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Inactive phospholipase C-like protein 1 (PLC-L1) (Phospholipase C-deleted in lung carcinoma) (Phospholipase C-related but catalytically inactive protein) (PRIP)

 PLCL1_HUMAN             Reviewed;        1095 AA.
Q15111; Q3MJ90; Q53SD3; Q7Z3S3;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
14-APR-2009, sequence version 3.
22-NOV-2017, entry version 147.
RecName: Full=Inactive phospholipase C-like protein 1;
Short=PLC-L1;
AltName: Full=Phospholipase C-deleted in lung carcinoma;
AltName: Full=Phospholipase C-related but catalytically inactive protein;
Short=PRIP;
Name=PLCL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=7633416; DOI=10.1093/hmg/4.4.667;
Kohno T., Otsuka T., Takano H., Yamamoto T., Hamaguchi M., Terada M.,
Yokota J.;
"Identification of a novel phospholipase C family gene at chromosome
2q33 that is homozygously deleted in human small cell lung
carcinoma.";
Hum. Mol. Genet. 4:667-674(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ILE-667.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 741-1095.
TISSUE=Rectum tumor;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
INTERACTION WITH PPP1C.
PubMed=11278544; DOI=10.1074/jbc.M009677200;
Yoshimura K., Takeuchi H., Sato O., Hidaka K., Doira N., Terunuma M.,
Harada K., Ogawa Y., Ito Y., Kanematsu T., Hirata M.;
"Interaction of p130 with, and consequent inhibition of, the catalytic
subunit of protein phosphatase 1alpha.";
J. Biol. Chem. 276:17908-17913(2001).
[6]
INTERACTION WITH GABARAP AND PPP1C.
PubMed=11867528; DOI=10.1093/emboj/21.5.1004;
Kanematsu T., Jang I.S., Yamaguchi T., Nagahama H., Yoshimura K.,
Hidaka K., Matsuda M., Takeuchi H., Misumi Y., Nakayama K.,
Yamamoto T., Akaike N., Hirata M., Nakayama K.;
"Role of the PLC-related, catalytically inactive protein p130 in
GABA(A) receptor function.";
EMBO J. 21:1004-1011(2002).
[7]
INTERACTION WITH PPP1C; GABA A RECEPTOR SUBUNIT BETA; GABA A RECEPTOR
AND SUBUNIT GAMMA-2.
PubMed=16404143;
Kanematsu T., Takeuchi H., Terunuma M., Hirata M.;
"PRIP, a novel Ins(1,4,5)P3 binding protein, functional significance
in Ca2+ signaling and extension to neuroscience and beyond.";
Mol. Cells 20:305-314(2005).
[8]
INTERACTION WITH PPP1C.
PubMed=16854455; DOI=10.1016/j.advenzreg.2006.01.006;
Yanagihori S., Terunuma M., Koyano K., Kanematsu T., Ho Ryu S.,
Hirata M.;
"Protein phosphatase regulation by PRIP, a PLC-related catalytically
inactive protein -- implications in the phospho-modulation of the
GABAA receptor.";
Adv. Enzyme Regul. 46:203-222(2006).
[9]
TISSUE SPECIFICITY.
PubMed=16952428; DOI=10.1016/j.gene.2006.07.005;
Murakami A., Matsuda M., Nakasima A., Hirata M.;
"Characterization of the human PRIP-1 gene structure and
transcriptional regulation.";
Gene 382:129-139(2006).
[10]
INTERACTION WITH GABA A RECEPTOR.
PubMed=16754670; DOI=10.1074/jbc.M603118200;
Jovanovic J.N., Takenaka K., Nakayama K.I., Fukami K., Takenawa T.,
Moss S.J., Nabekura J., Hirata M.;
"Modulation of GABA(A) receptor phosphorylation and membrane
trafficking by phospholipase C-related inactive protein/protein
phosphatase 1 and 2A signaling complex underlying brain-derived
neurotrophic factor-dependent regulation of GABAergic inhibition.";
J. Biol. Chem. 281:22180-22189(2006).
[11]
FUNCTION.
PubMed=17254016; DOI=10.1111/j.1471-4159.2006.04399.x;
Kanematsu T., Fujii M., Mizokami A., Kittler J.T., Nabekura J.,
Moss S.J., Hirata M.;
"Phospholipase C-related inactive protein is implicated in the
constitutive internalization of GABAA receptors mediated by clathrin
and AP2 adaptor complex.";
J. Neurochem. 101:898-905(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-95, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Involved in an inositol phospholipid-based intracellular
signaling cascade. Shows no PLC activity to phosphatidylinositol
4,5-bisphosphate and phosphatidylinositol. Component in the
phospho-dependent endocytosis process of GABA A receptor (By
similarity). Regulates the turnover of receptors and thus
contributes to the maintenance of GABA-mediated synaptic
inhibition. Its aberrant expression could contribute to the
genesis and progression of lung carcinoma. Acts as an inhibitor of
PPP1C. {ECO:0000250, ECO:0000269|PubMed:17254016}.
