Full text data of KDELR1
KDELR1
(ERD2.1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
ER lumen protein retaining receptor 1 (KDEL endoplasmic reticulum protein retention receptor 1; KDEL receptor 1; Putative MAPK-activating protein PM23)
ER lumen protein retaining receptor 1 (KDEL endoplasmic reticulum protein retention receptor 1; KDEL receptor 1; Putative MAPK-activating protein PM23)
UniProt
P24390
ID ERD21_HUMAN Reviewed; 212 AA.
AC P24390; B2R6N4; Q54A39;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-1992, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=ER lumen protein retaining receptor 1;
DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 1;
DE Short=KDEL receptor 1;
DE AltName: Full=Putative MAPK-activating protein PM23;
GN Name=KDELR1; Synonyms=ERD2.1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=2172835; DOI=10.1038/348162a0;
RA Lewis M.J., Pelham H.R.B.;
RT "A human homologue of the yeast HDEL receptor.";
RL Nature 348:162-163(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP MUTAGENESIS.
RX PubMed=8392934;
RA Townsley F.M., Wilson D.W., Pelham H.R.B.;
RT "Mutational analysis of the human KDEL receptor: distinct structural
RT requirements for Golgi retention, ligand binding and retrograde
RT transport.";
RL EMBO J. 12:2821-2829(1993).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11703931; DOI=10.1016/S1534-5807(01)00004-1;
RA Majoul I., Straub M., Hell S.W., Duden R., Soling H.D.;
RT "KDEL-cargo regulates interactions between proteins involved in COPI
RT vesicle traffic: measurements in living cells using FRET.";
RL Dev. Cell 1:139-153(2001).
RN [8]
RP PHOSPHORYLATION AT SER-209, MUTAGENESIS OF SER-209, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14517323; DOI=10.1091/mbc.E03-04-0194;
RA Cabrera M., Muniz M., Hidalgo J., Vega L., Martin M.E., Velasco A.;
RT "The retrieval function of the KDEL receptor requires PKA
RT phosphorylation of its C-terminus.";
RL Mol. Biol. Cell 14:4114-4125(2003).
CC -!- FUNCTION: Required for the retention of luminal endoplasmic
CC reticulum resident proteins via vesicular recycling. This receptor
CC recognizes the C-terminal K-D-E-L motif. COPI-coated transport
CC intermediates, either in the form of round vesicles or as tubular
CC processes, mediate retrograde traffic of the KDEL receptor-ligand
CC complexes. Also required for normal vesicular traffic through the
CC Golgi.
CC -!- SUBUNIT: Upon ligand binding the receptor oligomerizes and
CC interacts with components of the transport machinery such as
CC ARFGAP1 and ARF1.
CC -!- INTERACTION:
CC Q7L1Q6:BZW1; NbExp=1; IntAct=EBI-1043076, EBI-1046727;
CC Q9HC98:NEK6; NbExp=1; IntAct=EBI-1043076, EBI-740364;
CC Q13530:SERINC3; NbExp=1; IntAct=EBI-1043076, EBI-1045571;
CC Q9UHQ7:WBP5; NbExp=1; IntAct=EBI-1043076, EBI-1051372;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle
CC membrane; Multi-pass membrane protein. Endoplasmic reticulum
CC membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane.
CC -!- PTM: Phosphorylation by PKA at Ser-209 is required for endoplasmic
CC reticulum retention function.
CC -!- SIMILARITY: Belongs to the ERD2 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X55885; CAA39371.1; -; mRNA.
DR EMBL; AB097047; BAC77400.1; -; mRNA.
DR EMBL; AK312647; BAG35531.1; -; mRNA.
DR EMBL; CH471177; EAW52340.1; -; Genomic_DNA.
DR EMBL; BC018778; AAH18778.1; -; mRNA.
DR PIR; S13293; S13293.
DR RefSeq; NP_006792.1; NM_006801.2.
DR UniGene; Hs.515515; -.
DR ProteinModelPortal; P24390; -.
DR DIP; DIP-48668N; -.
