PLPP7_MOUSE
ID PLPP7_MOUSE Reviewed; 271 AA.
AC Q91WB2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Inactive phospholipid phosphatase 7 {ECO:0000250|UniProtKB:Q8NBV4};
DE AltName: Full=Nuclear envelope transmembrane protein 39;
DE AltName: Full=Phosphatidic acid phosphatase type 2 domain-containing protein 3;
GN Name=Plpp7 {ECO:0000250|UniProtKB:Q8NBV4}; Synonyms=Net39, Ppapdc3;
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].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Medulla oblongata;
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].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17062158; DOI=10.1186/1471-2121-7-38;
RA Chen I.-H., Huber M., Guan T., Bubeck A., Gerace L.;
RT "Nuclear envelope transmembrane proteins (NETs) that are up-regulated
RT during myogenesis.";
RL BMC Cell Biol. 7:38-38(2006).
RN [4]
RP FUNCTION, LACK OF ENZYMATIC ACTIVITY, SUBUNIT, INTERACTION WITH MTOR,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOPOLOGY, AND INDUCTION.
RX PubMed=19704009; DOI=10.1128/mcb.00684-09;
RA Liu G.H., Guan T., Datta K., Coppinger J., Yates J. III, Gerace L.;
RT "Regulation of myoblast differentiation by the nuclear envelope protein
RT NET39.";
RL Mol. Cell. Biol. 29:5800-5812(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC 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).
CC -!- FUNCTION: Plays a role as negative regulator of myoblast
CC differentiation, in part through effects on MTOR signaling. Has no
CC detectable enzymatic activity. Knockdown in myoblasts strongly promotes
CC differentiation, whereas overexpression represses myogenesis.
CC {ECO:0000269|PubMed:19704009}.
CC -!- SUBUNIT: Homo- and heterooligomer. Interacts with MTOR; controls MTOR-
CC dependent IGF2 expression during myoblast differentiation.
CC {ECO:0000269|PubMed:19704009}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope. Endoplasmic reticulum membrane.
CC Membrane; Multi-pass membrane protein. Note=Both the N- and C-terminal
CC are exposed to the cytoplasm/nucleoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and muscle.
CC {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19704009}.
CC -!- INDUCTION: Up-regulated during myoblast differentiation.
CC {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19704009}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AK052883; BAC35188.1; -; mRNA.
DR EMBL; AK134638; BAE22220.1; -; mRNA.
DR EMBL; BC016136; AAH16136.1; -; mRNA.
DR CCDS; CCDS15906.1; -.
DR RefSeq; NP_663496.1; NM_145521.3.
DR AlphaFoldDB; Q91WB2; -.
DR SMR; Q91WB2; -.
DR STRING; 10090.ENSMUSP00000054337; -.
DR iPTMnet; Q91WB2; -.
DR PhosphoSitePlus; Q91WB2; -.
DR jPOST; Q91WB2; -.
DR PaxDb; Q91WB2; -.
DR PeptideAtlas; Q91WB2; -.
DR PRIDE; Q91WB2; -.
DR ProteomicsDB; 289452; -.
DR Antibodypedia; 45196; 109 antibodies from 27 providers.
DR DNASU; 227721; -.
DR Ensembl; ENSMUST00000057423; ENSMUSP00000054337; ENSMUSG00000051373.
DR GeneID; 227721; -.
DR KEGG; mmu:227721; -.
DR UCSC; uc008jel.1; mouse.
DR CTD; 84814; -.
DR MGI; MGI:2445183; Plpp7.
DR VEuPathDB; HostDB:ENSMUSG00000051373; -.
DR eggNOG; KOG4268; Eukaryota.
DR GeneTree; ENSGT00940000157147; -.
DR HOGENOM; CLU_072573_4_0_1; -.
DR InParanoid; Q91WB2; -.
DR OMA; MFHFSLM; -.
DR OrthoDB; 1356295at2759; -.
DR PhylomeDB; Q91WB2; -.
DR TreeFam; TF323272; -.
DR BioGRID-ORCS; 227721; 1 hit in 44 CRISPR screens.
DR PRO; PR:Q91WB2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91WB2; protein.
DR Bgee; ENSMUSG00000051373; Expressed in triceps brachii and 156 other tissues.
DR ExpressionAtlas; Q91WB2; baseline and differential.
DR Genevisible; Q91WB2; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; IMP:MGI.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..271
FT /note="Inactive phospholipid phosphatase 7"
FT /id="PRO_0000239402"
FT TOPO_DOM 1..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..91
FT /note="Interaction with MTOR"
FT /evidence="ECO:0000269|PubMed:19704009"
FT COMPBIAS 19..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 271 AA; 29710 MW; 91595666F0BF0508 CRC64;
MPASQSRARA RDRNNVLNRA EFLSLNQPPK GTQEPRSSGR KASGPSTQPP PSSDGARERR
QSQQLPEEDC MQLNPSFKGI AFNSLLAIDI CMSKRLGVCA GRAASWASAR SMVKLIGITG
HGIPWIGGTI LCLVRSSTLA GQEVLMNLLL ALLLDIMTVA GVQKLIKRRG PYETSPGLLD
YLTMDIYAFP AGHASRAAMV SKFFLSHLVL AVPLRVLLVL WAFCVGLSRV MIGRHHITDV
ISGFIIGYFQ FRLVELVWMS SNTCQMLISA W
