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Leptin receptor gene-related protein (Endospanin-1) (Leptin receptor overlapping transcript protein) (OB-R gene-related protein) (OB-RGRP)

 OBRG_HUMAN              Reviewed;         131 AA.
O15243; Q6FHL5;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
12-SEP-2018, entry version 135.
RecName: Full=Leptin receptor gene-related protein;
AltName: Full=Endospanin-1;
AltName: Full=Leptin receptor overlapping transcript protein;
AltName: Full=OB-R gene-related protein;
Short=OB-RGRP;
Name=LEPROT; Synonyms=LEPR, OBR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9207021; DOI=10.1093/nar/25.14.2752;
Bailleul B., Akerblom I., Strosberg A.D.;
"The leptin receptor promoter controls expression of a second distinct
protein.";
Nucleic Acids Res. 25:2752-2758(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate, and Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION.
PubMed=18042720; DOI=10.1073/pnas.0706671104;
Couturier C., Sarkis C., Seron K., Belouzard S., Chen P., Lenain A.,
Corset L., Dam J., Vauthier V., Dubart A., Mallet J., Froguel P.,
Rouille Y., Jockers R.;
"Silencing of OB-RGRP in mouse hypothalamic arcuate nucleus increases
leptin receptor signaling and prevents diet-induced obesity.";
Proc. Natl. Acad. Sci. U.S.A. 104:19476-19481(2007).
[8]
FUNCTION.
PubMed=19907080; DOI=10.1172/JCI34997;
Touvier T., Conte-Auriol F., Briand O., Cudejko C., Paumelle R.,
Caron S., Bauge E., Rouille Y., Salles J.P., Staels B., Bailleul B.;
"LEPROT and LEPROTL1 cooperatively decrease hepatic growth hormone
action in mice.";
J. Clin. Invest. 119:3830-3838(2009).
-!- FUNCTION: Negatively regulates leptin receptor (LEPR) cell surface
expression, and thus decreases response to leptin. Negatively
regulates growth hormone (GH) receptor cell surface expression in
liver. May play a role in liver resistance to GH during periods of
reduced nutrient availability. {ECO:0000269|PubMed:18042720,
ECO:0000269|PubMed:19907080}.
-!- SUBUNIT: Interacts with LEPR. Interacts with RAB13 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
P48357:LEPR; NbExp=2; IntAct=EBI-15672507, EBI-518596;
O95807:TMEM50A; NbExp=4; IntAct=EBI-15672507, EBI-12903814;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000250}. Endosome membrane
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed at the highest levels in heart and
placenta and at a lesser extent in lung, liver, skeletal muscle,
kidney and pancreas.
-!- SIMILARITY: Belongs to the OB-RGRP/VPS55 family. {ECO:0000305}.
-!- CAUTION: This protein is encoded by LEPR gene, but shares with
LEPR only the first two 5'-UTR exons. It therefore does not share
any sequence similarity with LEPR. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y12670; CAA73211.1; -; mRNA.
EMBL; CR541647; CAG46448.1; -; mRNA.
EMBL; CR541737; CAG46537.1; -; mRNA.
EMBL; AK074841; BAG52014.1; -; mRNA.
EMBL; AC119800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06527.1; -; Genomic_DNA.
EMBL; CH471059; EAX06531.1; -; Genomic_DNA.
EMBL; BC011027; AAH11027.2; -; mRNA.
EMBL; BC056250; AAH56250.1; -; mRNA.
CCDS; CCDS630.1; -.
RefSeq; NP_001185612.1; NM_001198683.1.
RefSeq; NP_059996.1; NM_017526.4.
UniGene; Hs.23581; -.
UniGene; Hs.258228; -.
ProteinModelPortal; O15243; -.
BioGrid; 120123; 1.
DIP; DIP-29969N; -.
IntAct; O15243; 10.
STRING; 9606.ENSP00000360104; -.
SwissPalm; O15243; -.
BioMuta; LEPROT; -.
EPD; O15243; -.
MaxQB; O15243; -.
PaxDb; O15243; -.
PeptideAtlas; O15243; -.
PRIDE; O15243; -.
ProteomicsDB; 48532; -.
DNASU; 54741; -.
Ensembl; ENST00000371065; ENSP00000360104; ENSG00000213625.
GeneID; 54741; -.
KEGG; hsa:54741; -.
UCSC; uc001dcf.4; human.
CTD; 54741; -.
DisGeNET; 54741; -.
EuPathDB; HostDB:ENSG00000213625.8; -.
GeneCards; LEPROT; -.
HGNC; HGNC:29477; LEPROT.
HPA; HPA069444; -.
MIM; 613461; gene.
neXtProt; NX_O15243; -.
OpenTargets; ENSG00000213625; -.
PharmGKB; PA134913422; -.
eggNOG; KOG2174; Eukaryota.
eggNOG; ENOG4111UCZ; LUCA.
GeneTree; ENSGT00390000006503; -.
HOGENOM; HOG000038515; -.
HOVERGEN; HBG001034; -.
InParanoid; O15243; -.
PhylomeDB; O15243; -.
TreeFam; TF313689; -.
ChiTaRS; LEPROT; human.
GenomeRNAi; 54741; -.
PRO; PR:O15243; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000213625; Expressed in 240 organ(s), highest expression level in oviduct epithelium.
CleanEx; HS_LEPR; -.
ExpressionAtlas; O15243; baseline and differential.
Genevisible; O15243; HS.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
GO; GO:0060400; P:negative regulation of growth hormone receptor signaling pathway; IDA:UniProtKB.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IDA:UniProtKB.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:UniProtKB.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
InterPro; IPR007262; VPS55.
PANTHER; PTHR12050; PTHR12050; 1.
Pfam; PF04133; Vps55; 1.
1: Evidence at protein level;
Complete proteome; Endosome; Golgi apparatus; Membrane;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 131 Leptin receptor gene-related protein.
/FTId=PRO_0000215194.
TRANSMEM 7 27 Helical. {ECO:0000255}.
TRANSMEM 32 52 Helical. {ECO:0000255}.
TRANSMEM 69 89 Helical. {ECO:0000255}.
TRANSMEM 100 120 Helical. {ECO:0000255}.
SEQUENCE 131 AA; 14254 MW; 0F9CE741C2C5ED9C CRC64;
MAGVKALVAL SFSGAIGLTF LMLGCALEDY GVYWPLFVLI FHAISPIPHF IAKRVTYDSD
ATSSACRELA YFFTTGIVVS AFGFPVILAR VAVIKWGACG LVLAGNAVIF LTIQGFFLIF
GRGDDFSWEQ W


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