DR IntAct; P24390; 6.
DR MINT; MINT-3010262; -.
DR STRING; 9606.ENSP00000329471; -.
DR PhosphoSite; P24390; -.
DR DMDM; 119543; -.
DR PaxDb; P24390; -.
DR PRIDE; P24390; -.
DR DNASU; 10945; -.
DR Ensembl; ENST00000330720; ENSP00000329471; ENSG00000105438.
DR GeneID; 10945; -.
DR KEGG; hsa:10945; -.
DR UCSC; uc002pja.1; human.
DR CTD; 10945; -.
DR GeneCards; GC19M048885; -.
DR HGNC; HGNC:6304; KDELR1.
DR HPA; CAB017455; -.
DR MIM; 131235; gene.
DR neXtProt; NX_P24390; -.
DR PharmGKB; PA30083; -.
DR eggNOG; COG5196; -.
DR HOGENOM; HOG000231400; -.
DR HOVERGEN; HBG001398; -.
DR InParanoid; P24390; -.
DR KO; K10949; -.
DR OrthoDB; EOG761BW0; -.
DR PhylomeDB; P24390; -.
DR ChiTaRS; KDELR1; human.
DR GeneWiki; KDELR1; -.
DR GenomeRNAi; 10945; -.
DR NextBio; 41585; -.
DR PRO; PR:P24390; -.
DR ArrayExpress; P24390; -.
DR Bgee; P24390; -.
DR CleanEx; HS_KDELR1; -.
DR Genevestigator; P24390; -.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0005046; F:KDEL sequence binding; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR GO; GO:0006621; P:protein retention in ER lumen; IEA:InterPro.
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 1: Evidence at protein level;
KW Complete proteome; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; Phosphoprotein; Protein transport;
KW Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 212 ER lumen protein retaining receptor 1.
FT /FTId=PRO_0000194153.
FT TOPO_DOM 1 2 Lumenal (Potential).
FT TRANSMEM 3 21 Helical; (Potential).
FT TOPO_DOM 22 35 Cytoplasmic (Potential).
FT TRANSMEM 36 53 Helical; (Potential).
FT TOPO_DOM 54 61 Lumenal (Potential).
FT TRANSMEM 62 80 Helical; (Potential).
FT TOPO_DOM 81 96 Cytoplasmic (Potential).
FT TRANSMEM 97 110 Helical; (Potential).
FT TOPO_DOM 111 117 Lumenal (Potential).
FT TRANSMEM 118 137 Helical; (Potential).
FT TOPO_DOM 138 149 Cytoplasmic (Potential).
FT TRANSMEM 150 168 Helical; (Potential).
FT TOPO_DOM 169 178 Lumenal (Potential).
FT TRANSMEM 179 199 Helical; (Potential).
FT TOPO_DOM 200 212 Cytoplasmic (Potential).
FT MOD_RES 209 209 Phosphoserine; by PKA.
FT MUTAGEN 209 209 S->A: Inhibits coatomer/ARF-GAP
FT recruitment, receptor redistribution, and
FT intracellular retention of KDEL ligands.
FT MUTAGEN 209 209 S->D: Redistribution to the ER is not
FT affected upon PKA inactivation.
SQ SEQUENCE 212 AA; 24542 MW; B863C0F09CFC0551 CRC64;
MNLFRFLGDL SHLLAIILLL LKIWKSRSCA GISGKSQVLF AVVFTARYLD LFTNYISLYN
TCMKVVYIAC SFTTVWLIYS KFKATYDGNH DTFRVEFLVV PTAILAFLVN HDFTPLEILW
TFSIYLESVA ILPQLFMVSK TGEAETITSH YLFALGVYRT LYLFNWIWRY HFEGFFDLIA
IVAGLVQTVL YCDFFYLYIT KVLKGKKLSL PA
//
ID ERD21_HUMAN Reviewed; 212 AA.
