RETR1_MOUSE
ID RETR1_MOUSE Reviewed; 480 AA.
AC Q8VE91; E9QPM1; Q7TMY5; Q9CUJ4; Q9D8Z5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Reticulophagy regulator 1;
DE AltName: Full=Reticulophagy receptor 1 {ECO:0000305};
GN Name=Retreg1; Synonyms=Fam134b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Liver, Pancreas, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19838196; DOI=10.1038/ng.464;
RA Kurth I., Pamminger T., Hennings J.C., Soehendra D., Huebner A.K.,
RA Rotthier A., Baets J., Senderek J., Topaloglu H., Farrell S.A.,
RA Nuernberg G., Nurnberg P., De Jonghe P., Gal A., Kaether C., Timmerman V.,
RA Huebner C.A.;
RT "Mutations in FAM134B, encoding a newly identified Golgi protein, cause
RT severe sensory and autonomic neuropathy.";
RL Nat. Genet. 41:1179-1181(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=26040720; DOI=10.1038/nature14498;
RA Khaminets A., Heinrich T., Mari M., Grumati P., Huebner A.K., Akutsu M.,
RA Liebmann L., Stolz A., Nietzsche S., Koch N., Mauthe M., Katona I.,
RA Qualmann B., Weis J., Reggiori F., Kurth I., Huebner C.A., Dikic I.;
RT "Regulation of endoplasmic reticulum turnover by selective autophagy.";
RL Nature 522:354-358(2015).
CC -!- FUNCTION: Endoplasmic reticulum-anchored autophagy receptor that
CC mediates ER delivery into lysosomes through sequestration into
CC autophagosomes (PubMed:26040720). Promotes membrane remodeling and ER
CC scission via its membrane bending capacity and targets the fragments
CC into autophagosomes via interaction with ATG8 family proteins
CC (PubMed:26040720). Required for long-term survival of nociceptive and
CC autonomic ganglion neurons (PubMed:19838196, PubMed:26040720).
CC {ECO:0000269|PubMed:19838196, ECO:0000269|PubMed:26040720}.
CC -!- SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A,
CC MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2.
CC {ECO:0000250|UniProtKB:Q9H6L5}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:19838196}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9H6L5}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=Q8VE91-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8VE91-1; Sequence=VSP_057838;
CC Name=2;
CC IsoId=Q8VE91-2; Sequence=VSP_057836;
CC Name=3;
CC IsoId=Q8VE91-3; Sequence=VSP_057837;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in sensory and autonomic
CC ganglia has demonstrated by in situ hybridizations of embryonic day
CC 14.5 mouse embryo sections. Detected specifically in organelle-like
CC intracellular structures of the small and large neurons of dorsal root
CC ganglia (DRG) and in Neuro-2a cells, a tumor cell line that is related
CC to autonomic ganglion neurons (at protein level).
CC {ECO:0000269|PubMed:19838196}.
CC -!- DOMAIN: The LIR motif interacts with ATG8 family proteins and is
CC necessary to target the ER fragments to autophagosomes for lysosomal
CC degradation. {ECO:0000269|PubMed:26040720}.
CC -!- DOMAIN: The reticulon homology domain provides capacity to bend the
CC membrane and promotes ER scission (PubMed:26040720). This domain does
CC not show relevant similarities with reticulon domains, preventing any
CC domain predictions within the protein sequence.
CC {ECO:0000269|PubMed:26040720, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Leads to an expanded endoplasmic reticulum.
CC {ECO:0000269|PubMed:26040720}.
CC -!- MISCELLANEOUS: [Isoform 4]: Predicted by similarity to human,.
CC -!- SIMILARITY: Belongs to the RETREG family. {ECO:0000305}.
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DR EMBL; AK007506; BAB25077.1; -; mRNA.
DR EMBL; AK146972; BAE27577.1; -; mRNA.
DR EMBL; AK015887; BAB30019.1; -; mRNA.
DR EMBL; AK167327; BAE39429.1; -; mRNA.
DR EMBL; AC131178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019494; AAH19494.1; -; mRNA.
DR EMBL; BC054415; AAH54415.1; -; mRNA.
DR CCDS; CCDS37050.1; -. [Q8VE91-4]
DR CCDS; CCDS37051.1; -. [Q8VE91-2]
DR CCDS; CCDS88741.1; -. [Q8VE91-1]
DR CCDS; CCDS88742.1; -. [Q8VE91-3]
DR RefSeq; NP_001030023.1; NM_001034851.2. [Q8VE91-4]
DR RefSeq; NP_001264244.1; NM_001277315.1. [Q8VE91-2]
DR RefSeq; NP_001264245.1; NM_001277316.1. [Q8VE91-1]
DR RefSeq; NP_001264246.1; NM_001277317.1. [Q8VE91-3]
DR RefSeq; NP_079735.2; NM_025459.3. [Q8VE91-2]
DR RefSeq; XP_006520197.1; XM_006520134.3. [Q8VE91-2]
DR RefSeq; XP_017172209.1; XM_017316720.1. [Q8VE91-2]
DR AlphaFoldDB; Q8VE91; -.
DR DIP; DIP-61579N; -.
DR IntAct; Q8VE91; 1.
DR STRING; 10090.ENSMUSP00000022881; -.
DR iPTMnet; Q8VE91; -.
DR PhosphoSitePlus; Q8VE91; -.
DR EPD; Q8VE91; -.
DR MaxQB; Q8VE91; -.
DR PaxDb; Q8VE91; -.
DR PeptideAtlas; Q8VE91; -.
DR PRIDE; Q8VE91; -.
DR ProteomicsDB; 255230; -. [Q8VE91-4]
DR ProteomicsDB; 255231; -. [Q8VE91-1]
DR ProteomicsDB; 255232; -. [Q8VE91-2]
DR ProteomicsDB; 255233; -. [Q8VE91-3]
DR Antibodypedia; 5201; 142 antibodies from 22 providers.
