PLPR5_HUMAN
ID PLPR5_HUMAN Reviewed; 321 AA.
AC Q32ZL2; A8MPX4; B7UCH3; Q32ZD0; Q3ZCU7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Phospholipid phosphatase-related protein type 5 {ECO:0000305};
DE AltName: Full=Lipid phosphate phosphatase-related protein type 5 {ECO:0000305};
DE AltName: Full=Phosphatidic acid phosphatase type 2d {ECO:0000303|PubMed:16010976};
DE AltName: Full=Plasticity-related gene 5 protein {ECO:0000305|PubMed:20032306};
DE Short=PRG-5;
GN Name=PLPPR5 {ECO:0000312|HGNC:HGNC:31703};
GN Synonyms=LPPR5 {ECO:0000312|HGNC:HGNC:31703},
GN PAP2D {ECO:0000303|PubMed:16010976}, PRG5 {ECO:0000303|PubMed:20032306};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=16010976; DOI=10.1007/s11010-005-7640-6;
RA Sun L., Gu S., Sun Y., Zheng D., Wu Q., Li X., Dai J., Dai J., Ji C.,
RA Xie Y., Mao Y.;
RT "Cloning and characterization of a novel human phosphatidic acid
RT phosphatase type 2, PAP2d, with two different transcripts PAP2d_v1 and
RT PAP2d_v2.";
RL Mol. Cell. Biochem. 272:91-96(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
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:0000250|UniProtKB:Q8BJ52}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BJ52};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PAP2d_v1;
CC IsoId=Q32ZL2-1; Sequence=Displayed;
CC Name=2; Synonyms=PAP2d_v2;
CC IsoId=Q32ZL2-2; Sequence=VSP_031828;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain, lung, kidney and
CC colon. Isoform 2 is expressed in placenta, skeletal muscle and kidney.
CC {ECO:0000269|PubMed:16010976}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH40174.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY574039; AAS76645.1; -; mRNA.
DR EMBL; AY634620; AAT64918.1; -; mRNA.
DR EMBL; FJ472844; ACJ60628.1; -; mRNA.
DR EMBL; AL445433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW72994.1; -; Genomic_DNA.
DR EMBL; BC040174; AAH40174.1; ALT_INIT; mRNA.
DR EMBL; BC136350; AAI36351.1; -; mRNA.
DR EMBL; BC144000; AAI44001.1; -; mRNA.
DR CCDS; CCDS30778.1; -. [Q32ZL2-1]
DR CCDS; CCDS30779.1; -. [Q32ZL2-2]
DR RefSeq; NP_001010861.1; NM_001010861.2. [Q32ZL2-2]
DR RefSeq; NP_001032394.1; NM_001037317.1. [Q32ZL2-1]
DR AlphaFoldDB; Q32ZL2; -.
DR STRING; 9606.ENSP00000263177; -.
DR DEPOD; PLPPR5; -.
DR iPTMnet; Q32ZL2; -.
DR PhosphoSitePlus; Q32ZL2; -.
DR BioMuta; PLPPR5; -.
DR DMDM; 172046620; -.
DR PaxDb; Q32ZL2; -.
DR PeptideAtlas; Q32ZL2; -.
DR PRIDE; Q32ZL2; -.
DR ProteomicsDB; 61633; -. [Q32ZL2-1]
DR Antibodypedia; 19967; 120 antibodies from 19 providers.
DR DNASU; 163404; -.
DR Ensembl; ENST00000263177.5; ENSP00000263177.4; ENSG00000117598.13. [Q32ZL2-1]
DR Ensembl; ENST00000370188.7; ENSP00000359207.3; ENSG00000117598.13. [Q32ZL2-2]
DR GeneID; 163404; -.
DR KEGG; hsa:163404; -.
DR MANE-Select; ENST00000263177.5; ENSP00000263177.4; NM_001037317.2; NP_001032394.1.
DR UCSC; uc001dsb.4; human. [Q32ZL2-1]
DR CTD; 163404; -.
DR DisGeNET; 163404; -.
DR GeneCards; PLPPR5; -.
DR HGNC; HGNC:31703; PLPPR5.
DR HPA; ENSG00000117598; Tissue enhanced (brain, retina, testis).
DR neXtProt; NX_Q32ZL2; -.
DR OpenTargets; ENSG00000117598; -.
DR VEuPathDB; HostDB:ENSG00000117598; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000158610; -.
DR InParanoid; Q32ZL2; -.
DR OMA; TAYTKPY; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q32ZL2; -.
DR BRENDA; 3.1.3.4; 2681.
DR PathwayCommons; Q32ZL2; -.
DR Reactome; R-HSA-419408; Lysosphingolipid and LPA receptors.
DR BioGRID-ORCS; 163404; 10 hits in 1030 CRISPR screens.
DR ChiTaRS; PLPPR5; human.
DR GenomeRNAi; 163404; -.
DR Pharos; Q32ZL2; Tdark.
DR PRO; PR:Q32ZL2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q32ZL2; protein.
DR Bgee; ENSG00000117598; Expressed in cortical plate and 78 other tissues.
DR ExpressionAtlas; Q32ZL2; baseline and differential.
DR Genevisible; Q32ZL2; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS: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_0000321933"
FT TRANSMEM 10..30
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:16010976"
FT /id="VSP_031828"
SQ SEQUENCE 321 AA; 35427 MW; 2B1915ED740EE572 CRC64;
MPLLPAALTS SMLYFQMVIM AGTVMLAYYF EYTDTFTVNV QGFFCHDSAY RKPYPGPEDS
SAVPPVLLYS LAAGVPVLVI IVGETAVFCL QLATRDFENQ EKTILTGDCC YINPLVRRTV
RFLGIYTFGL FATDIFVNAG QVVTGNLAPH FLALCKPNYT ALGCQQYTQF ISGEEACTGN
PDLIMRARKT FPSKEAALSV YAAMYLTMYI TNTIKAKGTR LAKPVLCLGL MCLAFLTGLN
RVAEYRNHWS DVIAGFLVGI SIAVFLVVCV VNNFKGRQAE NEHIHMDNLA QMPMISIPRV
ESPLEKVTSV QNHITAFAEV T
