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ERD21_XENTR
ID   ERD21_XENTR             Reviewed;         212 AA.
AC   Q5XHA2; Q28FZ7;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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; ORFNames=TGas070a01.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) 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   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P33946}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P33946}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P33946}; 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:0000250|UniProtKB:P33946}.
CC   -!- SIMILARITY: Belongs to the ERD2 family. {ECO:0000305}.
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DR   EMBL; CR761657; CAJ83568.1; -; mRNA.
DR   EMBL; BC084170; AAH84170.1; -; mRNA.
DR   RefSeq; NP_001011046.1; NM_001011046.1.
DR   AlphaFoldDB; Q5XHA2; -.
DR   SMR; Q5XHA2; -.
DR   STRING; 8364.ENSXETP00000023269; -.
DR   PaxDb; Q5XHA2; -.
DR   DNASU; 496456; -.
DR   GeneID; 496456; -.
DR   KEGG; xtr:496456; -.
DR   CTD; 11014; -.
DR   Xenbase; XB-GENE-943535; kdelr2.
DR   eggNOG; KOG3106; Eukaryota.
DR   HOGENOM; CLU_057784_0_0_1; -.
DR   InParanoid; Q5XHA2; -.
DR   OMA; MRYLDIM; -.
DR   OrthoDB; 1186269at2759; -.
DR   PhylomeDB; Q5XHA2; -.
DR   TreeFam; TF314792; -.
DR   Reactome; R-XTR-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-XTR-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000010606; Expressed in liver and 15 other tissues.
DR   ExpressionAtlas; Q5XHA2; baseline.
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   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 1"
FT                   /id="PRO_0000252346"
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   CONFLICT        114
FT                   /note="T -> I (in Ref. 1; CAJ83568)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   212 AA;  24551 MW;  81A21EEAE9B0223B CRC64;
     MNIFRFLGDI SHLSAILILL LKIWKSRSCA GISGKSQLLF AIVFTTRYLD LFTNFISLYN
     TSMKMVYVAS SYATIWMIYS KFKATYDGNH DTFRVEFLIV PTAILAFLVN HDFTPLEILW
     TFSIYLESVA ILPQLFMVSK TGEAETITSH YLFALGIYRA LYLFNWIWRY QFEGFFDLIA
     IVAGLVQTVL YCDFFYLYIT KVLKGKKLSL PA
 
 
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