-!- SUBUNIT: Interacts with PPP2CA (By similarity). Interacts with
Ins(1,4,5)P3, Ins(1,4,5,6)P4, GABARAP, GABA receptor beta
subunits, GABA receptor gamma-2 subunits and PPP1C. May form a
ternary complex with GABA receptor beta subunit and GABARAP. The
formation of a ternary complex with GABA receptor beta subunit and
GABARAP could be the key step for facilitating the association of
GABARAP with the GABA receptor gamma-2 subunit and to allow it to
be transported at the right destination. {ECO:0000250,
ECO:0000269|PubMed:11278544, ECO:0000269|PubMed:11867528,
ECO:0000269|PubMed:16404143, ECO:0000269|PubMed:16754670,
ECO:0000269|PubMed:16854455}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15111-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q15111-2; Sequence=VSP_031475;
-!- TISSUE SPECIFICITY: Expressed in a variety of fetal and adult
organs including brain, lung and kidney. Its expression was
greatly reduced in small and non-small cell lung carcinoma.
Isoform 1 is predominantly expressed in brain.
{ECO:0000269|PubMed:16952428, ECO:0000269|PubMed:7633416}.
-!- PTM: Phosphorylated by the catalytic subunit of PKA.
Phosphorylation of Thr-93 resulted in dissociation of PPP1C from
PRIP1 (By similarity). {ECO:0000250}.
-!- CAUTION: In the PI-PLC X-box Asn-458 is present instead of the
conserved His which is one of the active site residues. It is
therefore expected that this protein lacks catalytic activity.
{ECO:0000305}.
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EMBL; D42108; BAA07688.1; -; mRNA.
EMBL; AC011997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC013478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC020719; AAY14733.1; -; Genomic_DNA.
EMBL; BC101531; AAI01532.1; -; mRNA.
EMBL; BC111985; AAI11986.1; -; mRNA.
EMBL; BX537442; CAD97684.1; -; mRNA.
CCDS; CCDS2326.2; -. [Q15111-1]
PIR; I54390; I54390.
RefSeq; NP_006217.3; NM_006226.3. [Q15111-1]
RefSeq; XP_016859829.1; XM_017004340.1. [Q15111-2]
UniGene; Hs.153322; -.
ProteinModelPortal; Q15111; -.
SMR; Q15111; -.
STRING; 9606.ENSP00000402861; -.
DrugBank; DB01103; Quinacrine.
iPTMnet; Q15111; -.
PhosphoSitePlus; Q15111; -.
BioMuta; PLCL1; -.
DMDM; 226694170; -.
MaxQB; Q15111; -.
PaxDb; Q15111; -.
PeptideAtlas; Q15111; -.
PRIDE; Q15111; -.
Ensembl; ENST00000428675; ENSP00000402861; ENSG00000115896. [Q15111-1]
GeneID; 5334; -.
KEGG; hsa:5334; -.
UCSC; uc010fsp.4; human. [Q15111-1]
CTD; 5334; -.
DisGeNET; 5334; -.
EuPathDB; HostDB:ENSG00000115896.15; -.
GeneCards; PLCL1; -.
H-InvDB; HIX0023967; -.
HGNC; HGNC:9063; PLCL1.
HPA; HPA031849; -.
MIM; 600597; gene.
neXtProt; NX_Q15111; -.
OpenTargets; ENSG00000115896; -.
PharmGKB; PA33394; -.
eggNOG; KOG0169; Eukaryota.
eggNOG; ENOG410XPSW; LUCA.
GeneTree; ENSGT00760000118936; -.
HOGENOM; HOG000006871; -.
InParanoid; Q15111; -.
KO; K15375; -.
OMA; NQKCGGR; -.
OrthoDB; EOG091G00S7; -.
PhylomeDB; Q15111; -.
TreeFam; TF313216; -.
BRENDA; 2.7.11.10; 2681.
ChiTaRS; PLCL1; human.
GenomeRNAi; 5334; -.
PRO; PR:Q15111; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115896; -.
CleanEx; HS_PLCL1; -.
ExpressionAtlas; Q15111; baseline and differential.
Genevisible; Q15111; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0050811; F:GABA receptor binding; IEA:InterPro.
GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:InterPro.
GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
GO; GO:0004629; F:phospholipase C activity; TAS:ProtInc.
GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
GO; GO:1900122; P:positive regulation of receptor binding; IEA:Ensembl.
GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 2.60.40.150; -; 1.
Gene3D; 3.20.20.190; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR001192; PI-PLC_fam.
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
InterPro; IPR015359; PLC_EF-hand-like.
InterPro; IPR028382; PLCL1/PLCL2.
InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
PANTHER; PTHR10336; PTHR10336; 1.
PANTHER; PTHR10336:SF84; PTHR10336:SF84; 1.
Pfam; PF00168; C2; 1.
Pfam; PF09279; EF-hand_like; 1.
Pfam; PF16457; PH_12; 1.
Pfam; PF00388; PI-PLC-X; 1.
Pfam; PF00387; PI-PLC-Y; 1.
