA.
AC   O44017; Q7K9G5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=ER lumen protein-retaining receptor;
GN   Name=ERD2;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HK-9;
RX   PubMed=9657339; DOI=10.1016/s0166-6851(98)00017-6;
RA   Sanchez-Lopez R., Gama-Castro S., Ramos M.A., Merino E., Lizardi P.M.,
RA   Alagon A.;
RT   "Cloning and expression of the Entamoeba histolytica ERD2 gene.";
RL   Mol. Biochem. Parasitol. 92:355-359(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11545438; DOI=10.1078/1434-4610-00053;
RA   Willhoeft U., Campos-Gongora E., Touzni S., Bruchhaus I., Tannich E.;
RT   "Introns of Entamoeba histolytica and Entamoeba dispar.";
RL   Protist 152:149-156(2001).
CC   -!- FUNCTION: Required for the retention of luminal endoplasmic reticulum
CC       proteins. Determines the specificity of the luminal ER protein
CC       retention system. Also required for normal vesicular traffic through
CC       the Golgi (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ERD2 family. {ECO:0000305}.
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DR   EMBL; AJ002138; CAA05206.1; -; Genomic_DNA.
DR   EMBL; AJ311623; CAC34303.1; -; Genomic_DNA.
DR   AlphaFoldDB; O44017; -.
DR   SMR; O44017; -.
DR   STRING; 5759.rna_EHI_170470-1; -.
DR   VEuPathDB; AmoebaDB:EHI5A_023770; -.
DR   VEuPathDB; AmoebaDB:EHI7A_011190; -.
DR   VEuPathDB; AmoebaDB:EHI8A_008740; -.
DR   VEuPathDB; AmoebaDB:EHI_170470; -.
DR   VEuPathDB; AmoebaDB:KM1_026690; -.
DR   eggNOG; KOG3106; Eukaryota.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046923; F:ER retention sequence binding; IEA:InterPro.
DR   GO; GO:0006621; P:protein retention in ER lumen; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000133; ER_ret_rcpt.
DR   PANTHER; PTHR10585; PTHR10585; 1.
DR   Pfam; PF00810; ER_lumen_recept; 1.
DR   PRINTS; PR00660; ERLUMENR.
DR   PROSITE; PS00951; ER_LUMEN_RECEPTOR_1; 1.
DR   PROSITE; PS00952; ER_LUMEN_RECEPTOR_2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; ER-Golgi transport; Membrane; Protein transport;
KW   Receptor; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..215
FT                   /note="ER lumen protein-retaining receptor"
FT                   /id="PRO_0000194164"
FT   TOPO_DOM        1..4
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..63
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..119
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..181
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        203..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   215 AA;  25724 MW;  92CC39788711AB66 CRC64;
     MVFNLFRISA DLVHLLSIYF LLTKIISHKN CIGISLRSQI LFFIVWVTRY LDIFYNFYSL
     YNTILKIVYL TTSAYTIYLI SKRFRATYDK IHDTLNVWYL IVPCIVLAFI FTEDYSITEI
     CWTFSIFLEA VAILPQILLL RSTGEVENLN SQYIFCLGLY RALYIINWIY RYATEQSYWS
     PLTWICGSIQ TLLYVEYFYY YIKSRVEGTK FVLPY