PLCL1_MOUSE
ID PLCL1_MOUSE Reviewed; 1096 AA.
AC Q3USB7; D3Z0W5; Q3TSM9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Inactive phospholipase C-like protein 1;
DE Short=PLC-L1;
DE AltName: Full=Phospholipase C-related but catalytically inactive protein;
DE Short=PRIP;
GN Name=Plcl1;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
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 [2]
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 [3]
RP PHOSPHORYLATION AT THR-94 AND SER-96, AND MUTAGENESIS OF THR-94 AND SER-96.
RX PubMed=15306641; DOI=10.1523/jneurosci.1323-04.2004;
RA Terunuma M., Jang I.S., Ha S.H., Kittler J.T., Kanematsu T.,
RA Jovanovic J.N., Nakayama K.I., Akaike N., Ryu S.H., Moss S.J., Hirata M.;
RT "GABAA receptor phospho-dependent modulation is regulated by phospholipase
RT C-related inactive protein type 1, a novel protein phosphatase 1 anchoring
RT protein.";
RL J. Neurosci. 24:7074-7084(2004).
RN [4]
RP FUNCTION.
RX PubMed=16854455; DOI=10.1016/j.advenzreg.2006.01.006;
RA Yanagihori S., Terunuma M., Koyano K., Kanematsu T., Ho Ryu S., Hirata M.;
RT "Protein phosphatase regulation by PRIP, a PLC-related catalytically
RT inactive protein -- implications in the phospho-modulation of the GABAA
RT receptor.";
RL Adv. Enzyme Regul. 46:203-222(2006).
RN [5]
RP FUNCTION.
RX PubMed=17301177; DOI=10.1523/jneurosci.3155-06.2007;
RA Mizokami A., Kanematsu T., Ishibashi H., Yamaguchi T., Tanida I.,
RA Takenaka K., Nakayama K.I., Fukami K., Takenawa T., Kominami E., Moss S.J.,
RA Yamamoto T., Nabekura J., Hirata M.;
RT "Phospholipase C-related inactive protein is involved in trafficking of
RT gamma2 subunit-containing GABA(A) receptors to the cell surface.";
RL J. Neurosci. 27:1692-1701(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-94 AND THR-557, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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).
CC -!- FUNCTION: Involved in an inositol phospholipid-based intracellular
CC signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-
CC bisphosphate and phosphatidylinositol. Component in the phospho-
CC dependent endocytosis process of GABA A receptor. Acts as an inhibitor
CC of PPP1C (By similarity). Involved in the assembly and/or the
CC trafficking of gamma-2 subunit-containing GABA A receptors.
CC {ECO:0000250, ECO:0000269|PubMed:16854455,
CC ECO:0000269|PubMed:17301177}.
CC -!- SUBUNIT: Interacts with PPP2CA, Ins(1,4,5)P3, Ins(1,4,5,6)P4 GABARAP,
CC GABA receptor beta subunits, GABA receptor gamma-2 subunits and PPP1C
CC (By similarity). May form a ternary complex with GABA receptor beta
CC subunit and GABARAP. The formation of a ternary complex with GABA
CC receptor beta subunit and GABARAP could be the key step for
CC facilitating the association of GABARAP with the GABA receptor gamma-2
CC subunit and to allow it to be transported at the right destination.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated by the catalytic subunit of PKA. Phosphorylation of
CC Thr-94 resulted in dissociation of PPP1C from PRIP1.
CC {ECO:0000269|PubMed:15306641}.
CC -!- CAUTION: In the PI-PLC X-box Asn-459 is present instead of the
CC conserved His which is one of the active site residues. It is therefore
CC expected that this protein lacks catalytic activity. {ECO:0000305}.
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DR EMBL; AK140530; BAE24416.1; -; mRNA.
DR EMBL; AK161943; BAE36646.1; -; mRNA.
DR EMBL; AC099696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC145691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48263.1; -.
DR RefSeq; NP_001108135.1; NM_001114663.1.
DR AlphaFoldDB; Q3USB7; -.
DR SMR; Q3USB7; -.
DR BioGRID; 230595; 2.
DR IntAct; Q3USB7; 2.
DR MINT; Q3USB7; -.
DR STRING; 10090.ENSMUSP00000037854; -.
DR iPTMnet; Q3USB7; -.
DR PhosphoSitePlus; Q3USB7; -.
DR SwissPalm; Q3USB7; -.
DR EPD; Q3USB7; -.
DR jPOST; Q3USB7; -.
DR MaxQB; Q3USB7; -.
DR PaxDb; Q3USB7; -.
DR PeptideAtlas; Q3USB7; -.
DR PRIDE; Q3USB7; -.
DR ProteomicsDB; 289616; -.
DR Antibodypedia; 34073; 156 antibodies from 24 providers.
DR DNASU; 227120; -.
DR Ensembl; ENSMUST00000042986; ENSMUSP00000037854; ENSMUSG00000038349.
DR GeneID; 227120; -.