PRINTS; PR00390; PHPHLIPASEC.
SMART; SM00239; C2; 1.
SMART; SM00233; PH; 1.
SMART; SM00148; PLCXc; 1.
SMART; SM00149; PLCYc; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF51695; SSF51695; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Phosphoprotein; Polymorphism; Reference proteome; Transducer.
CHAIN 1 1095 Inactive phospholipase C-like protein 1.
/FTId=PRO_0000319414.
DOMAIN 113 223 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 398 542 PI-PLC X-box. {ECO:0000255|PROSITE-
ProRule:PRU00270}.
DOMAIN 585 701 PI-PLC Y-box. {ECO:0000255|PROSITE-
ProRule:PRU00271}.
DOMAIN 708 813 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
REGION 83 222 Interaction with PPP1C.
REGION 543 567 Interaction with GABA A beta subunit.
{ECO:0000250}.
COILED 894 914 {ECO:0000255}.
COILED 1034 1059 {ECO:0000255}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000250|UniProtKB:Q3USB7}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 93 93 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:Q3USB7}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 556 556 Phosphothreonine.
{ECO:0000250|UniProtKB:Q3USB7}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000250|UniProtKB:Q62688}.
MOD_RES 1079 1079 Phosphoserine.
{ECO:0000250|UniProtKB:Q62688}.
VAR_SEQ 1 98 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7633416}.
/FTId=VSP_031475.
VARIANT 445 445 D -> N (in dbSNP:rs45506698).
/FTId=VAR_038993.
VARIANT 454 454 P -> S (in dbSNP:rs45506696).
/FTId=VAR_038994.
VARIANT 546 546 S -> F (in dbSNP:rs45596936).
/FTId=VAR_038995.
VARIANT 667 667 V -> I (in dbSNP:rs1064213).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_038996.
VARIANT 684 684 W -> C (in dbSNP:rs6741084).
/FTId=VAR_038997.
VARIANT 937 937 S -> N (in dbSNP:rs45452996).
/FTId=VAR_038998.
CONFLICT 176 176 R -> T (in Ref. 1; BAA07688).
{ECO:0000305}.
CONFLICT 563 563 E -> Q (in Ref. 1; BAA07688).
{ECO:0000305}.
SEQUENCE 1095 AA; 122728 MW; C7B34D38C654E2D3 CRC64;
MAEGAAGRED PAPPDAAGGE DDPRVGPDAA GDCVTAASGG RMRDRRSGVA LPGAAGTPAD
SEAGLLEAAR ATPRRSSIIK DPSNQKCGGR KKTVSFSSMP SEKKISSAND CISFMQAGCE
LKKVRPNSRI YNRFFTLDTD LQALRWEPSK KDLEKAKLDI SAIKEIRLGK NTETFRNNGL
ADQICEDCAF SILHGENYES LDLVANSADV ANIWVSGLRY LVSRSKQPLD FMEGNQNTPR
FMWLKTVFEA ADVDGNGIML EDTSVELIKQ LNPTLKEAKI RLKFKEIQKS KEKLTTRVTE
EEFCEAFCEL CTRPEVYFLL VQISKNKEYL DANDLMLFLE AEQGVTHITE DICLDIIRRY
ELSEEGRQKG FLAIDGFTQY LLSSECDIFD PEQKKVAQDM TQPLSHYYIN ASHNTYLIED
QFRGPADING YIRALKMGCR SVELDVSDGS DNEPILCNRN NMTTHVSFRS VIEVINKFAF
VASEYPLILC LGNHCSLPQQ KVMAQQMKKV FGNKLYTEAP LPSESYLPSP EKLKRMIIVK
GKKLPSDPDV LEGEVTDEDE EAEMSRRMSV DYNGEQKQIR LCRELSDLVS ICKSVQYRDF
ELSMKSQNYW EMCSFSETEA SRIANEYPED FVNYNKKFLS RIYPSAMRID SSNLNPQDFW
NCGCQIVAMN FQTPGPMMDL HTGWFLQNGG CGYVLRPSIM RDEVSYFSAN TKGILPGVSP
LALHIKIISG QNFPKPKGAC AKGDVIDPYV CIEIHGIPAD CSEQRTKTVQ QNSDNPIFDE
TFEFQVNLPE LAMIRFVVLD DDYIGDEFIG QYTIPFECLQ PGYRHVPLRS FVGDIMEHVT
LFVHIAITNR SGGGKAQKRS LSVRMGKKVR EYTMLRNIGL KTIDDIFKIA VHPLREAIDM
RENMQNAIVS IKELCGLPPI ASLKQCLLTL SSRLITSDNT PSVSLVMKDS FPYLEPLGAI
PDVQKKMLTA YDLMIQESRF LIEMADTVQE KIVQCQKAGM EFHEELHNLG AKEGLKGRKL
NKATESFAWN ITVLKGQGDL LKNAKNEAIE NMKQIQLACL SCGLSKAPSS SAEAKSKRSL
EAIEEKESSE ENGKL


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