ERD21_HUMAN
ID ERD21_HUMAN Reviewed; 212 AA.
AC P24390; B2R6N4; Q54A39; Q8NBW7;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 179.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
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] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., 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] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-32; 91-ASP-THR-92
RP AND ASP-193.
RX PubMed=8392934; DOI=10.1002/j.1460-2075.1993.tb05943.x;
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 [8]
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 [9]
RP FUNCTION, PHOSPHORYLATION AT SER-209, MUTAGENESIS OF SER-209, AND
RP SUBCELLULAR 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 phosphorylation
RT of its C-terminus.";
RL Mol. Biol. Cell 14:4114-4125(2003).
RN [10]
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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-12; ARG-47; GLU-127;
RP TYR-158; ASP-193 AND 204-LYS--LYS-207.
RX PubMed=30846601; DOI=10.1126/science.aaw2859;
RA Braeuer P., Parker J.L., Gerondopoulos A., Zimmermann I., Seeger M.A.,
RA Barr F.A., Newstead S.;
RT "Structural basis for pH-dependent retrieval of ER proteins from the Golgi
RT by the KDEL receptor.";
RL Science 363:1103-1107(2019).
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:11703931, ECO:0000269|PubMed:14517323,
CC ECO:0000269|PubMed:18086916, ECO:0000269|PubMed:30846601,
CC ECO:0000269|PubMed:8392934}.
CC -!- SUBUNIT: Upon ligand binding the receptor oligomerizes and interacts
CC with components of the transport machinery such as ARFGAP1 and ARF1.
CC {ECO:0000269|PubMed:11703931}.
CC -!- INTERACTION:
CC P24390; Q15700: DLG2; NbExp=3; IntAct=EBI-1043076, EBI-80426;
CC P24390; Q92796: DLG3; NbExp=3; IntAct=EBI-1043076, EBI-80440;
CC P24390; O76011: KRT34; NbExp=3; IntAct=EBI-1043076, EBI-1047093;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18086916, ECO:0000269|PubMed:2172835,
CC ECO:0000269|PubMed:30846601, ECO:0000269|PubMed:8392934}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P33946}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000269|PubMed:18086916}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P33946}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:18086916, ECO:0000269|PubMed:30846601,
CC ECO:0000269|PubMed:8392934}; 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:0000269|PubMed:18086916, ECO:0000269|PubMed:30846601,
CC ECO:0000269|PubMed:8392934}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P24390-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P24390-2; Sequence=VSP_055484;
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
CC (PubMed:30846601). {ECO:0000250|UniProtKB:Q5ZKX9,
CC ECO:0000269|PubMed:30846601}.
CC -!- PTM: Phosphorylation by PKA at Ser-209 is required for endoplasmic
CC reticulum retention function. {ECO:0000269|PubMed:14517323}.
CC -!- SIMILARITY: Belongs to the ERD2 family. {ECO:0000305}.
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DR EMBL; X55885; CAA39371.1; -; mRNA.
DR EMBL; AB097047; BAC77400.1; -; mRNA.
DR EMBL; AK075185; BAC11457.1; -; mRNA.
DR EMBL; AK312647; BAG35531.1; -; mRNA.
DR EMBL; AC011514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52340.1; -; Genomic_DNA.
DR EMBL; CH471177; EAW52343.1; -; Genomic_DNA.
DR EMBL; CH471177; EAW52345.1; -; Genomic_DNA.
DR EMBL; BC018778; AAH18778.1; -; mRNA.
DR CCDS; CCDS12718.1; -. [P24390-1]
DR PIR; S13293; S13293.
DR RefSeq; NP_006792.1; NM_006801.2. [P24390-1]
DR AlphaFoldDB; P24390; -.
DR SMR; P24390; -.
DR BioGRID; 116145; 108.
DR DIP; DIP-48668N; -.
DR IntAct; P24390; 38.
DR MINT; P24390; -.
DR STRING; 9606.ENSP00000329471; -.
DR TCDB; 9.B.191.1.5; the endoplasmic reticulum retention receptor (kdelr) family.
DR iPTMnet; P24390; -.
DR PhosphoSitePlus; P24390; -.
DR SwissPalm; P24390; -.
DR BioMuta; KDELR1; -.
DR DMDM; 119543; -.
DR EPD; P24390; -.
DR jPOST; P24390; -.
DR MassIVE; P24390; -.
DR MaxQB; P24390; -.
DR PaxDb; P24390; -.
DR PeptideAtlas; P24390; -.
DR PRIDE; P24390; -.
