ID   PLPP7_RAT               Reviewed;         271 AA.
AC   Q5FVJ3;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Inactive phospholipid phosphatase 7 {ECO:0000312|RGD:1305821};
DE   AltName: Full=Phosphatidic acid phosphatase type 2 domain-containing protein 3;
GN   Name=Plpp7 {ECO:0000312|RGD:1305821}; Synonyms=Ppapdc3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homo- and heterooligomer. Interacts with MTOR; controls MTOR-
CC       dependent IGF2 expression during myoblast differentiation (By
CC       similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
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DR   EMBL; BC089948; AAH89948.1; -; mRNA.
DR   RefSeq; NP_001012349.1; NM_001012349.2.
DR   AlphaFoldDB; Q5FVJ3; -.
DR   SMR; Q5FVJ3; -.
DR   STRING; 10116.ENSRNOP00000013507; -.
DR   PaxDb; Q5FVJ3; -.
DR   PRIDE; Q5FVJ3; -.
DR   Ensembl; ENSRNOT00000013507; ENSRNOP00000013507; ENSRNOG00000010068.
DR   GeneID; 296635; -.
DR   KEGG; rno:296635; -.
DR   UCSC; RGD:1305821; rat.
DR   CTD; 84814; -.
DR   RGD; 1305821; Plpp7.
DR   eggNOG; KOG4268; Eukaryota.
DR   GeneTree; ENSGT00940000157147; -.
DR   HOGENOM; CLU_072573_4_0_1; -.
DR   InParanoid; Q5FVJ3; -.
DR   OMA; MFHFSLM; -.
DR   OrthoDB; 1356295at2759; -.
DR   PhylomeDB; Q5FVJ3; -.
DR   TreeFam; TF323272; -.
DR   PRO; PR:Q5FVJ3; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000010068; Expressed in skeletal muscle tissue and 20 other tissues.
DR   Genevisible; Q5FVJ3; RN.
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; ISO:RGD.
DR   GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0010832; P:negative regulation of myotube differentiation; ISO:RGD.
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   2: Evidence at transcript 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_0000239403"
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..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..91
FT                   /note="Interaction with MTOR"
FT                   /evidence="ECO:0000250"
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:0000250|UniProtKB:Q91WB2"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WB2"
SQ   SEQUENCE   271 AA;  29768 MW;  531FE032F4502353 CRC64;
     MPVSQSRARA RDRNNVLNRA EFLSLNQPPK GTQEPRSSGR KASGPSTQPP PSSDGARERR
     QSQQLPEEDC MQLNPSFKGI AFNSLLAIDI CMSKRLGVCA GRAASWASAR SMVKLIGITS
     HGIPWIGGTI LCLVRSSTLA GQEVLMNLLL ALLLDIMTVA GVQKLIKRRG PYETSPGLLD
     YLTMDIYAFP AGHASRAAMV SKFFLSHLVL AVPLRVLLVL WAFCVGLSRV MIGRHHITDV
     ISGFIIGYFQ FRLVELVWMS SNTCQMLISA W