ERD21_MOUSE
ID ERD21_MOUSE Reviewed; 212 AA.
AC Q99JH8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ER lumen protein-retaining receptor 1;
DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 1;
DE Short=KDEL receptor 1 {ECO:0000303|Ref.1};
GN Name=Kdelr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Yamamoto K., Fujii R., Toyofuku Y., Koseki H., Aoe T.;
RT "Cloning, expression and genomic structure of the murine KDEL receptor 1.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Ievolella C., Negrisolo E., Lanfranchi G., Valle G.;
RT "Full-length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
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DR EMBL; AY027435; AAK11732.1; -; mRNA.
DR EMBL; AJ278132; CAC34584.1; -; mRNA.
DR EMBL; BC011370; AAH11370.1; -; mRNA.
DR CCDS; CCDS21268.1; -.
DR RefSeq; NP_598711.1; NM_133950.2.
DR AlphaFoldDB; Q99JH8; -.
DR SMR; Q99JH8; -.
DR BioGRID; 212676; 4.
DR STRING; 10090.ENSMUSP00000002855; -.
DR PhosphoSitePlus; Q99JH8; -.
DR EPD; Q99JH8; -.
DR jPOST; Q99JH8; -.
DR MaxQB; Q99JH8; -.
DR PaxDb; Q99JH8; -.
DR PeptideAtlas; Q99JH8; -.
DR PRIDE; Q99JH8; -.
DR ProteomicsDB; 275533; -.
DR TopDownProteomics; Q99JH8; -.
DR ABCD; Q99JH8; 1 sequenced antibody.
DR Antibodypedia; 3381; 208 antibodies from 27 providers.
DR DNASU; 68137; -.
DR Ensembl; ENSMUST00000002855; ENSMUSP00000002855; ENSMUSG00000002778.
DR GeneID; 68137; -.
DR KEGG; mmu:68137; -.
DR UCSC; uc009gxn.1; mouse.
DR CTD; 10945; -.
DR MGI; MGI:1915387; Kdelr1.
DR VEuPathDB; HostDB:ENSMUSG00000002778; -.
DR eggNOG; KOG3106; Eukaryota.
DR GeneTree; ENSGT00390000004010; -.
DR HOGENOM; CLU_057784_0_0_1; -.
DR InParanoid; Q99JH8; -.
DR OMA; APFELLW; -.
DR OrthoDB; 1186269at2759; -.
DR PhylomeDB; Q99JH8; -.
DR TreeFam; TF314792; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 68137; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Kdelr1; mouse.
DR PRO; PR:Q99JH8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99JH8; protein.
DR Bgee; ENSMUSG00000002778; Expressed in ileal epithelium and 263 other tissues.
DR ExpressionAtlas; Q99JH8; baseline and differential.
DR Genevisible; Q99JH8; MM.
DR GO; GO:0005801; C:cis-Golgi network; IDA:MGI.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
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; IMP:MGI.
DR GO; GO:0030217; P:T cell differentiation; IMP:MGI.
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 1: Evidence at protein 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_0000194154"
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; 24560 MW; 261285F09CFD4051 CRC64;
MNLFRFLGDL SHLLAIILLL LKIWKSRSCA GISGKSQVLF AVVFTARYLD LFTNYISLYN
TCMKVVYIAC SFTTVWMIYS KFKATYDGNH DTFRVEFLVV PTAILAFLVN HDFTPLEILW
TFSIYLESVA ILPQLFMVSK TGEAETITSH YLFALGVYRT LYLFNWIWRY HFEGFFDLIA
IVAGLVQTVL YCDFFYLYIT KVLKGKKLSL PA
