ERD22_CHICK
ID ERD22_CHICK Reviewed; 212 AA.
AC Q5ZKX9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=ER lumen protein-retaining receptor 2;
DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 2;
DE Short=KDEL receptor 2;
GN Name=KDELR2; ORFNames=RCJMB04_8l23;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-207 IN COMPLEX WITH KDEL
RP PEPTIDE, FUNCTION, TOPOLOGY, AND MUTAGENESIS OF HIS-12; ARG-47; GLU-127 AND
RP TYR-158.
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: Membrane receptor that binds the K-D-E-L sequence motif in
CC the C-terminal part of endoplasmic reticulum resident proteins and
CC maintains their localization in that compartment by participating to
CC their vesicle-mediated recycling back from the Golgi (By similarity).
CC Binding is pH dependent, and is optimal at pH 5-5.4 (PubMed:30846601).
CC {ECO:0000250|UniProtKB:P33947, ECO:0000269|PubMed:30846601}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30846601}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30846601}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30846601}. Note=Localized in the Golgi in the
CC absence of bound proteins with the sequence motif K-D-E-L. Trafficks
CC back to the endoplasmic reticulum together with cargo proteins
CC containing the sequence motif K-D-E-L. {ECO:0000250|UniProtKB:P33947}.
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 (PubMed:30846601). This patch mediates recycling from the Golgi
CC to the endoplasmic reticulum, probably via COPI vesicles (By
CC similarity). {ECO:0000250|UniProtKB:P33947,
CC ECO:0000269|PubMed:30846601}.
CC -!- SIMILARITY: Belongs to the ERD2 family. {ECO:0000305}.
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DR EMBL; AJ719955; CAG31614.1; -; mRNA.
DR RefSeq; NP_001153187.1; NM_001159715.1.
DR PDB; 6I6B; X-ray; 2.59 A; A=1-203.
DR PDB; 6I6H; X-ray; 2.00 A; A=1-207.
DR PDB; 6I6J; X-ray; 2.23 A; A=1-204.
DR PDB; 6Y7V; X-ray; 2.24 A; A=1-212.
DR PDB; 6ZXR; X-ray; 2.31 A; A=1-212.
DR PDB; 7RXC; EM; 3.20 A; K=1-212.
DR PDBsum; 6I6B; -.
DR PDBsum; 6I6H; -.
DR PDBsum; 6I6J; -.
DR PDBsum; 6Y7V; -.
DR PDBsum; 6ZXR; -.
DR PDBsum; 7RXC; -.
DR AlphaFoldDB; Q5ZKX9; -.
DR SMR; Q5ZKX9; -.
DR STRING; 9031.ENSGALP00000011467; -.
DR TCDB; 9.B.191.1.8; the endoplasmic reticulum retention receptor (kdelr) family.
DR PaxDb; Q5ZKX9; -.
DR ABCD; Q5ZKX9; 1 sequenced antibody.
DR Ensembl; ENSGALT00000073117; ENSGALP00000045653; ENSGALG00000040793.
DR Ensembl; ENSGALT00000096755; ENSGALP00000072133; ENSGALG00000040793.
DR GeneID; 771927; -.
DR KEGG; gga:771927; -.
DR CTD; 11014; -.
DR VEuPathDB; HostDB:geneid_771927; -.
DR eggNOG; KOG3106; Eukaryota.
DR GeneTree; ENSGT00390000004010; -.
DR InParanoid; Q5ZKX9; -.
DR OMA; AYTVYLM; -.
DR OrthoDB; 1186269at2759; -.
DR PhylomeDB; Q5ZKX9; -.
DR Reactome; R-GGA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-GGA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q5ZKX9; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000040793; Expressed in colon and 13 other tissues.
DR ExpressionAtlas; Q5ZKX9; baseline and differential.
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; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
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:0035437; P:maintenance of protein localization in endoplasmic reticulum; ISS:UniProtKB.
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 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 3D-structure; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Membrane; Protein transport; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..212
FT /note="ER lumen protein-retaining receptor 2"
FT /id="PRO_0000252348"
FT TOPO_DOM 1..4
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TRANSMEM 5..24
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TOPO_DOM 25..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TRANSMEM 33..52
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TOPO_DOM 53..58
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TOPO_DOM 80..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TRANSMEM 93..110
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TOPO_DOM 111..116
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TRANSMEM 117..135
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TOPO_DOM 136..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TRANSMEM 150..168
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TOPO_DOM 169..178
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30846601"
FT TOPO_DOM 200..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30846601"
FT REGION 47..48
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000269|PubMed:30846601"
FT REGION 159..169
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000269|PubMed:30846601"
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:0000305|PubMed:30846601"
FT SITE 5
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000269|PubMed:30846601"
FT SITE 54
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000269|PubMed:30846601"
FT SITE 117
FT /note="Interaction with the K-D-E-L motif on target
FT proteins"
FT /evidence="ECO:0000269|PubMed:30846601"
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 MUTAGEN 12
FT /note="H->A: Loss of binding to the sequence motif K-D-E-
FT L."
FT /evidence="ECO:0000269|PubMed:30846601"
FT MUTAGEN 47
FT /note="R->K: Loss of binding to the sequence motif K-D-E-
FT L."
FT /evidence="ECO:0000269|PubMed:30846601"
FT MUTAGEN 127
FT /note="E->A,Q: Loss of binding to the sequence motif K-D-E-
FT L."
FT /evidence="ECO:0000269|PubMed:30846601"
FT MUTAGEN 158
FT /note="Y->F: Loss of binding to the sequence motif K-D-E-
FT L."
FT /evidence="ECO:0000269|PubMed:30846601"
FT HELIX 3..26
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 34..47
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 58..79
FT /evidence="ECO:0007829|PDB:6I6H"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6I6H"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:6I6H"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 146..173
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:6I6H"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6I6H"
SQ SEQUENCE 212 AA; 24456 MW; 51D3862AAE07C140 CRC64;
MNIFRLTGDL SHLAAIIILL LKIWKSRSCA GISGKSQLLF ALVFTTRYLD LFTSFISLYN
TSMKLIYIAC SYATVYLIYM KFKATYDGNH DTFRVEFLIV PVGGLSFLVN HDFSPLEILW
TFSIYLESVA ILPQLFMISK TGEAETITTH YLFFLGLYRA LYLVNWIWRY YFEGFFDLIA
VVAGVVQTVL YCDFFYLYVT KVLKGKKLSL PA
