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PLPR5_XENLA
ID   PLPR5_XENLA             Reviewed;         314 AA.
AC   Q6GM05;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 70.
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};
GN   Name=plppr5 {ECO:0000250|UniProtKB:Q32ZL2}; Synonyms=lppr5;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Induces filopodia formation and promotes neurite growth.
CC       {ECO:0000250|UniProtKB:Q8BJ52}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BJ52};
CC       Multi-pass membrane protein {ECO:0000255}.
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=AAH74287.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC074287; AAH74287.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001086172.1; NM_001092703.1.
DR   AlphaFoldDB; Q6GM05; -.
DR   DNASU; 444601; -.
DR   GeneID; 444601; -.
DR   KEGG; xla:444601; -.
DR   CTD; 444601; -.
DR   OMA; QPENEHV; -.
DR   OrthoDB; 1621899at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 444601; Expressed in brain and 2 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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   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   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..314
FT                   /note="Phospholipid phosphatase-related protein type 5"
FT                   /id="PRO_0000321935"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   314 AA;  34979 MW;  4CE3F1E16D0C4A95 CRC64;
     MSFQFSLTIM LYFQMVIMAG TVMLAYYFEY TDTFTVNVQG FFCYDSSYTK PYPGPDESSD
     IPPVLLLSLV TGVPVLVIIV GETVVFCLQV ATRDFENQEK TLLTGDCCYI NPLVRRTVRF
     LGIYTFGLFA TDIFVNAGQV VTGNLAPHFL TVCKPNYTAL GCRQFTQFIT DANACTGIPD
     LVIKARRTFP SKDAALSVYA ALYLAMYITS TIKAKGTRLA KPVLCLGLMC LAFLTGINRV
     AEYRNHWSDV IAGFLIGISI AVFLVVCVVN NFKGRRTEHE HWPTENLAQM PIISIPRVEN
     PLEKNHLTAF AEVT
 
 
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