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ERD22_BOVIN
ID   ERD22_BOVIN             Reviewed;         212 AA.
AC   Q2KJ37;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P33947, ECO:0000250|UniProtKB:Q5ZKX9}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q5ZKX9}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q5ZKX9}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000250|UniProtKB:P33947}; 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: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 (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; BC105537; AAI05538.1; -; mRNA.
DR   RefSeq; NP_001073247.1; NM_001079779.1.
DR   AlphaFoldDB; Q2KJ37; -.
DR   SMR; Q2KJ37; -.
DR   STRING; 9913.ENSBTAP00000012175; -.
DR   PaxDb; Q2KJ37; -.
DR   PRIDE; Q2KJ37; -.
DR   Ensembl; ENSBTAT00000012175; ENSBTAP00000012175; ENSBTAG00000009237.
DR   GeneID; 531676; -.
DR   KEGG; bta:531676; -.
DR   CTD; 11014; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009237; -.
DR   VGNC; VGNC:30519; KDELR2.
DR   eggNOG; KOG3106; Eukaryota.
DR   GeneTree; ENSGT00390000004010; -.
DR   InParanoid; Q2KJ37; -.
DR   OMA; AYTVYLM; -.
DR   OrthoDB; 1186269at2759; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000009237; Expressed in spermatocyte 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; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
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: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   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Protein transport; Receptor; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..212
FT                   /note="ER lumen protein-retaining receptor 2"
FT                   /id="PRO_0000252347"
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: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            54
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"
SQ   SEQUENCE   212 AA;  24454 MW;  774388DAF56FEC24 CRC64;
     MNIFRLTGDL SHLAAIVILL LKIWKTRSCA GISGKSQLLF ALVFTTRYLD LFTSFISLYN
     TSMKLIYIAC SYATVYLIYM KFKATYDGNH DTFRVEFLVV PVGGLSFLVN HDFSPLEILW
     TFSIYLESVA ILPQLFMISK TGEAETITTH YLFFLGLYRA LYLVNWIWRF YFEGFFDLIA
     VVAGVVQTIL YCDFFYLYIT KVLKGKKLSL PA
 
 
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