PLPR5_MOUSE
ID PLPR5_MOUSE Reviewed; 321 AA.
AC Q8BJ52; Q8BIL7; Q8K0B6; Q9D606;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phospholipid phosphatase-related protein type 5 {ECO:0000250|UniProtKB:Q32ZL2};
DE AltName: Full=Lipid phosphate phosphatase-related protein type 5 {ECO:0000250|UniProtKB:Q32ZL2};
DE AltName: Full=Plasticity-related gene 5 protein {ECO:0000305|PubMed:20032306};
DE Short=PRG-5;
GN Name=Plppr5 {ECO:0000312|MGI:MGI:1923019};
GN Synonyms=Lppr5 {ECO:0000312|MGI:MGI:1923019};
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), FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=20032306; DOI=10.1091/mbc.e09-06-0506;
RA Broggini T., Nitsch R., Savaskan N.E.;
RT "Plasticity-related gene 5 (PRG5) induces filopodia and neurite growth and
RT impedes lysophosphatidic acid- and nogo-A-mediated axonal retraction.";
RL Mol. Biol. Cell 21:521-537(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Head, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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: Induces filopodia formation and promotes neurite growth in a
CC CDC42-independent manner; impedes neurite growth inhibitory-mediated
CC axonal retraction. {ECO:0000269|PubMed:20032306}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20032306};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BJ52-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJ52-2; Sequence=VSP_031829;
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- CAUTION: Has most probably no lipid phosphatase activity (By
CC similarity). Critical residues that support the reaction mechanism in
CC active members of that protein family, including the residues of the
CC active site acting respectively as proton donor and nucleophile, are
CC not conserved. {ECO:0000250|UniProtKB:Q6WAY2, ECO:0000305}.
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DR EMBL; AY512657; AAS80161.1; -; mRNA.
DR EMBL; AK014763; BAB29538.1; -; mRNA.
DR EMBL; AK032034; BAC27663.1; -; mRNA.
DR EMBL; AK043629; BAC31601.1; -; mRNA.
DR EMBL; BC031879; AAH31879.1; -; mRNA.
DR CCDS; CCDS17796.1; -. [Q8BJ52-2]
DR CCDS; CCDS80009.1; -. [Q8BJ52-1]
DR RefSeq; NP_001292380.1; NM_001305451.1. [Q8BJ52-1]
DR RefSeq; NP_083701.2; NM_029425.3. [Q8BJ52-2]
DR AlphaFoldDB; Q8BJ52; -.
DR STRING; 10090.ENSMUSP00000045121; -.
DR iPTMnet; Q8BJ52; -.
DR PhosphoSitePlus; Q8BJ52; -.
DR SwissPalm; Q8BJ52; -.
DR PaxDb; Q8BJ52; -.
DR PRIDE; Q8BJ52; -.
DR ProteomicsDB; 289694; -. [Q8BJ52-1]
DR ProteomicsDB; 289695; -. [Q8BJ52-2]
DR Antibodypedia; 19967; 120 antibodies from 19 providers.
DR DNASU; 75769; -.
DR Ensembl; ENSMUST00000039564; ENSMUSP00000045121; ENSMUSG00000033342. [Q8BJ52-2]
DR Ensembl; ENSMUST00000106473; ENSMUSP00000102081; ENSMUSG00000033342. [Q8BJ52-1]
DR GeneID; 75769; -.
DR KEGG; mmu:75769; -.
DR UCSC; uc008rda.3; mouse. [Q8BJ52-2]
DR UCSC; uc008rdb.3; mouse. [Q8BJ52-1]
DR CTD; 163404; -.
DR MGI; MGI:1923019; Plppr5.
DR VEuPathDB; HostDB:ENSMUSG00000033342; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000158610; -.
DR HOGENOM; CLU_021458_1_0_1; -.
DR InParanoid; Q8BJ52; -.
DR OMA; TAYTKPY; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q8BJ52; -.
DR TreeFam; TF316040; -.
DR BioGRID-ORCS; 75769; 3 hits in 27 CRISPR screens.
DR PRO; PR:Q8BJ52; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BJ52; protein.
DR Bgee; ENSMUSG00000033342; Expressed in lumbar subsegment of spinal cord and 94 other tissues.
DR ExpressionAtlas; Q8BJ52; baseline and differential.
DR Genevisible; Q8BJ52; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR028680; LPPR5.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR PANTHER; PTHR10165:SF17; PTHR10165:SF17; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..321
FT /note="Phospholipid phosphatase-related protein type 5"
FT /id="PRO_0000321934"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 307..311
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031829"
FT CONFLICT 68
FT /note="L -> P (in Ref. 2; BAC31601)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="L -> F (in Ref. 3; AAH31879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35388 MW; 3217E919E56E913D CRC64;
MPLLPVALIS SMLYFQMVIM AGTVMLAYYF EYTDTFTVNV QGFFCHDSAY RKPYPGPEDS
SAVPPVLLYS LAAGVPVLVI IVGETAVFCL QLATRDFENQ EKTILTGDCC YINPLVRRTV
RFLGIYAFGL FATDIFVNAG QVVTGNLAPH FLALCKPNYT ALGCQQYTQF ISGEEACTGN
PDLIMRARKT FPSKEAALSV YAATYLTMYI TSTIKAKGTR LAKPVLCLGL MCLAFLTGLN
RVAEYRNHWS DVIAGFLVGI SIAVFLVVCV VNNFKGRQPE NGHIHRDNVA RMPMTNIPRV
ESPLEKVTSL QNHVTAFAEV T
