ERD2_KLULA
ID ERD2_KLULA Reviewed; 219 AA.
AC P18413;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=ER lumen protein-retaining receptor;
GN Name=ERD2; OrderedLocusNames=KLLA0E05566g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2194671; DOI=10.1016/0092-8674(90)90699-f;
RA Lewis M.J., Sweet D.J., Pelham H.R.B.;
RT "The ERD2 gene determines the specificity of the luminal ER protein
RT retention system.";
RL Cell 61:1359-1363(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [3]
RP RESIDUE IMPORTANT FOR SPECIFICITY.
RX PubMed=1312604; DOI=10.1016/0022-2836(92)90571-z;
RA Semenza J.C., Pelham H.R.B.;
RT "Changing the specificity of the sorting receptor for luminal endoplasmic
RT reticulum proteins.";
RL J. Mol. Biol. 224:1-5(1992).
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. This receptor recognizes H-D-E-L and D-D-E-L, but not K-D-E-
CC L.
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; M34844; AAA35253.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99286.1; -; Genomic_DNA.
DR PIR; A35618; A35618.
DR RefSeq; XP_454199.1; XM_454199.1.
DR AlphaFoldDB; P18413; -.
DR SMR; P18413; -.
DR STRING; 28985.XP_454199.1; -.
DR EnsemblFungi; CAG99286; CAG99286; KLLA0_E05611g.
DR GeneID; 2894129; -.
DR KEGG; kla:KLLA0_E05611g; -.
DR eggNOG; KOG3106; Eukaryota.
DR HOGENOM; CLU_057784_0_0_1; -.
DR InParanoid; P18413; -.
DR OMA; AYTVYLM; -.
DR Proteomes; UP000000598; Chromosome E.
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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..219
FT /note="ER lumen protein-retaining receptor"
FT /id="PRO_0000194169"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..62
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..123
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..184
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 51
FT /note="Important for specificity of recognition"
SQ SEQUENCE 219 AA; 25851 MW; E73149E12C933F4B CRC64;
MLNVFRIAGD FSHLASIIIL IQSITTSNSV DGISLKTQLL YTLVFITRYL NLFTKWTSLY
NFLMKIVFIS SSVYVIVLMR QQKFKNPVAY QDMITRDQFK IKFLIVPCIL LGLIFNYRFS
FIQICWSFSL WLESVAILPQ LFMLTKTGKA KQLTSHYIFA LGLYRALYIP NWIWRYYTEE
RFDKLSVFTG VIQTLVYSDF FYIYYQKVIK LGGDLELPQ
