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