ERD23_XENLA
ID ERD23_XENLA Reviewed; 214 AA.
AC O42580; Q5D084;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ER lumen protein-retaining receptor 3;
DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 3;
DE Short=KDEL receptor 3;
GN Name=kdelr3; Synonyms=erd2, kdelr;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA de Antoni A., Valle G.;
RT "Xenopus laevis KDEL receptor.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for the C-terminal sequence motif K-D-E-L that is
CC present on endoplasmic reticulum resident proteins and that mediates
CC their recycling from the Golgi back to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:O43731}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O43731}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5ZKX9}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O43731}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5ZKX9}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000250|UniProtKB:O43731}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q5ZKX9}. Note=Localized in the Golgi in
CC the absence of bound proteins with the sequence motif K-D-E-L.
CC Trafficks back to the endoplasmic reticulum together with cargo
CC proteins containing the sequence motif K-D-E-L.
CC {ECO:0000250|UniProtKB:O43731}.
CC -!- DOMAIN: Binds the C-terminal sequence motif K-D-E-L in a hydrophilic
CC cavity between the transmembrane domains. This triggers a conformation
CC change that exposes a Lys-rich patch on the cytosolic surface of the
CC protein (By similarity). This patch mediates recycling from the Golgi
CC to the endoplasmic reticulum, probably via COPI vesicles (By
CC similarity). {ECO:0000250|UniProtKB:P24390,
CC ECO:0000250|UniProtKB:Q5ZKX9}.
CC -!- SIMILARITY: Belongs to the ERD2 family. {ECO:0000305}.
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DR EMBL; AJ001533; CAA04817.1; -; mRNA.
DR EMBL; BC054181; AAH54181.1; -; mRNA.
DR RefSeq; NP_001079763.1; NM_001086294.1.
DR AlphaFoldDB; O42580; -.
DR SMR; O42580; -.
DR DNASU; 379453; -.
DR GeneID; 379453; -.
DR KEGG; xla:379453; -.
DR CTD; 379453; -.
DR Xenbase; XB-GENE-865837; kdelr3.L.
DR OMA; LMKIWRS; -.
DR OrthoDB; 1186269at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 379453; Expressed in egg cell and 19 other tissues.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005046; F:KDEL sequence binding; ISS:UniProtKB.
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:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Protein transport; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..214
FT /note="ER lumen protein-retaining receptor 3"
FT /id="PRO_0000194160"
FT TOPO_DOM 1..4
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..24
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 25..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 53..58
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 80..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..110
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 111..116
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 117..135
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 136..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 150..168
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 169..178
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT TOPO_DOM 200..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 47..48
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT REGION 159..169
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT REGION 204..207
FT /note="Important for recycling of cargo proteins with the
FT sequence motif K-D-E-L from the Golgi to the endoplasmic
FT reticulum"
FT /evidence="ECO:0000250|UniProtKB:P33947"
FT SITE 5
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT SITE 117
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q5ZKX9"
FT SITE 193
FT /note="Important for recycling of cargo proteins with the
FT sequence motif K-D-E-L from the Golgi to the endoplasmic
FT reticulum"
FT /evidence="ECO:0000250|UniProtKB:P24390"
SQ SEQUENCE 214 AA; 25010 MW; 4E43E467D2B3C6ED CRC64;
MNIFRILGDV SHLLAIIILL LKMWKSKSCA GISGKSQLLF ALVFTTRYLD LFTVFISPYN
TVMKIIFLAC AYVTVYLIYG KLRKSYDSEN DTFRLEFLLV PVIGLSFLEN YEFTPLEILW
TFSIYLESVA ILPQLFMISK TGEAESITTH YLFFLGLYRV LYLANWIWRY HTEKFYDQIA
VVSGVVQTIF YFDFFYLYVT KVLKGKKLSL PMPV
