ERD22_RAT
ID ERD22_RAT Reviewed; 212 AA.
AC Q5U305;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ER lumen protein-retaining receptor 2;
DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 2;
DE Short=KDEL receptor 2;
GN Name=Kdelr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Membrane receptor that binds the K-D-E-L sequence motif in
CC the C-terminal part of endoplasmic reticulum resident proteins and
CC maintains their localization in that compartment by participating to
CC their vesicle-mediated recycling back from the Golgi (By similarity).
CC Binding is pH dependent, and is optimal at pH 5-5.4 (By similarity).
CC {ECO:0000250|UniProtKB:P33947, ECO:0000250|UniProtKB:Q5ZKX9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5ZKX9}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5ZKX9}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000250|UniProtKB:P33947}; 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:P33947}.
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; BC085786; AAH85786.1; -; mRNA.
DR RefSeq; NP_001013140.1; NM_001013122.1.
DR AlphaFoldDB; Q5U305; -.
DR SMR; Q5U305; -.
DR STRING; 10116.ENSRNOP00000001438; -.
DR jPOST; Q5U305; -.
DR PaxDb; Q5U305; -.
DR GeneID; 304290; -.
DR KEGG; rno:304290; -.
DR CTD; 11014; -.
DR RGD; 1304618; Kdelr2.
DR VEuPathDB; HostDB:ENSRNOG00000001083; -.
DR eggNOG; KOG3106; Eukaryota.
DR HOGENOM; CLU_057784_0_0_1; -.
DR InParanoid; Q5U305; -.
DR OMA; AYTVYLM; -.
DR OrthoDB; 1186269at2759; -.
DR PhylomeDB; Q5U305; -.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q5U305; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001083; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q5U305; RN.
DR GO; GO:0005801; C:cis-Golgi network; IDA:MGI.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0046923; F:ER retention sequence binding; IBA:GO_Central.
DR GO; GO:0005046; F:KDEL sequence binding; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0006621; P:protein retention in ER lumen; IBA:GO_Central.
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..212
FT /note="ER lumen protein-retaining receptor 2"
FT /id="PRO_0000194157"
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..212
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:P24390"
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 54
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 212 AA; 24454 MW; 774388DAF56FEC24 CRC64;
MNIFRLTGDL SHLAAIVILL LKIWKTRSCA GISGKSQLLF ALVFTTRYLD LFTSFISLYN
TSMKLIYIAC SYATVYLIYM KFKATYDGNH DTFRVEFLVV PVGGLSFLVN HDFSPLEILW
TFSIYLESVA ILPQLFMISK TGEAETITTH YLFFLGLYRA LYLVNWIWRF YFEGFFDLIA
VVAGVVQTIL YCDFFYLYIT KVLKGKKLSL PA