DR DNASU; 66270; -.
DR Ensembl; ENSMUST00000022881; ENSMUSP00000022881; ENSMUSG00000022270. [Q8VE91-4]
DR Ensembl; ENSMUST00000110438; ENSMUSP00000106068; ENSMUSG00000022270. [Q8VE91-2]
DR Ensembl; ENSMUST00000226438; ENSMUSP00000154765; ENSMUSG00000022270. [Q8VE91-1]
DR Ensembl; ENSMUST00000227275; ENSMUSP00000154471; ENSMUSG00000022270. [Q8VE91-2]
DR Ensembl; ENSMUST00000228306; ENSMUSP00000154070; ENSMUSG00000022270. [Q8VE91-3]
DR GeneID; 66270; -.
DR KEGG; mmu:66270; -.
DR UCSC; uc007vjf.2; mouse.
DR UCSC; uc007vjg.2; mouse. [Q8VE91-4]
DR UCSC; uc007vji.2; mouse. [Q8VE91-2]
DR UCSC; uc033gth.1; mouse. [Q8VE91-3]
DR CTD; 54463; -.
DR MGI; MGI:1913520; Retreg1.
DR VEuPathDB; HostDB:ENSMUSG00000022270; -.
DR eggNOG; ENOG502QPW8; Eukaryota.
DR GeneTree; ENSGT00940000160746; -.
DR HOGENOM; CLU_036265_0_0_1; -.
DR InParanoid; Q8VE91; -.
DR OMA; WPLISSQ; -.
DR OrthoDB; 901531at2759; -.
DR PhylomeDB; Q8VE91; -.
DR TreeFam; TF329111; -.
DR BioGRID-ORCS; 66270; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Fam134b; mouse.
DR PRO; PR:Q8VE91; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VE91; protein.
DR Bgee; ENSMUSG00000022270; Expressed in plantaris and 262 other tissues.
DR ExpressionAtlas; Q8VE91; baseline and differential.
DR Genevisible; Q8VE91; MM.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:GO_Central.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0140506; F:endoplasmic reticulum-autophagosome adaptor activity; IMP:MGI.
DR GO; GO:0006914; P:autophagy; IDA:MGI.
DR GO; GO:0030574; P:collagen catabolic process; IMP:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0000423; P:mitophagy; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IDA:MGI.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0050872; P:white fat cell differentiation; IDA:MGI.
DR InterPro; IPR033358; RETREG1.
DR InterPro; IPR043384; RETREG1/3.
DR PANTHER; PTHR28659; PTHR28659; 1.
DR PANTHER; PTHR28659:SF3; PTHR28659:SF3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Endoplasmic reticulum; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..480
FT /note="Reticulophagy regulator 1"
FT /id="PRO_0000288467"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..75
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..191
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..216
FT /note="Reticulon homology domain"
FT /evidence="ECO:0000305|PubMed:26040720"
FT REGION 302..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 436..441
FT /note="LIR motif"
FT /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT COMPBIAS 333..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..135
FT /note="MASPAPEEHATQGCPATEEQPPRPGVPGEEAGPEGAGPQVEEAAGRVAAALT
FT WLLGEPVLWLGWRADELLSWKRPLRSLLTFLGANLLFWFLALTPWRVYHLISVMILGRV
FT IMQIIKEMVLSRTRGAQLWRSLTE -> MPAGGGCGPGR (in isoform 2)"
FT /id="VSP_057836"
FT VAR_SEQ 1..135
FT /note="MASPAPEEHATQGCPATEEQPPRPGVPGEEAGPEGAGPQVEEAAGRVAAALT
FT WLLGEPVLWLGWRADELLSWKRPLRSLLTFLGANLLFWFLALTPWRVYHLISVMILGRV
FT IMQIIKEMVLSRTRGAQLWRSLTE -> M (in isoform 3)"
FT /id="VSP_057837"
FT VAR_SEQ 1..134
FT /note="MASPAPEEHATQGCPATEEQPPRPGVPGEEAGPEGAGPQVEEAAGRVAAALT
FT WLLGEPVLWLGWRADELLSWKRPLRSLLTFLGANLLFWFLALTPWRVYHLISVMILGRV
FT IMQIIKEMVLSRTRGAQLWRSLT -> MLGDWAALLPSCLSRCWS (in isoform
FT 1)"
FT /id="VSP_057838"
SQ SEQUENCE 480 AA; 52967 MW; 6181AF418CBCC29A CRC64;
MASPAPEEHA TQGCPATEEQ PPRPGVPGEE AGPEGAGPQV EEAAGRVAAA LTWLLGEPVL
WLGWRADELL SWKRPLRSLL TFLGANLLFW FLALTPWRVY HLISVMILGR VIMQIIKEMV
LSRTRGAQLW RSLTESWEVI NSKPDERARL SQCIAESWMN FSMFLQEMSL FKQQSPGKFC
LLVCSVCTFF TILGSYIPGV ILSYLLLLFA FLCPLFKCND IGQKIYSKVK SILLKLDFGI
GEYINQKKRE RSEADKEKSH KDDSELDFSA LCPKISLTVA AKELSVSDTD VSEVSWTDNG
TFNLSEGYTP QTDTSDDLDR PSEEVFSRDL SDFPSLENGT GTNDEDELSL GLPTELKRKK
QQLDSAHRPS KERQSAAGLS LPLKSDQALH LMSNLAGDVI TAAMTAAIKD QLEGARQALT
QVAPTAGEDT DTEEGDDFEL LDQAELDQIE SELGLTQDQG AEAQQSKKSS GFLSNLLGGH
