ID   GPCP1_RAT               Reviewed;         672 AA.
AC   Q80VJ4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Glycerophosphocholine phosphodiesterase GPCPD1;
DE            EC=3.1.4.2;
DE   AltName: Full=Glycerophosphodiester phosphodiesterase 5;
GN   Name=Gpcpd1; Synonyms=Gde5;
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 [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain capillary;
RA   Li J.Y., Boado R.J., Pardridge W.M.;
RT   "Blood-brain barrier genomics.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: May be involved in the negative regulation of skeletal muscle
CC       differentiation, independently of its glycerophosphocholine
CC       phosphodiesterase activity. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + sn-glycerol 3-phosphocholine = choline + H(+) + sn-
CC         glycerol 3-phosphate; Xref=Rhea:RHEA:16061, ChEBI:CHEBI:15354,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:57597; EC=3.1.4.2;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC       family. {ECO:0000305}.
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DR   EMBL; AY233980; AAO84024.1; -; mRNA.
DR   RefSeq; NP_942074.1; NM_198779.1.
DR   AlphaFoldDB; Q80VJ4; -.
DR   SMR; Q80VJ4; -.
DR   STRING; 10116.ENSRNOP00000028890; -.
DR   BindingDB; Q80VJ4; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   iPTMnet; Q80VJ4; -.
DR   PhosphoSitePlus; Q80VJ4; -.
DR   PaxDb; Q80VJ4; -.
DR   GeneID; 362219; -.
DR   KEGG; rno:362219; -.
DR   UCSC; RGD:735140; rat.
DR   CTD; 56261; -.
DR   RGD; 735140; Gpcpd1.
DR   eggNOG; KOG2421; Eukaryota.
DR   InParanoid; Q80VJ4; -.
DR   OrthoDB; 687958at2759; -.
DR   PhylomeDB; Q80VJ4; -.
DR   PRO; PR:Q80VJ4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0047389; F:glycerophosphocholine phosphodiesterase activity; ISO:RGD.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR   GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR   CDD; cd05814; CBM20_Prei4; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR034839; CBM20_GPCPD1.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR033506; Gde1.
DR   InterPro; IPR030395; GP_PDE_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   PANTHER; PTHR22958:SF1; PTHR22958:SF1; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF03009; GDPD; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
DR   SUPFAM; SSF51695; SSF51695; 1.
DR   PROSITE; PS51166; CBM20; 1.
DR   PROSITE; PS51704; GP_PDE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..672
FT                   /note="Glycerophosphocholine phosphodiesterase GPCPD1"
FT                   /id="PRO_0000251948"
FT   DOMAIN          1..113
FT                   /note="CBM20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   DOMAIN          318..618
FT                   /note="GP-PDE"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         86..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         608
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C0L9"
SQ   SEQUENCE   672 AA;  76269 MW;  096E1F2BCF382858 CRC64;
     MTPSQVTFEI RGTLLPGEVF AMCGNCDALG NWSPQNAVPL TESETGESVW KAVIVLSRGM
     SVKYRYFRGC FLEPKTIGGP CQVIVHKWET HLQPRSITPL ENEIIIDDGQ FGIHNGVETL
     DSGWLTCQTE IRLRLHFSEK PPVSITKKKF KKSRFRVKLT LEGLEEDDDD DDKASPTVLH
     KMSNSLEISL ISDNEFKCRH SQPECGYGLQ PDRWTEYSIQ TMEPDNLELI FDFFEEDLSE
     HVVQGDVLPG HVGTACLLSS TIAESERSAG ILTLPIMSRS SRKTIGKVRV DFIIIKPLPG
     YSCSMQSSFS KYWKPRIPLD VGHRGAGNST TTAKLAKVQE NTIASLRNAA SHGAAFVEFD
     VHLSKDLVPV VYHDLTCCLT MKRKYEADPV ELFEIPVKEL TFDQLQLLKL SHVTALKTKD
     QKQCMAEEEN SFSENQPFPS LKMVLESLPE NVGFNIEIKW ICQHRDGVWD GNLSTYFDMN
     AFLDIILKTV LENSGKRRIV FSSFDADICT MVRQKQNKYP ILFLTQGKSD IYPELMDLRS
     RTTPIAMSFA QFENILGINA HTEDLLRNPS YVQEAKDKGL VIFCWGDDTN DPENRRKLKE
     FGVNGLIYDR IYDWMPEQPN IFQVEQLERL KRELPELKNC LCPTVSHFIP PSFCMESKIH
     VDANGIDNVE NA