AC P24390; B2R6N4; Q54A39;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-1992, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=ER lumen protein retaining receptor 1;
DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 1;
DE Short=KDEL receptor 1;
DE AltName: Full=Putative MAPK-activating protein PM23;
GN Name=KDELR1; Synonyms=ERD2.1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=2172835; DOI=10.1038/348162a0;
RA Lewis M.J., Pelham H.R.B.;
RT "A human homologue of the yeast HDEL receptor.";
RL Nature 348:162-163(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP MUTAGENESIS.
RX PubMed=8392934;
RA Townsley F.M., Wilson D.W., Pelham H.R.B.;
RT "Mutational analysis of the human KDEL receptor: distinct structural
RT requirements for Golgi retention, ligand binding and retrograde
RT transport.";
RL EMBO J. 12:2821-2829(1993).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11703931; DOI=10.1016/S1534-5807(01)00004-1;
RA Majoul I., Straub M., Hell S.W., Duden R., Soling H.D.;
RT "KDEL-cargo regulates interactions between proteins involved in COPI
RT vesicle traffic: measurements in living cells using FRET.";
RL Dev. Cell 1:139-153(2001).
RN [8]
RP PHOSPHORYLATION AT SER-209, MUTAGENESIS OF SER-209, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14517323; DOI=10.1091/mbc.E03-04-0194;
RA Cabrera M., Muniz M., Hidalgo J., Vega L., Martin M.E., Velasco A.;
RT "The retrieval function of the KDEL receptor requires PKA
RT phosphorylation of its C-terminus.";
RL Mol. Biol. Cell 14:4114-4125(2003).
CC -!- FUNCTION: Required for the retention of luminal endoplasmic
CC reticulum resident proteins via vesicular recycling. This receptor
CC recognizes the C-terminal K-D-E-L motif. COPI-coated transport
CC intermediates, either in the form of round vesicles or as tubular
CC processes, mediate retrograde traffic of the KDEL receptor-ligand
CC complexes. Also required for normal vesicular traffic through the
CC Golgi.
CC -!- SUBUNIT: Upon ligand binding the receptor oligomerizes and
CC interacts with components of the transport machinery such as
CC ARFGAP1 and ARF1.
CC -!- INTERACTION:
CC Q7L1Q6:BZW1; NbExp=1; IntAct=EBI-1043076, EBI-1046727;
CC Q9HC98:NEK6; NbExp=1; IntAct=EBI-1043076, EBI-740364;
CC Q13530:SERINC3; NbExp=1; IntAct=EBI-1043076, EBI-1045571;
CC Q9UHQ7:WBP5; NbExp=1; IntAct=EBI-1043076, EBI-1051372;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle
CC membrane; Multi-pass membrane protein. Endoplasmic reticulum
CC membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane.
CC -!- PTM: Phosphorylation by PKA at Ser-209 is required for endoplasmic
CC reticulum retention function.
CC -!- SIMILARITY: Belongs to the ERD2 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X55885; CAA39371.1; -; mRNA.
DR EMBL; AB097047; BAC77400.1; -; mRNA.
DR EMBL; AK312647; BAG35531.1; -; mRNA.
DR EMBL; CH471177; EAW52340.1; -; Genomic_DNA.
DR EMBL; BC018778; AAH18778.1; -; mRNA.
DR PIR; S13293; S13293.
DR RefSeq; NP_006792.1; NM_006801.2.
DR UniGene; Hs.515515; -.
DR ProteinModelPortal; P24390; -.
DR DIP; DIP-48668N; -.
DR IntAct; P24390; 6.
DR MINT; MINT-3010262; -.
DR STRING; 9606.ENSP00000329471; -.
DR PhosphoSite; P24390; -.
DR DMDM; 119543; -.
DR PaxDb; P24390; -.
DR PRIDE; P24390; -.
DR DNASU; 10945; -.
DR Ensembl; ENST00000330720; ENSP00000329471; ENSG00000105438.
DR GeneID; 10945; -.
DR KEGG; hsa:10945; -.
DR UCSC; uc002pja.1; human.
DR CTD; 10945; -.
DR GeneCards; GC19M048885; -.
DR HGNC; HGNC:6304; KDELR1.
