GPCP1_MOUSE
ID GPCP1_MOUSE Reviewed; 675 AA.
AC Q8C0L9; A2AMD5; Q3TLV6; Q80TD5; Q8BKJ7; Q8BKW7; Q8CFW2; Q9D759;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glycerophosphocholine phosphodiesterase GPCPD1;
DE EC=3.1.4.2;
DE AltName: Full=Glycerophosphodiester phosphodiesterase 5;
DE AltName: Full=Preimplantation protein 4;
GN Name=Gpcpd1; Synonyms=Gde5, Kiaa1434, Prei4;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Embryonic spinal ganglion, Head, Mammary gland, and Tongue;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-611, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20576599; DOI=10.1074/jbc.m110.106708;
RA Okazaki Y., Ohshima N., Yoshizawa I., Kamei Y., Mariggio S., Okamoto K.,
RA Maeda M., Nogusa Y., Fujioka Y., Izumi T., Ogawa Y., Shiro Y., Wada M.,
RA Kato N., Corda D., Yanaka N.;
RT "A novel glycerophosphodiester phosphodiesterase, GDE5, controls skeletal
RT muscle development via a non-enzymatic mechanism.";
RL J. Biol. Chem. 285:27652-27663(2010).
CC -!- FUNCTION: May be involved in the negative regulation of skeletal muscle
CC differentiation, independently of its glycerophosphocholine
CC phosphodiesterase activity. {ECO:0000269|PubMed:20576599}.
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 Evidence={ECO:0000269|PubMed:20576599};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=2.0 umol/min/mg enzyme with glycerophosphocholine as substrate
CC {ECO:0000269|PubMed:20576599};
CC Vmax=0.34 umol/min/mg enzyme with glycerophosphoethanolamine as
CC substrate {ECO:0000269|PubMed:20576599};
CC Note=No significant reactions when glycerophosphoglycerol,
CC glycerophosphoinositol and glycerophosphoserine are used as
CC substrates.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20576599}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C0L9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0L9-2; Sequence=VSP_020820;
CC Name=3;
CC IsoId=Q8C0L9-3; Sequence=VSP_020819;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in skeletal
CC muscle and heart. {ECO:0000269|PubMed:20576599}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated in skeletal muscles atrophies,
CC including atrophies linked to aging and denervation.
CC {ECO:0000269|PubMed:20576599}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26361.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC33775.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC34739.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65792.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122510; BAC65792.1; ALT_INIT; mRNA.
DR EMBL; AK009563; BAB26361.2; ALT_INIT; mRNA.
DR EMBL; AK030645; BAC27063.1; -; mRNA.
DR EMBL; AK049491; BAC33775.1; ALT_INIT; mRNA.
DR EMBL; AK051728; BAC34739.1; ALT_INIT; mRNA.
DR EMBL; AK166293; BAE38686.1; -; mRNA.
DR EMBL; AL807386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033408; AAH33408.1; -; mRNA.
DR CCDS; CCDS38246.1; -. [Q8C0L9-1]
DR CCDS; CCDS71151.1; -. [Q8C0L9-2]
DR RefSeq; NP_001277979.1; NM_001291050.1. [Q8C0L9-2]
DR RefSeq; NP_001277980.1; NM_001291051.1. [Q8C0L9-2]
DR RefSeq; NP_001277981.1; NM_001291052.1. [Q8C0L9-2]
DR RefSeq; NP_081372.1; NM_027096.2. [Q8C0L9-2]
DR RefSeq; NP_083078.3; NM_028802.3. [Q8C0L9-1]
DR RefSeq; XP_011238111.1; XM_011239809.2.
DR RefSeq; XP_017174784.1; XM_017319295.1.
DR AlphaFoldDB; Q8C0L9; -.
DR SMR; Q8C0L9; -.
DR STRING; 10090.ENSMUSP00000105769; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR iPTMnet; Q8C0L9; -.
DR PhosphoSitePlus; Q8C0L9; -.
DR EPD; Q8C0L9; -.
DR jPOST; Q8C0L9; -.
DR MaxQB; Q8C0L9; -.
DR PaxDb; Q8C0L9; -.
DR PeptideAtlas; Q8C0L9; -.
DR PRIDE; Q8C0L9; -.
DR ProteomicsDB; 271434; -. [Q8C0L9-1]
DR ProteomicsDB; 271435; -. [Q8C0L9-2]
DR ProteomicsDB; 271436; -. [Q8C0L9-3]
DR Antibodypedia; 23917; 27 antibodies from 10 providers.