DR KEGG; mmu:227120; -.
DR UCSC; uc007ban.2; mouse.
DR CTD; 5334; -.
DR MGI; MGI:3036262; Plcl1.
DR VEuPathDB; HostDB:ENSMUSG00000038349; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000158407; -.
DR HOGENOM; CLU_002738_0_1_1; -.
DR InParanoid; Q3USB7; -.
DR OMA; CNRNSMT; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q3USB7; -.
DR TreeFam; TF313216; -.
DR BioGRID-ORCS; 227120; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Plcl1; mouse.
DR PRO; PR:Q3USB7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3USB7; protein.
DR Bgee; ENSMUSG00000038349; Expressed in lumbar subsegment of spinal cord and 194 other tissues.
DR Genevisible; Q3USB7; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050811; F:GABA receptor binding; ISO:MGI.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IGI:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IGI:YuBioLab.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:1900122; P:positive regulation of receptor binding; IGI:MGI.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR042124; PLCL1.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF102; PTHR10336:SF102; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF16457; PH_12; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..1096
FT /note="Inactive phospholipase C-like protein 1"
FT /id="PRO_0000319415"
FT DOMAIN 114..224
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 399..543
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 586..702
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 702..831
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..222
FT /note="Interaction with PPP1C"
FT /evidence="ECO:0000250"
FT REGION 544..568
FT /note="Interaction with GABA A beta subunit"
FT /evidence="ECO:0000250"
FT REGION 550..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1040..1060
FT /evidence="ECO:0000255"
FT COMPBIAS 78..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15111"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 94
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000305|PubMed:15306641,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 96
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000305|PubMed:15306641"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62688"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62688"
FT MUTAGEN 94
FT /note="T->A: Decreased level of phosphorylation. Loss of
FT phosphorylation; when associated with A-96."
FT /evidence="ECO:0000269|PubMed:15306641"
FT MUTAGEN 96
FT /note="S->A: Decreased level of phosphorylation. Loss of
FT phosphorylation; when associated with A-94."
FT /evidence="ECO:0000269|PubMed:15306641"
FT CONFLICT 116
FT /note="M -> I (in Ref. 1; BAE36646)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="D -> N (in Ref. 1; BAE24416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1096 AA; 122673 MW; 5C11ADB0725F5776 CRC64;
MAEGAASREA PAPLDVAGGE DDPRAGADAA SGDAPPPALG GRMRDRRSGV ALPGAAGVPA
DSEAGLLEAA RATPRRSSII KDPSNQKCGG RKKTVSFSSM PSEKKISSAH DCISFMQAGC
ELKKVRPNSR IYNRFFTLDT DLQALRWEPS KKDLEKAKLD ISAIKEIRLG KNTETFRNNG
LADQICEDCA FSILHGENYE SLDLVANSAD VANIWVSGLR YLVSRSKQPL DFIEGNQNTP
RFMWLKTVFE AADVDGNGIM LEDTSVELIK QLNPTLKESK IRLKFKEIQK SKEKLTTRVT
EEEFCEAFCE LCTRPEVYFL LVQISKNKEY LDANDLMLFL EAEQGVTHIT EDMCLDIIRR
YELSEDGRQK GFLAIDGFTQ YLLSPECDIF DPEQKKVAQD MTQPLSHYYI NASHNTYLIE
DQFRGPADIN GYVRALKMGC RSIELDVSDG PDNEPILCNR NNMAMHLSFR SVLEVINKFA
FVASEYPLIL CLGNHCSLPQ QKVMAQQMKK VFGEKLYTEA PLSSESYLPS PEKLKNMIIV
KGKKLPSESD LLEGEVTDED EEAEMSRRMS GDYNGEQKHI WLCRELSDLV SICKSVQHRD
FELSMKTQNY WEMCSFSETE ASRIANEYPE DFVNYNKKFL SRVYPSAMRI DSSNLNPQDF
WNCGCQIVAM NFQTPGPMMD LHTGWFLQNG GCGYVLRPSI MRDEVSYFSA NTKGIVPGVS
PLVLHIKIIS GQNFPKPKGA CAKGDVIDPY VCVEIHGIPA DCCEQRTKTV QQNSDNPIFD
ETFEFQVNLP ELTMVRFVIL DDDYIGDEFI GQYTIPFECL QPGYRHVPLR SFVGDIMEHV
TLFVHIAITN RSGGGKPQKR SLSVRMGKKV REYTMLRNIG LKTIDDIFKI AVHPLREAID
MRENMQNAIV SVKELCGLPP IASLKQCLLT LSSRLITSDS TPSVSLVMKD CFPYLEPLGA
IPDVQKRMLA AYDLMIQESR VLIEMADTVQ EKIVQCQKAG MEFHEELHNL GAKEGLKGRK
LNKAIESFAW NITVLKGQGD LLKNAKNEAV ENIKQIQLAC LSCGLSKGPG GGSEAKGKRS
LEAIEEKESS EENGKL
