NEPR1_MOUSE
ID NEPR1_MOUSE Reviewed; 125 AA.
AC Q3UJ81; A7E1Z4; Q8VEG8; Q9D3Q4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Nuclear envelope phosphatase-regulatory subunit 1;
DE Short=NEP1-R1;
DE AltName: Full=Transmembrane protein 188;
GN Name=Cnep1r1; Synonyms=Tmem188;
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 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic heart;
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 MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=Czech II; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=22134922; DOI=10.1074/jbc.m111.324350;
RA Han S., Bahmanyar S., Zhang P., Grishin N., Oegema K., Crooke R.,
RA Graham M., Reue K., Dixon J.E., Goodman J.M.;
RT "Nuclear envelope phosphatase-regulatory subunit 1 (formerly TMEM188) is
RT the metazoan SPO7 ortholog and functions in the lipin activation pathway.";
RL J. Biol. Chem. 287:3123-3137(2012).
CC -!- FUNCTION: Forms with the serine/threonine protein phosphatase CTDNEP1
CC an active complex which dephosphorylates and may activate LPIN1 and
CC LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the
CC conversion of phosphatidic acid to diacylglycerol and control the
CC metabolism of fatty acids at different levels. May indirectly modulate
CC the lipid composition of nuclear and/or endoplasmic reticulum membranes
CC and be required for proper nuclear membrane morphology and/or dynamics.
CC May also indirectly regulate the production of lipid droplets and
CC triacylglycerol (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTDNEP1; the complex dephosphorylates LPIN1 and
CC LPIN2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Filamentous pattern in the cytoplasm. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UJ81-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UJ81-2; Sequence=VSP_025131;
CC Name=3;
CC IsoId=Q3UJ81-3; Sequence=VSP_025129, VSP_025130;
CC -!- TISSUE SPECIFICITY: Muscle specific with lower expression in other
CC metabolic tissues. {ECO:0000269|PubMed:22134922}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CNEP1R1 family. {ECO:0000305}.
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DR EMBL; AK017198; BAB30631.1; -; mRNA.
DR EMBL; AK146578; BAE27274.1; -; mRNA.
DR EMBL; BC018498; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC148291; AAI48292.2; -; mRNA.
DR CCDS; CCDS52628.1; -. [Q3UJ81-1]
DR RefSeq; NP_083350.2; NM_029074.3. [Q3UJ81-1]
DR AlphaFoldDB; Q3UJ81; -.
DR STRING; 10090.ENSMUSP00000092839; -.
DR iPTMnet; Q3UJ81; -.
DR PhosphoSitePlus; Q3UJ81; -.
DR EPD; Q3UJ81; -.
DR MaxQB; Q3UJ81; -.
DR PaxDb; Q3UJ81; -.
DR PeptideAtlas; Q3UJ81; -.
DR PRIDE; Q3UJ81; -.
DR ProteomicsDB; 287476; -. [Q3UJ81-1]
DR ProteomicsDB; 287477; -. [Q3UJ81-2]
DR ProteomicsDB; 287478; -. [Q3UJ81-3]
DR Antibodypedia; 49431; 13 antibodies from 7 providers.
DR Ensembl; ENSMUST00000095214; ENSMUSP00000092839; ENSMUSG00000036810. [Q3UJ81-1]
DR Ensembl; ENSMUST00000121097; ENSMUSP00000113435; ENSMUSG00000036810. [Q3UJ81-2]
DR Ensembl; ENSMUST00000127490; ENSMUSP00000120121; ENSMUSG00000036810. [Q3UJ81-3]
DR GeneID; 382030; -.
DR KEGG; mmu:382030; -.
DR UCSC; uc009mqx.2; mouse. [Q3UJ81-2]
DR UCSC; uc009mqz.2; mouse. [Q3UJ81-1]
DR CTD; 255919; -.
DR MGI; MGI:1921981; Cnep1r1.
DR VEuPathDB; HostDB:ENSMUSG00000036810; -.
DR eggNOG; KOG4606; Eukaryota.
DR GeneTree; ENSGT00390000008576; -.
DR HOGENOM; CLU_138149_1_0_1; -.
DR InParanoid; Q3UJ81; -.
DR OMA; DQTVCED; -.
DR OrthoDB; 1586654at2759; -.
DR PhylomeDB; Q3UJ81; -.
DR TreeFam; TF313179; -.
DR Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
DR BioGRID-ORCS; 382030; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Cnep1r1; mouse.
DR PRO; PR:Q3UJ81; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3UJ81; protein.
DR Bgee; ENSMUSG00000036810; Expressed in humerus cartilage element and 244 other tissues.
DR ExpressionAtlas; Q3UJ81; baseline and differential.
DR Genevisible; Q3UJ81; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071595; C:Nem1-Spo7 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR InterPro; IPR019168; NEP1-R1.
DR PANTHER; PTHR20996; PTHR20996; 1.
DR Pfam; PF09771; Tmemb_18A; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Lipid metabolism; Membrane;
KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..125
FT /note="Nuclear envelope phosphatase-regulatory subunit 1"
FT /id="PRO_0000286616"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9A8"
FT VAR_SEQ 33..47
FT /note="MLLIVVSVCTATGAW -> SVLLHVIMEPSVFHY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025129"
FT VAR_SEQ 48..125
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025130"
FT VAR_SEQ 94..125
FT /note="IIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ -> MYPLPRVEFCYHN
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025131"
SQ SEQUENCE 125 AA; 14267 MW; 546EB9BEFE8EA593 CRC64;
MNSLEQAEDL KAFERRLTEY IHCLQPATGR WRMLLIVVSV CTATGAWNWL IDPETQKVSF
FTSLWNHPFF TISCITLIGL FFAGIHKRVV APSIIAARCR TVLAEYNMSC DDTGKLILKP
RPHVQ