DR DNASU; 74182; -.
DR Ensembl; ENSMUST00000060955; ENSMUSP00000062221; ENSMUSG00000027346. [Q8C0L9-1]
DR Ensembl; ENSMUST00000110136; ENSMUSP00000105763; ENSMUSG00000027346. [Q8C0L9-2]
DR Ensembl; ENSMUST00000110142; ENSMUSP00000105769; ENSMUSG00000027346. [Q8C0L9-1]
DR GeneID; 74182; -.
DR KEGG; mmu:74182; -.
DR UCSC; uc008mmv.2; mouse. [Q8C0L9-1]
DR CTD; 56261; -.
DR MGI; MGI:104898; Gpcpd1.
DR VEuPathDB; HostDB:ENSMUSG00000027346; -.
DR eggNOG; KOG2421; Eukaryota.
DR GeneTree; ENSGT00440000033970; -.
DR HOGENOM; CLU_013007_2_0_1; -.
DR InParanoid; Q8C0L9; -.
DR OMA; YHTAEGL; -.
DR OrthoDB; 687958at2759; -.
DR PhylomeDB; Q8C0L9; -.
DR TreeFam; TF314722; -.
DR BioGRID-ORCS; 74182; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Gpcpd1; mouse.
DR PRO; PR:Q8C0L9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C0L9; protein.
DR Bgee; ENSMUSG00000027346; Expressed in triceps brachii and 256 other tissues.
DR ExpressionAtlas; Q8C0L9; baseline and differential.
DR Genevisible; Q8C0L9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0047389; F:glycerophosphocholine phosphodiesterase activity; IDA:MGI.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; TAS:Reactome.
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; IMP:MGI.
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 Alternative splicing; Cytoplasm; Hydrolase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..675
FT /note="Glycerophosphocholine phosphodiesterase GPCPD1"
FT /id="PRO_0000251947"
FT DOMAIN 1..115
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT DOMAIN 321..621
FT /note="GP-PDE"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 88..89
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPB8"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 611
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT VAR_SEQ 1..445
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_020819"
FT VAR_SEQ 1..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020820"
FT CONFLICT 289
FT /note="G -> D (in Ref. 2; BAE38686)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="E -> Q (in Ref. 2; BAC33775)"
FT /evidence="ECO:0000305"
FT CONFLICT 494..495
FT /note="LE -> SQ (in Ref. 2; BAC33775)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="K -> N (in Ref. 2; BAC33775)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="L -> S (in Ref. 2; BAB26361)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="K -> E (in Ref. 2; BAB26361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 76579 MW; 7ABF9EE48CF39B47 CRC64;
MTPSQVTFEI RGTLLPGEVF AICGSCDALG NWNPQNAVAL INENETGDSV LWKAVIALNR
GVSVKYRYFR GCFLEPKTIG GPCQVIVHKW ETHLQPRSIT PLESEIIIDD GQFGIHNGVE
TLDSGWLTCQ TEIRLRLHFS EKPPVSISKK KFKKSRFRVK LTLEGLEEDE DDDDDKVSPT
VLHKMSNSLE ISLISDNEFK CRHSQPECGY GLQPDRWTEY SIQTMEPDNL ELIFDFFEED
LSEHVVQGDV LPGHVGTACL LSSTIAESGR SAGILTLPIM SRNSRKTIGK VRVDFIIIKP
LPGYSCSMQS SFSKYWKPRI PLDVGHRGAG NSTTTAKLAK VQENTIASLR NAASHGAAFV
EFDVHLSKDF VPVVYHDLTC CLTMKRKYEA DPVELFEIPV KELTFDQLQL LKLSHVTALK
TKDRKQSLYE EENFFSENQP FPSLKMVLES LPENVGFNIE IKWICQHRDG VWDGNLSTYF
DMNVFLDIIL KTVLENSGKR RIVFSSFDAD ICTMVRQKQN KYPILFLTQG KSDIYPELMD
LRSRTTPIAM SFAQFENILG INAHTEDLLR NPSYVQEAKA KGLVIFCWGD DTNDPENRRK
LKEFGVNGLI YDRIYDWMPE QPNIFQVEQL ERLKQELPEL KNCLCPTVSH FIPSSFCVEP
DIHVDANGID SVENA
