ID Q6PH70_DANRE Unreviewed; 212 AA. AC Q6PH70; A0A8M1PLF1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 108. DE RecName: Full=ER lumen protein-retaining receptor 2 {ECO:0000256|ARBA:ARBA00040686}; DE AltName: Full=KDEL endoplasmic reticulum protein retention receptor 2 {ECO:0000256|ARBA:ARBA00042141}; GN Name=kdelr2l {ECO:0000313|EMBL:AAH56694.1, GN ECO:0000313|RefSeq:NP_997860.1}; GN Synonyms=wu:fa93g04 {ECO:0000313|RefSeq:NP_997860.1}, wu:fc79e05 GN {ECO:0000313|RefSeq:NP_997860.1}, zgc:66047 GN {ECO:0000313|RefSeq:NP_997860.1}; GN OrderedLocusNames=kdelr2b {ECO:0000313|Ensembl:ENSDARP00000054366, GN ECO:0000313|RefSeq:NP_997860.1, GN ECO:0000313|ZFIN:ZDB-GENE-030131-4189}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH56694.1}; RN [1] {ECO:0000313|EMBL:AAH56694.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney {ECO:0000313|EMBL:AAH56694.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|RefSeq:NP_997860.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16109975; RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R., RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.; RT "The zebrafish gene map defines ancestral vertebrate chromosomes."; RL Genome Res. 15:1307-1314(2005). RN [3] {ECO:0000313|Ensembl:ENSDARP00000054366} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000054366}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [4] {ECO:0000313|Ensembl:ENSDARP00000054366, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000054366}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [5] {ECO:0000313|RefSeq:NP_997860.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26469318; RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M., RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D., RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E., RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M., RA Reith W., Hertzano R.; RT "RFX transcription factors are essential for hearing in mice."; RL Nat. Commun. 6:8549-8549(2015). RN [6] {ECO:0000313|RefSeq:NP_997860.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=27189481; RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I., RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y., RA Bobe J.; RT "Gene evolution and gene expression after whole genome duplication in fish: RT the PhyloFish database."; RL BMC Genomics 17:368-368(2016). RN [7] {ECO:0000313|RefSeq:NP_997860.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (SEP-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle membrane CC {ECO:0000256|ARBA:ARBA00004129}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004129}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004653}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the ERD2 family. CC {ECO:0000256|ARBA:ARBA00010120}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU565526; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC056694; AAH56694.1; -; mRNA. DR RefSeq; NP_997860.1; NM_212695.1. DR STRING; 7955.ENSDARP00000054366; -. DR PaxDb; 7955-ENSDARP00000054366; -. DR Ensembl; ENSDART00000054367.5; ENSDARP00000054366.3; ENSDARG00000037361.5. DR GeneID; 325464; -. DR KEGG; dre:325464; -. DR CTD; 325464; -. DR ZFIN; ZDB-GENE-030131-4189; kdelr2b. DR eggNOG; KOG3106; Eukaryota. DR HOGENOM; CLU_057784_0_0_1; -. DR OMA; WKSRSCE; -. DR OrthoDB; 5258269at2759; -. DR TreeFam; TF314792; -. DR Reactome; R-DRE-6807878; COPI-mediated anterograde transport. DR Reactome; R-DRE-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Proteomes; UP000000437; Chromosome 12. DR Bgee; ENSDARG00000037361; Expressed in caudal fin and 39 other cell types or 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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046923; F:ER retention sequence binding; IBA:GO_Central. 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 InterPro; IPR000133; ER_ret_rcpt. DR PANTHER; PTHR10585; ER LUMEN PROTEIN RETAINING RECEPTOR; 1. DR PANTHER; PTHR10585:SF37; ER LUMEN PROTEIN-RETAINING RECEPTOR 2; 1. DR Pfam; PF00810; ER_lumen_recept; 1. DR PRINTS; PR00660; ERLUMENR. DR PROSITE; PS00951; ER_LUMEN_RECEPTOR_1; 1. PE 2: Evidence at transcript level; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Protein transport {ECO:0000256|ARBA:ARBA00022927}; KW Receptor {ECO:0000313|EMBL:AAH56694.1, ECO:0000313|RefSeq:NP_997860.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 65..82 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 94..113 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 119..139 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 151..172 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 178..199 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 212 AA; 24396 MW; 099419C43AD4B697 CRC64; MNLFRLTGDL SHLAAIIILL LKIWKSRSCA GISGKSQILF ALVFTTRYLD LLTSFISLYN TSMKVIYIAC AYATVYLIYA KFKATYDGNH DTFRVEFLVV PVGGLAFLVN HDFSPLEILW TFSIYLESVS ILPQLFMISK TGEAETITTH YLFFLGLYRA LYLFNWIWRF YFEGFFDMIA IVAGVVQTIL YCDFFYLYVT KVLKGKKLSL PA //