DR HPA; CAB017455; -.
DR MIM; 131235; gene.
DR neXtProt; NX_P24390; -.
DR PharmGKB; PA30083; -.
DR eggNOG; COG5196; -.
DR HOGENOM; HOG000231400; -.
DR HOVERGEN; HBG001398; -.
DR InParanoid; P24390; -.
DR KO; K10949; -.
DR OrthoDB; EOG761BW0; -.
DR PhylomeDB; P24390; -.
DR ChiTaRS; KDELR1; human.
DR GeneWiki; KDELR1; -.
DR GenomeRNAi; 10945; -.
DR NextBio; 41585; -.
DR PRO; PR:P24390; -.
DR ArrayExpress; P24390; -.
DR Bgee; P24390; -.
DR CleanEx; HS_KDELR1; -.
DR Genevestigator; P24390; -.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0005046; F:KDEL sequence binding; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR GO; GO:0006621; P:protein retention in ER lumen; IEA:InterPro.
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 1: Evidence at protein level;
KW Complete proteome; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; Phosphoprotein; Protein transport;
KW Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 212 ER lumen protein retaining receptor 1.
FT /FTId=PRO_0000194153.
FT TOPO_DOM 1 2 Lumenal (Potential).
FT TRANSMEM 3 21 Helical; (Potential).
FT TOPO_DOM 22 35 Cytoplasmic (Potential).
FT TRANSMEM 36 53 Helical; (Potential).
FT TOPO_DOM 54 61 Lumenal (Potential).
FT TRANSMEM 62 80 Helical; (Potential).
FT TOPO_DOM 81 96 Cytoplasmic (Potential).
FT TRANSMEM 97 110 Helical; (Potential).
FT TOPO_DOM 111 117 Lumenal (Potential).
FT TRANSMEM 118 137 Helical; (Potential).
FT TOPO_DOM 138 149 Cytoplasmic (Potential).
FT TRANSMEM 150 168 Helical; (Potential).
FT TOPO_DOM 169 178 Lumenal (Potential).
FT TRANSMEM 179 199 Helical; (Potential).
FT TOPO_DOM 200 212 Cytoplasmic (Potential).
FT MOD_RES 209 209 Phosphoserine; by PKA.
FT MUTAGEN 209 209 S->A: Inhibits coatomer/ARF-GAP
FT recruitment, receptor redistribution, and
FT intracellular retention of KDEL ligands.
FT MUTAGEN 209 209 S->D: Redistribution to the ER is not
FT affected upon PKA inactivation.
SQ SEQUENCE 212 AA; 24542 MW; B863C0F09CFC0551 CRC64;
MNLFRFLGDL SHLLAIILLL LKIWKSRSCA GISGKSQVLF AVVFTARYLD LFTNYISLYN
TCMKVVYIAC SFTTVWLIYS KFKATYDGNH DTFRVEFLVV PTAILAFLVN HDFTPLEILW
TFSIYLESVA ILPQLFMVSK TGEAETITSH YLFALGVYRT LYLFNWIWRY HFEGFFDLIA
IVAGLVQTVL YCDFFYLYIT KVLKGKKLSL PA
//
MIM
131235
*RECORD*
*FIELD* NO
131235
*FIELD* TI
*131235 KDEL ENDOPLASMIC RETICULUM PROTEIN RETENTION RECEPTOR 1; KDELR1
;;ERD2, S. CEREVISIAE, HOMOLOG OF; ERD2;;
read moreHDEL RECEPTOR, S. CEREVISIAE, HOMOLOG OF
*FIELD* TX
DESCRIPTION
Resident soluble proteins within the lumen of the endoplasmic reticulum
(ER) are retained there by virtue of a C-terminal tetrapeptide ER
retention signal, commonly lys-asp-glu-leu (KDEL) in mammals. KDELR1
cycles between the Golgi apparatus and the ER, returning proteins
containing the KDEL signal to the ER (Lewis and Pelham, 1992).