DR ProteomicsDB; 54202; -. [P24390-1]
DR TopDownProteomics; P24390-1; -. [P24390-1]
DR ABCD; P24390; 1 sequenced antibody.
DR Antibodypedia; 3381; 208 antibodies from 27 providers.
DR DNASU; 10945; -.
DR Ensembl; ENST00000330720.7; ENSP00000329471.2; ENSG00000105438.9. [P24390-1]
DR Ensembl; ENST00000597017.5; ENSP00000470841.1; ENSG00000105438.9. [P24390-2]
DR GeneID; 10945; -.
DR KEGG; hsa:10945; -.
DR MANE-Select; ENST00000330720.7; ENSP00000329471.2; NM_006801.3; NP_006792.1.
DR UCSC; uc002pja.2; human. [P24390-1]
DR CTD; 10945; -.
DR DisGeNET; 10945; -.
DR GeneCards; KDELR1; -.
DR HGNC; HGNC:6304; KDELR1.
DR HPA; ENSG00000105438; Low tissue specificity.
DR MIM; 131235; gene.
DR neXtProt; NX_P24390; -.
DR OpenTargets; ENSG00000105438; -.
DR PharmGKB; PA30083; -.
DR VEuPathDB; HostDB:ENSG00000105438; -.
DR eggNOG; KOG3106; Eukaryota.
DR GeneTree; ENSGT00390000004010; -.
DR HOGENOM; CLU_057784_0_0_1; -.
DR InParanoid; P24390; -.
DR OMA; APFELLW; -.
DR OrthoDB; 1186269at2759; -.
DR PhylomeDB; P24390; -.
DR TreeFam; TF314792; -.
DR PathwayCommons; P24390; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; P24390; -.
DR SIGNOR; P24390; -.
DR BioGRID-ORCS; 10945; 23 hits in 1076 CRISPR screens.
DR ChiTaRS; KDELR1; human.
DR GeneWiki; KDELR1; -.
DR GenomeRNAi; 10945; -.
DR Pharos; P24390; Tbio.
DR PRO; PR:P24390; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P24390; protein.
DR Bgee; ENSG00000105438; Expressed in parotid gland and 182 other tissues.
DR ExpressionAtlas; P24390; baseline and differential.
DR Genevisible; P24390; 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; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
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 GO; GO:0070231; P:T cell apoptotic process; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
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; Phosphoprotein;
KW Protein transport; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..212
FT /note="ER lumen protein-retaining receptor 1"
FT /id="PRO_0000194153"
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:0000269|PubMed:30846601"
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:0000269|PubMed:30846601,
FT ECO:0000269|PubMed:8392934"
FT MOD_RES 209
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:14517323"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055484"
FT MUTAGEN 12
FT /note="H->A: Loss of recycling together with cargo proteins
FT containing the sequence motif K-D-E-L from the Golgi to the
FT endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:30846601"
FT MUTAGEN 32
FT /note="I->A: Decreased binding to the sequence motif K-D-E-
FT L."
FT /evidence="ECO:0000269|PubMed:8392934"
FT MUTAGEN 47
FT /note="R->K: Loss of recycling together with cargo proteins
FT containing the sequence motif K-D-E-L from the Golgi to the
FT endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:30846601"
FT MUTAGEN 91..92
FT /note="DT->AA: Decreased binding to the sequence motif K-D-
FT E-L."
FT /evidence="ECO:0000269|PubMed:8392934"
FT MUTAGEN 127
FT /note="E->A,Q: Loss of recycling together with cargo
FT proteins containing the sequence motif K-D-E-L from the
FT Golgi to the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:30846601"
FT MUTAGEN 158
FT /note="Y->F: Loss of recycling together with cargo proteins
FT containing the sequence motif K-D-E-L from the Golgi to the
FT endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:30846601"
FT MUTAGEN 193
FT /note="D->N: Loss of recycling together with cargo proteins
FT containing the sequence motif K-D-E-L from the Golgi to the
FT endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:30846601,
FT ECO:0000269|PubMed:8392934"
FT MUTAGEN 204..207
FT /note="KGKK->AGAA: Loss of recycling together with cargo
FT proteins containing the sequence motif K-D-E-L from the
FT Golgi to the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:30846601"
FT MUTAGEN 209
FT /note="S->A: Inhibits coatomer/ARF-GAP recruitment,
FT receptor redistribution, and intracellular retention of
FT KDEL ligands."
FT /evidence="ECO:0000269|PubMed:14517323"
FT MUTAGEN 209
FT /note="S->D: Redistribution to the ER is not affected upon
FT PKA inactivation."
FT /evidence="ECO:0000269|PubMed:14517323"
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
