ERD23_HUMAN
ID ERD23_HUMAN Reviewed; 214 AA.
AC O43731; A8K7T7; B8ZZ26; O95557; Q4V750; Q4V767; Q53FP4; Q53GK1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 183.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Synovial cell;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 MRNA] (ISOFORM 1), AND VARIANT GLY-199.
RC TISSUE=Kidney, and Stomach;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-199.
RC TISSUE=Cervix;
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18086916; DOI=10.1083/jcb.200705180;
RA Raykhel I., Alanen H., Salo K., Jurvansuu J., Nguyen V.D., Latva-Ranta M.,
RA Ruddock L.;
RT "A molecular specificity code for the three mammalian KDEL receptors.";
RL J. Cell Biol. 179:1193-1204(2007).
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:0000269|PubMed:18086916}.
CC -!- INTERACTION:
CC O43731-2; O60636: TSPAN2; NbExp=3; IntAct=EBI-18157502, EBI-3914288;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18086916}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5ZKX9}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:18086916}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5ZKX9}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000269|PubMed:18086916}; 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:0000305|PubMed:18086916}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43731-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43731-2; Sequence=VSP_022856;
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; AL035081; CAA22673.1; -; mRNA.
DR EMBL; AL035082; CAA22674.1; -; mRNA.
DR EMBL; CR456509; CAG30395.1; -; mRNA.
DR EMBL; AK292102; BAF84791.1; -; mRNA.
DR EMBL; AK222930; BAD96650.1; -; mRNA.
DR EMBL; AK223238; BAD96958.1; -; mRNA.
DR EMBL; Z97056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60237.1; -; Genomic_DNA.
DR EMBL; BC001277; AAH01277.1; -; mRNA.
DR EMBL; BC096722; AAH96722.1; -; mRNA.
DR EMBL; BC098131; AAH98131.1; -; mRNA.
DR EMBL; BC098156; AAH98156.1; -; mRNA.
DR EMBL; BC098336; AAH98336.1; -; mRNA.
DR CCDS; CCDS13972.1; -. [O43731-1]
DR CCDS; CCDS46705.1; -. [O43731-2]
DR RefSeq; NP_006846.1; NM_006855.3. [O43731-1]
DR RefSeq; NP_057839.1; NM_016657.2. [O43731-2]
DR AlphaFoldDB; O43731; -.
DR SMR; O43731; -.
DR BioGRID; 116205; 51.
DR IntAct; O43731; 18.
DR MINT; O43731; -.
DR STRING; 9606.ENSP00000386918; -.
DR iPTMnet; O43731; -.
DR PhosphoSitePlus; O43731; -.
DR BioMuta; KDELR3; -.
DR EPD; O43731; -.
DR jPOST; O43731; -.
DR MassIVE; O43731; -.
DR MaxQB; O43731; -.
DR PaxDb; O43731; -.
DR PeptideAtlas; O43731; -.
DR PRIDE; O43731; -.
DR ProteomicsDB; 49134; -. [O43731-1]
DR ProteomicsDB; 49135; -. [O43731-2]
DR Antibodypedia; 26349; 104 antibodies from 23 providers.
DR DNASU; 11015; -.
DR Ensembl; ENST00000216014.9; ENSP00000216014.4; ENSG00000100196.11. [O43731-1]
DR Ensembl; ENST00000409006.3; ENSP00000386918.3; ENSG00000100196.11. [O43731-2]
DR GeneID; 11015; -.
DR KEGG; hsa:11015; -.
DR MANE-Select; ENST00000216014.9; ENSP00000216014.4; NM_006855.4; NP_006846.1.
DR UCSC; uc003avu.5; human. [O43731-1]
DR CTD; 11015; -.
DR DisGeNET; 11015; -.
DR GeneCards; KDELR3; -.
DR HGNC; HGNC:6306; KDELR3.
DR HPA; ENSG00000100196; Low tissue specificity.
DR neXtProt; NX_O43731; -.
DR OpenTargets; ENSG00000100196; -.
DR PharmGKB; PA30085; -.
DR VEuPathDB; HostDB:ENSG00000100196; -.
DR eggNOG; KOG3106; Eukaryota.
DR GeneTree; ENSGT00390000004010; -.
DR HOGENOM; CLU_057784_0_0_1; -.
DR InParanoid; O43731; -.
DR OMA; LMKIWRS; -.
DR OrthoDB; 1186269at2759; -.
DR PhylomeDB; O43731; -.
DR TreeFam; TF314792; -.
DR PathwayCommons; O43731; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; O43731; -.
DR BioGRID-ORCS; 11015; 20 hits in 1075 CRISPR screens.
DR ChiTaRS; KDELR3; human.
DR GeneWiki; KDELR3; -.
DR GenomeRNAi; 11015; -.
DR Pharos; O43731; Tdark.
DR PRO; PR:O43731; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O43731; protein.
DR Bgee; ENSG00000100196; Expressed in tibia and 166 other tissues.
DR ExpressionAtlas; O43731; baseline and differential.
DR Genevisible; O43731; HS.
DR GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0046923; F:ER retention sequence binding; IBA:GO_Central.
DR GO; GO:0005046; F:KDEL sequence binding; IDA: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; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Membrane; Protein transport; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..214
FT /note="ER lumen protein-retaining receptor 3"
FT /id="PRO_0000194158"
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: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 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 VAR_SEQ 202..214
FT /note="VLKGKKLSLPMPI -> GRSWDDSNADTGLRSYSSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12529303,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022856"
FT VARIANT 199
FT /note="V -> G (in dbSNP:rs12004)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_014506"
FT CONFLICT 42
FT /note="L -> P (in Ref. 4; BAD96650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 25027 MW; ED5F7D303390B314 CRC64;
MNVFRILGDL SHLLAMILLL GKIWRSKCCK GISGKSQILF ALVFTTRYLD LFTNFISIYN
TVMKVVFLLC AYVTVYMIYG KFRKTFDSEN DTFRLEFLLV PVIGLSFLEN YSFTLLEILW
TFSIYLESVA ILPQLFMISK TGEAETITTH YLFFLGLYRA LYLANWIRRY QTENFYDQIA
VVSGVVQTIF YCDFFYLYVT KVLKGKKLSL PMPI