CLONING
By PCR of a T-cell cDNA library using degenerate primers based on yeast
ERD2, followed by screening a placenta cDNA library, Lewis and Pelham
(1990) cloned KDELR1. The deduced 212-amino acid protein has 7
hydrophobic regions and shares 50% identity with the yeast receptor.
Following expression in COS cells, epitope tagged KDELR1 concentrated in
the Golgi apparatus and in punctate structures that may have been
transport vesicles or functional intermediates between the ER and Golgi.
GENE FUNCTION
Lewis and Pelham (1992) found that overexpression of human ERD2 improved
the retention of a protein with a weakly recognized variant of the KDEL
retention signal, DDEL. Overexpression of KDEL or DDEL ligands caused
redistribution of ERD2 from the Golgi apparatus to the ER, and mutation
of ERD2 altered the ligand specificity of this redistribution. The
authors concluded that ligand control of receptor movement may limit
retrograde flow and minimize fruitless recycling of secretory proteins.
Hsu et al. (1992) found that about half of KDELR1- or KDELR2
(609024)-transfected COS cells expressed the receptors in a
juxtanuclear, Golgi-like pattern, while the remainder showed a
reticular, ER-like pattern with nuclear envelope staining.
Overexpression of the KDEL receptors led to the ER-like pattern and was
associated with the collapse of the Golgi apparatus into the ER, as seen
in cells treated with brefeldin A. In addition to the loss of the Golgi
apparatus as a distinct organelle, overexpression resulted in
redistribution of the Golgi coat protein, beta-COP (COPB; 600959), to
the cytosol, addition of complex oligosaccharides to resident ER
glycoproteins, and blockage of anterograde traffic. Hsu et al. (1992)
concluded that the KDEL receptors provide signals that regulate
retrograde traffic between the Golgi and the ER.
Townsley et al. (1993) expressed mutant forms of KDELR1 in COS cells and
examined their intracellular locations and ligand-binding capacities.
They found that ligand binding was dependent on charged residues within
the transmembrane domains. Retrograde transport of occupied receptors
was unaffected by most mutations in the cytoplasmic loops, but was
critically dependent upon asp193 in transmembrane domain 7. Retention in
the Golgi apparatus required neither ligand binding nor asp193. Townsley
et al. (1993) concluded that movement of the receptor is controlled by
conformational changes and intermolecular interactions within the
membrane bilayer.
MAPPING
By genomic sequence analysis, Smith et al. (2000) mapped the KDELR1 gene
to chromosome 19q13.3.
ANIMAL MODEL
Hamada et al. (2004) created transgenic mice expressing a
transport-defective human KDEL receptor. The mutant receptor sensitized
cells to ER stress, and mutant mice developed dilated cardiomyopathy.
Ultrastructural analysis revealed expanded sarcoplasmic reticulums and
protein aggregates that obstructed the adjacent transverse tubules of
mutant cardiomyocytes. Mutant cardiomyocytes were sensitive to ER stress
following treatment with an N-glycosylation inhibitor, and they showed a
functional defect in the L-type Ca(2+) current. The authors observed
ubiquitinated protein aggregates, enhanced expression of Chop (126337),
a death-related transcriptional factor expressed upon ER stress, and
apoptosis in the mutant hearts. Hamada et al. (2004) concluded that
impairment of the KDEL receptor disturbed ER quality control, resulting
in accumulation of misfolded proteins in the ER, and that the dilated
cardiomyopathy in transgenic mice was associated with ER stress.
*FIELD* RF
1. Hamada, H.; Suzuki, M.; Yuasa, S.; Mimura, N.; Shinozuka, N.; Takada,
Y.; Suzuki, M.; Nishino, T.; Nakaya, H.; Koseki, H.; Aoe, T.: Dilated
cardiomyopathy caused by aberrant endoplasmic reticulum quality control
in mutant KDEL receptor transgenic mice. Molec. Cell. Biol. 24:
8007-8017, 2004.
2. Hsu, V. W.; Shah, N.; Klausner, R. D.: A brefeldin A-like phenotype
is induced by the overexpression of a human ERD-2-like protein, ELP-1. Cell 69:
625-635, 1992.
