OBRG_MOUSE
ID OBRG_MOUSE Reviewed; 131 AA.
AC O89013; A2AV64; Q3TGT4; Q3TWZ2; Q545G9; Q91Z23;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Leptin receptor gene-related protein;
DE AltName: Full=Endospanin-1;
DE AltName: Full=OB-R gene-related protein;
DE Short=OB-RGRP;
GN Name=Leprot; Synonyms=Lepr, Obr;
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 [MRNA] (ISOFORM 1).
RX PubMed=9207021; DOI=10.1093/nar/25.14.2752;
RA Bailleul B., Akerblom I., Strosberg A.D.;
RT "The leptin receptor promoter controls expression of a second distinct
RT protein.";
RL Nucleic Acids Res. 25:2752-2758(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Diencephalon, Embryonic kidney, Osteoclast, Pancreas, and Tongue;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, and 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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=10849209; DOI=10.1046/j.1365-2826.2000.00501.x;
RA Mercer J.G., Moar K.M., Hoggard N., Strosberg A.D., Froguel P.,
RA Bailleul B.;
RT "B219/OB-R 5'-UTR and leptin receptor gene-related protein gene expression
RT in mouse brain and placenta: tissue-specific leptin receptor promoter
RT activity.";
RL J. Neuroendocrinol. 12:649-655(2000).
RN [6]
RP FUNCTION, INTERACTION WITH LEPR, AND SUBCELLULAR LOCATION.
RX PubMed=18042720; DOI=10.1073/pnas.0706671104;
RA Couturier C., Sarkis C., Seron K., Belouzard S., Chen P., Lenain A.,
RA Corset L., Dam J., Vauthier V., Dubart A., Mallet J., Froguel P.,
RA Rouille Y., Jockers R.;
RT "Silencing of OB-RGRP in mouse hypothalamic arcuate nucleus increases
RT leptin receptor signaling and prevents diet-induced obesity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19476-19481(2007).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=19907080; DOI=10.1172/jci34997;
RA Touvier T., Conte-Auriol F., Briand O., Cudejko C., Paumelle R., Caron S.,
RA Bauge E., Rouille Y., Salles J.P., Staels B., Bailleul B.;
RT "LEPROT and LEPROTL1 cooperatively decrease hepatic growth hormone action
RT in mice.";
RL J. Clin. Invest. 119:3830-3838(2009).
CC -!- FUNCTION: Negatively regulates leptin receptor (LEPR) cell surface
CC expression, and thus decreases response to leptin. Negatively regulates
CC growth hormone (GH) receptor cell surface expression in liver. May play
CC a role in liver resistance to GH during periods of reduced nutrient
CC availability. {ECO:0000269|PubMed:18042720,
CC ECO:0000269|PubMed:19907080}.
CC -!- SUBUNIT: Interacts with LEPR. Interacts with RAB13 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18042720}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18042720}. Endosome membrane
CC {ECO:0000269|PubMed:18042720}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O89013-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O89013-2; Sequence=VSP_039718;
CC -!- TISSUE SPECIFICITY: Widely distributed in the brain, with elevated
CC expression in the hypothalamic regions, including the paraventricular
CC nucleus. In the placenta, present at high levels in the junctional zone
CC situated towards the maternal aspect and throughout the labyrinth zone
CC in close proximity to the developing fetus.
CC {ECO:0000269|PubMed:10849209}.
CC -!- INDUCTION: Up-regulated in the liver of fasting animals.
CC {ECO:0000269|PubMed:19907080}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the OB-RGRP/VPS55 family. {ECO:0000305}.
CC -!- CAUTION: This protein is encoded by the leptin receptor (LEPR) gene,
CC but shares with LEPR only the first two 5'-UTR exons. It therefore does
CC not share any sequence similarity with LEPR. {ECO:0000305}.
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DR EMBL; AJ011565; CAA09693.1; -; mRNA.
DR EMBL; AK009569; BAB26366.1; -; mRNA.
DR EMBL; AK159489; BAE35124.1; -; mRNA.
DR EMBL; AK160453; BAE35795.1; -; mRNA.
DR EMBL; AK165821; BAE38395.1; -; mRNA.
DR EMBL; AK168597; BAE40464.1; -; mRNA.
DR EMBL; AL929373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX323551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004744; AAH04744.1; -; mRNA.
DR EMBL; BC010289; AAH10289.1; -; mRNA.
DR CCDS; CCDS18396.1; -. [O89013-1]
DR RefSeq; NP_778201.1; NM_175036.4. [O89013-1]
DR AlphaFoldDB; O89013; -.
DR STRING; 10090.ENSMUSP00000030254; -.
DR SwissPalm; O89013; -.
DR MaxQB; O89013; -.
DR PaxDb; O89013; -.
DR PeptideAtlas; O89013; -.
DR PRIDE; O89013; -.
DR ProteomicsDB; 293825; -. [O89013-1]
DR Antibodypedia; 67309; 8 antibodies from 6 providers.
DR DNASU; 230514; -.
DR Ensembl; ENSMUST00000030254; ENSMUSP00000030254; ENSMUSG00000035212. [O89013-1]
DR Ensembl; ENSMUST00000106927; ENSMUSP00000102540; ENSMUSG00000035212. [O89013-2]
DR GeneID; 230514; -.
DR KEGG; mmu:230514; -.
DR UCSC; uc008tvu.1; mouse. [O89013-1]
DR UCSC; uc008tvv.1; mouse. [O89013-2]
DR CTD; 54741; -.
DR MGI; MGI:2687005; Leprot.
DR VEuPathDB; HostDB:ENSMUSG00000035212; -.
DR eggNOG; KOG2174; Eukaryota.
DR GeneTree; ENSGT00390000006503; -.
DR HOGENOM; CLU_134810_2_2_1; -.
DR InParanoid; O89013; -.
DR OMA; GGDEFSW; -.
DR OrthoDB; 1642378at2759; -.
DR PhylomeDB; O89013; -.
DR TreeFam; TF313689; -.
DR BioGRID-ORCS; 230514; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Leprot; mouse.
DR PRO; PR:O89013; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O89013; protein.
DR Bgee; ENSMUSG00000035212; Expressed in brain blood vessel and 262 other tissues.
DR Genevisible; O89013; MM.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0060400; P:negative regulation of growth hormone receptor signaling pathway; ISO:MGI.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR InterPro; IPR007262; Vps55/LEPROT.
DR PANTHER; PTHR12050; PTHR12050; 1.
DR Pfam; PF04133; Vps55; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endosome; Golgi apparatus; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..131
FT /note="Leptin receptor gene-related protein"
FT /id="PRO_0000215195"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 33..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039718"
FT CONFLICT 44
FT /note="I -> T (in Ref. 2; BAE40464)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="D -> G (in Ref. 2; BAE35124 and 4; AAH10289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 131 AA; 14316 MW; 67D71630A935481D CRC64;
MAGVKALVAL SFSGAIGLTF LMLGCALEDY GVYWPLFVLI FYVISPIPYF IAKRVTYDSD
ATSSACRELA YFFTTGIVVS AFGLPVVLAR VDVIKWGACG LVLAGNAVIF LTIQGFFLVF
GRGDDFSWEQ W
