PLCL1_RAT
ID PLCL1_RAT Reviewed; 1096 AA.
AC Q62688;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Inactive phospholipase C-like protein 1;
DE Short=PLC-L1;
DE AltName: Full=PRIP1;
DE AltName: Full=Phospholipase C-related but catalytically inactive protein;
DE AltName: Full=p130;
GN Name=Plcl1;
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], PROTEIN SEQUENCE OF 172-191; 228-242 AND
RP 1024-1034, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP INS(1,4,5)P3 AND INS(1,4,5,6)P4.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8546702; DOI=10.1042/bj3130319;
RA Kanematsu T., Misumi Y., Watanabe Y., Ozaki S., Koga T., Iwanaga S.,
RA Ikehara Y., Hirata M.;
RT "A new inositol 1,4,5-trisphosphate binding protein similar to
RT phospholipase C-delta 1.";
RL Biochem. J. 313:319-325(1996).
RN [2]
RP SUBCELLULAR LOCATION, INTERACTION WITH PPP1C, PHOSPHORYLATION BY PKA, AND
RP FUNCTION.
RX PubMed=11278544; DOI=10.1074/jbc.m009677200;
RA Yoshimura K., Takeuchi H., Sato O., Hidaka K., Doira N., Terunuma M.,
RA Harada K., Ogawa Y., Ito Y., Kanematsu T., Hirata M.;
RT "Interaction of p130 with, and consequent inhibition of, the catalytic
RT subunit of protein phosphatase 1alpha.";
RL J. Biol. Chem. 276:17908-17913(2001).
RN [3]
RP INTERACTION WITH GABARAP AND PPP1C.
RX PubMed=11867528; DOI=10.1093/emboj/21.5.1004;
RA Kanematsu T., Jang I.S., Yamaguchi T., Nagahama H., Yoshimura K.,
RA Hidaka K., Matsuda M., Takeuchi H., Misumi Y., Nakayama K., Yamamoto T.,
RA Akaike N., Hirata M., Nakayama K.;
RT "Role of the PLC-related, catalytically inactive protein p130 in GABA(A)
RT receptor function.";
RL EMBO J. 21:1004-1011(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12467885; DOI=10.1016/s0024-3205(02)02275-0;
RA Uji A., Matsuda M., Kukita T., Maeda K., Kanematsu T., Hirata M.;
RT "Molecules interacting with PRIP-2, a novel Ins(1,4,5)P3 binding protein
RT type 2: Comparison with PRIP-1.";
RL Life Sci. 72:443-453(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-94; SER-96; THR-557;
RP SER-570 AND SER-1080, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: 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. {ECO:0000269|PubMed:11278544, ECO:0000269|PubMed:8546702}.
CC -!- SUBUNIT: Interacts with PPP2CA, GABA receptor beta subunits, GABA
CC receptor gamma-2 subunits (By similarity). Interacts with Ins(1,4,5)P3,
CC Ins(1,4,5,6)P4, GABARAP, and PPP1C. May form a ternary complex with
CC GABA receptor beta subunit and GABARAP. The formation of a ternary
CC complex with GABA receptor beta subunit and GABARAP could be the key
CC step for facilitating the association of GABARAP with the GABA receptor
CC gamma-2 subunit and to allow it to be transported at the right
CC destination. {ECO:0000250, ECO:0000269|PubMed:11278544,
CC ECO:0000269|PubMed:11867528, ECO:0000269|PubMed:8546702}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278544,
CC ECO:0000269|PubMed:8546702}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Found in the granular cell and
CC Purkinje cell layers in the cerebellum; and in the hippocampal
CC pyramidal cells, dentate granule cells and pyramidal granule cells of
CC the cerebral cortex in the cerebrum. {ECO:0000269|PubMed:12467885}.
CC -!- PTM: Phosphorylation of Thr-94 resulted in dissociation of PPP1C from
CC PRIP1 (By similarity). In vitro, phosphorylated by the catalytic
CC subunit of PKA. {ECO:0000250, ECO:0000269|PubMed:11278544}.
CC -!- SIMILARITY: Belongs to the PRIP family. {ECO:0000305}.