3. Lewis, M. J.; Pelham, H. R. B.: A human homologue of the yeast
HDEL receptor. Nature 348: 162-163, 1990.
4. Lewis, M. J.; Pelham, H. R. B.: Ligand-induced redistribution
of a human KDEL receptor from the Golgi complex to the endoplasmic
reticulum. Cell 68: 353-364, 1992.
5. Smith, J. S.; Tachibana, I.; Pohl, U.; Lee, H. K.; Thanarajasingam,
U.; Portier, B. P.; Ueki, K.; Ramaswamy, S.; Billings, S. J.; Mohrenweiser,
H. W.; Louis, D. N.; Jenkins, R. B.: A transcript map of the chromosome
19q-arm glioma tumor suppressor region. Genomics 64: 44-50, 2000.
6. Townsley, F. M.; Wilson, D. W.; Pelham, H. R. B.: Mutational analysis
of the human KDEL receptor: distinct structural requirements for Golgi
retention, ligand binding and retrograde transport. EMBO J. 12:
2821-2829, 1993.
*FIELD* CN
Patricia A. Hartz - updated: 11/5/2004
Patricia A. Hartz - updated: 10/27/2004
Patricia A. Hartz - updated: 9/29/2004
*FIELD* CD
Victor A. McKusick: 1/2/1991
*FIELD* ED
mgross: 11/11/2004
terry: 11/5/2004
terry: 10/27/2004
mgross: 9/29/2004
supermim: 3/16/1992
carol: 2/12/1992
carol: 2/1/1991
carol: 1/2/1991
*RECORD*
*FIELD* NO
131235
*FIELD* TI
*131235 KDEL ENDOPLASMIC RETICULUM PROTEIN RETENTION RECEPTOR 1; KDELR1
;;ERD2, S. CEREVISIAE, HOMOLOG OF; ERD2;;
read moreHDEL RECEPTOR, S. CEREVISIAE, HOMOLOG OF
*FIELD* TX
DESCRIPTION
Resident soluble proteins within the lumen of the endoplasmic reticulum
(ER) are retained there by virtue of a C-terminal tetrapeptide ER
retention signal, commonly lys-asp-glu-leu (KDEL) in mammals. KDELR1
cycles between the Golgi apparatus and the ER, returning proteins
containing the KDEL signal to the ER (Lewis and Pelham, 1992).
CLONING
By PCR of a T-cell cDNA library using degenerate primers based on yeast
ERD2, followed by screening a placenta cDNA library, Lewis and Pelham
(1990) cloned KDELR1. The deduced 212-amino acid protein has 7
hydrophobic regions and shares 50% identity with the yeast receptor.
Following expression in COS cells, epitope tagged KDELR1 concentrated in
the Golgi apparatus and in punctate structures that may have been
transport vesicles or functional intermediates between the ER and Golgi.
GENE FUNCTION
Lewis and Pelham (1992) found that overexpression of human ERD2 improved
the retention of a protein with a weakly recognized variant of the KDEL
retention signal, DDEL. Overexpression of KDEL or DDEL ligands caused
redistribution of ERD2 from the Golgi apparatus to the ER, and mutation
of ERD2 altered the ligand specificity of this redistribution. The
authors concluded that ligand control of receptor movement may limit
retrograde flow and minimize fruitless recycling of secretory proteins.
Hsu et al. (1992) found that about half of KDELR1- or KDELR2
(609024)-transfected COS cells expressed the receptors in a
juxtanuclear, Golgi-like pattern, while the remainder showed a
reticular, ER-like pattern with nuclear envelope staining.
Overexpression of the KDEL receptors led to the ER-like pattern and was
associated with the collapse of the Golgi apparatus into the ER, as seen
in cells treated with brefeldin A. In addition to the loss of the Golgi
apparatus as a distinct organelle, overexpression resulted in
redistribution of the Golgi coat protein, beta-COP (COPB; 600959), to
the cytosol, addition of complex oligosaccharides to resident ER
glycoproteins, and blockage of anterograde traffic. Hsu et al. (1992)
concluded that the KDEL receptors provide signals that regulate
retrograde traffic between the Golgi and the ER.
