ERD21_RAT
ID ERD21_RAT Reviewed; 212 AA.
AC Q569A6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ER lumen protein-retaining receptor 1;
DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 1;
DE Short=KDEL receptor 1;
GN Name=Kdelr1;
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=Lung;
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: 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:P24390}.
CC -!- SUBUNIT: Upon ligand binding the receptor oligomerizes and interacts
CC with components of the transport machinery such as ARFGAP1 and ARF1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P33946}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P33946}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P33946}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:P33946};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P33946}.
CC Note=Localized in the Golgi in the absence of bound proteins with the
CC sequence motif K-D-E-L. Trafficks back to the endoplasmic reticulum
CC together with cargo proteins containing the sequence motif K-D-E-L.
CC {ECO:0000250|UniProtKB:P33946}.
CC -!- PTM: Phosphorylation by PKA at Ser-209 is required for endoplasmic
CC reticulum retention function. {ECO:0000250|UniProtKB:P24390}.
CC -!- SIMILARITY: Belongs to the ERD2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC092600; AAH92600.1; -; mRNA.
DR RefSeq; NP_001017385.1; NM_001017385.1.
DR AlphaFoldDB; Q569A6; -.
DR SMR; Q569A6; -.
DR IntAct; Q569A6; 1.
DR STRING; 10116.ENSRNOP00000028627; -.
DR jPOST; Q569A6; -.
DR PaxDb; Q569A6; -.
DR PRIDE; Q569A6; -.
DR Ensembl; ENSRNOT00000028627; ENSRNOP00000028627; ENSRNOG00000021082.
DR GeneID; 361577; -.
DR KEGG; rno:361577; -.
DR UCSC; RGD:1306764; rat.
DR CTD; 10945; -.
DR RGD; 1306764; Kdelr1.
DR eggNOG; KOG3106; Eukaryota.
DR GeneTree; ENSGT00390000004010; -.
DR HOGENOM; CLU_057784_0_0_1; -.
DR InParanoid; Q569A6; -.
DR OMA; APFELLW; -.
DR OrthoDB; 1186269at2759; -.
DR PhylomeDB; Q569A6; -.
DR TreeFam; TF314792; -.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q569A6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021082; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q569A6; 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; ISO:RGD.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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 GO; GO:0070231; P:T cell apoptotic process; ISO:RGD.
DR GO; GO:0030217; P:T cell differentiation; ISO:RGD.
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; Phosphoprotein; Protein transport; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..212
FT /note="ER lumen protein-retaining receptor 1"
FT /id="PRO_0000252343"
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: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"
FT MOD_RES 209
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P24390"
SQ SEQUENCE 212 AA; 24546 MW; CBA4498155CCCA79 CRC64;
MNLFRFLGDL SHLLAIILLL LKIWKSRSCA GISGKSQVLF AVVFTARYLD LFTNYISLYN
TCMKVVYIAC SFTTVWMIYS KFKATYDGNH DTFRVEFLVV PTAVLAFLVN HDFTPLEILW
TFSIYLESVA ILPQLFMVSK TGEAETITSH YLFALGVYRT LYLFNWIWRY HFEGFFDLIA
IVAGLVQTVL YCDFFYLYIT KVLKGKKLSL PA