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; D45920; BAA08351.1; -; mRNA.
DR PIR; S62358; S62358.
DR RefSeq; NP_445908.1; NM_053456.1.
DR AlphaFoldDB; Q62688; -.
DR SMR; Q62688; -.
DR STRING; 10116.ENSRNOP00000050087; -.
DR BindingDB; Q62688; -.
DR ChEMBL; CHEMBL3364; -.
DR iPTMnet; Q62688; -.
DR PhosphoSitePlus; Q62688; -.
DR PaxDb; Q62688; -.
DR GeneID; 84587; -.
DR KEGG; rno:84587; -.
DR UCSC; RGD:708420; rat.
DR CTD; 5334; -.
DR RGD; 708420; Plcl1.
DR eggNOG; KOG0169; Eukaryota.
DR InParanoid; Q62688; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q62688; -.
DR PRO; PR:Q62688; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0050811; F:GABA receptor binding; IDA: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; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:1900122; P:positive regulation of receptor binding; ISO:RGD.
DR GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISO:RGD.
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; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Transducer.
FT CHAIN 1..1096
FT /note="Inactive phospholipase C-like protein 1"
FT /id="PRO_0000319416"
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 REGION 544..568
FT /note="Interaction with GABA A beta subunit"
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:22673903"
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:22673903"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1096 AA; 122772 MW; 06F13B580660A01F CRC64;
MAEGAASREA PAPLDVAGGE DDPRAGADAA SGDAAPEASG GRMRDRRSGV ALPGNAGVPA
DSEAGLLEAA RATPRRTSII KDPSNQKCGG RKKTVSFSSM PSEKKISSAH DCISFMQAGC
ELKKVRPNSR IYNRFFTLDT DLQALRWEPS KKDLEKAKLD ISAIKEIRLG KNTETFRNNG
LADQICEDCA FSILHGENYE SLDLVANSAD VANIWVSGLR YLVSRSKQPL DFMEGNQNTP
RFMWLKTVFE AADVDGNGIM LEDTSVELIK QLNPTLKESK IRLKFKEIQK SKEKLTTRVT
EEEFCEAFCE LCTRPEVYFL LVQISKNKEY LDANDLMLFL EVEQGVTHVT EDMCLDIIRR
YELSEDGRQK GFLAIDGFTQ YLLSPECDIF DPEQKKVAQD MTQPLSHYYI NASHNTYLIE
DQFRGPADIN GYVRALKMGC RSIELDVSDG PDNEPILCNR NNMAMLLSFR SVLEVINKFA
FVASEYPLIL CLGNHCSLPQ QRVMVQQMKK VFGNKLYTEA PLSSESYLPS PEKLKHMIIV
KGKKLPSESD LLEGEVTDED EEAEMSRRVS GDYNGEQKHI WLCRELSDLV SICKSVQYRD
FELSMKTQNY WEICSFSETL ASRIANEYPE DFVNYNKKFL SRVYPSAMRI DSSNLNPQDF
WNCGCQIVAM NFQTPGPMMD LHTGWFLQNG GCGYVLRPSI MRDEVSYFSA NTKGIVPGVS
PLLLHIKIIS GQNFPKPKGA CAKGDVIDPY VCVEIHGIPA DCSEQRTKTV QQNSDNPIFD
ETFEFQVNLP ELTMVRFVIL DDDYIGDEFI GQYTIPFECL QPGYRHVPLR SFVGDIMEHV
TLFVHIAITN RSGGGKAQKR SLSVRMGKKV REYTMLRNIG LKTIDDIFKI AVHPLREAID
MRENMQNAIV SVKELCGLPP IASLKQCLLT LSSRLITSDS TPSVSLVMKD CFPYLEPLGT
IPDVQKRMLA AYDLMIQESR VLIEMADTVQ EKIVQCQKAG MEFHEELHNL GAKEGLKGRK
LNKAIESFAW NITVLKGQGD LLKNAKNEAV ENIKQIQLAC LSCGLSKGPG SAAEAKGKRS
LEAIEEKESS EENGKL
