ERD21_BOVIN
ID ERD21_BOVIN Reviewed; 212 AA.
AC P33946; Q17QP2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ER lumen protein-retaining receptor 1;
DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 1;
DE Short=KDEL receptor 1;
GN Name=KDELR1; Synonyms=KDELR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=8380600; DOI=10.1083/jcb.120.2.325;
RA Tang B.L., Wong S.H., Qi X.L., Low S.H., Hong W.;
RT "Molecular cloning, characterization, subcellular localization and dynamics
RT of p23, the mammalian KDEL receptor.";
RL J. Cell Biol. 120:325-338(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:8380600}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8380600}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000305|PubMed:8380600}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8380600}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8380600}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8380600}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:8380600}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:8380600}. 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:0000269|PubMed:8380600}.
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; BC118250; AAI18251.1; -; mRNA.
DR PIR; A44394; A44394.
DR RefSeq; NP_001069963.1; NM_001076495.1.
DR AlphaFoldDB; P33946; -.
DR SMR; P33946; -.
DR STRING; 9913.ENSBTAP00000005857; -.
DR PaxDb; P33946; -.
DR PRIDE; P33946; -.
DR Ensembl; ENSBTAT00000005857; ENSBTAP00000005857; ENSBTAG00000004463.
DR GeneID; 618184; -.
DR KEGG; bta:618184; -.
DR CTD; 10945; -.
DR VEuPathDB; HostDB:ENSBTAG00000004463; -.
DR VGNC; VGNC:52202; KDELR1.
DR eggNOG; KOG3106; Eukaryota.
DR GeneTree; ENSGT00390000004010; -.
DR HOGENOM; CLU_057784_0_0_1; -.
DR InParanoid; P33946; -.
DR OMA; APFELLW; -.
DR OrthoDB; 1186269at2759; -.
DR TreeFam; TF314792; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000004463; Expressed in ascending colon and 104 other tissues.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
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; 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 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_0000194152"
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"
FT CONFLICT 77
FT /note="M -> L (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 24574 MW; 9E0EE32BF14B8C20 CRC64;
MNLFRFLGDL SHLLAIILLL LKIWKSRSCA GISGKSQVLF AVVFTARYLD LFTNYISLYN
TCMKVVYIAC SFTTVWMIYS KFKATYDGNH DTFRVEFLVI PTAILAFLVN HDFTPLEILW
TFSIYLESVA ILPQLFMVSK TGEAETITSH YLFALGVYRT LYLFNWIWRY HFEGFFDLIA
IVAGLVQTVL YCDFFYLYIT KVLKGKKLSL PA