Townsley et al. (1993) expressed mutant forms of KDELR1 in COS cells and
examined their intracellular locations and ligand-binding capacities.
They found that ligand binding was dependent on charged residues within
the transmembrane domains. Retrograde transport of occupied receptors
was unaffected by most mutations in the cytoplasmic loops, but was
critically dependent upon asp193 in transmembrane domain 7. Retention in
the Golgi apparatus required neither ligand binding nor asp193. Townsley
et al. (1993) concluded that movement of the receptor is controlled by
conformational changes and intermolecular interactions within the
membrane bilayer.
MAPPING
By genomic sequence analysis, Smith et al. (2000) mapped the KDELR1 gene
to chromosome 19q13.3.
ANIMAL MODEL
Hamada et al. (2004) created transgenic mice expressing a
transport-defective human KDEL receptor. The mutant receptor sensitized
cells to ER stress, and mutant mice developed dilated cardiomyopathy.
Ultrastructural analysis revealed expanded sarcoplasmic reticulums and
protein aggregates that obstructed the adjacent transverse tubules of
mutant cardiomyocytes. Mutant cardiomyocytes were sensitive to ER stress
following treatment with an N-glycosylation inhibitor, and they showed a
functional defect in the L-type Ca(2+) current. The authors observed
ubiquitinated protein aggregates, enhanced expression of Chop (126337),
a death-related transcriptional factor expressed upon ER stress, and
apoptosis in the mutant hearts. Hamada et al. (2004) concluded that
impairment of the KDEL receptor disturbed ER quality control, resulting
in accumulation of misfolded proteins in the ER, and that the dilated
cardiomyopathy in transgenic mice was associated with ER stress.
*FIELD* RF
1. Hamada, H.; Suzuki, M.; Yuasa, S.; Mimura, N.; Shinozuka, N.; Takada,
Y.; Suzuki, M.; Nishino, T.; Nakaya, H.; Koseki, H.; Aoe, T.: Dilated
cardiomyopathy caused by aberrant endoplasmic reticulum quality control
in mutant KDEL receptor transgenic mice. Molec. Cell. Biol. 24:
8007-8017, 2004.
2. Hsu, V. W.; Shah, N.; Klausner, R. D.: A brefeldin A-like phenotype
is induced by the overexpression of a human ERD-2-like protein, ELP-1. Cell 69:
625-635, 1992.
3. Lewis, M. J.; Pelham, H. R. B.: A human homologue of the yeast
HDEL receptor. Nature 348: 162-163, 1990.
4. Lewis, M. J.; Pelham, H. R. B.: Ligand-induced redistribution
of a human KDEL receptor from the Golgi complex to the endoplasmic
reticulum. Cell 68: 353-364, 1992.
5. Smith, J. S.; Tachibana, I.; Pohl, U.; Lee, H. K.; Thanarajasingam,
U.; Portier, B. P.; Ueki, K.; Ramaswamy, S.; Billings, S. J.; Mohrenweiser,
H. W.; Louis, D. N.; Jenkins, R. B.: A transcript map of the chromosome
19q-arm glioma tumor suppressor region. Genomics 64: 44-50, 2000.
6. Townsley, F. M.; Wilson, D. W.; Pelham, H. R. B.: Mutational analysis
of the human KDEL receptor: distinct structural requirements for Golgi
retention, ligand binding and retrograde transport. EMBO J. 12:
2821-2829, 1993.
*FIELD* CN
Patricia A. Hartz - updated: 11/5/2004
Patricia A. Hartz - updated: 10/27/2004
Patricia A. Hartz - updated: 9/29/2004
*FIELD* CD
Victor A. McKusick: 1/2/1991
*FIELD* ED
mgross: 11/11/2004
terry: 11/5/2004
terry: 10/27/2004
mgross: 9/29/2004
supermim: 3/16/1992
carol: 2/12/1992
carol: 2/1/1991
carol: 1/2/1991