PLCL2_MOUSE
ID PLCL2_MOUSE Reviewed; 1128 AA.
AC Q8K394; Q3U4E2; Q80TK5; Q9QYG1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Inactive phospholipase C-like protein 2;
DE Short=PLC-L(2);
DE Short=PLC-L2;
DE Short=Phospholipase C-L2;
DE AltName: Full=Phospholipase C-epsilon-2;
DE Short=PLC-epsilon-2;
GN Name=Plcl2; Synonyms=Kiaa1092, Plce2;
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 [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=10581172; DOI=10.1006/bbrc.1999.1784;
RA Otsuki M., Fukami K., Kohno T., Yokota J., Takenawa T.;
RT "Identification and characterization of a new phospholipase C-like protein,
RT PLC-L(2).";
RL Biochem. Biophys. Res. Commun. 266:97-103(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
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 MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 240-1128.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-585, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85; THR-585 AND SER-1114, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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: May play an role in the regulation of Ins(1,4,5)P3 around the
CC endoplasmic reticulum. {ECO:0000269|PubMed:10581172}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10581172}.
CC Note=Predominantly localized to perinuclear areas in both myoblast and
CC myotube C2C12 cells.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with a strong expression in
CC skeletal muscle. {ECO:0000269|PubMed:10581172}.
CC -!- CAUTION: In the PI-PLC X-box Thr-487 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; AB033615; BAA89457.1; -; mRNA.
DR EMBL; AK154288; BAE32490.1; -; mRNA.
DR EMBL; BC027746; AAH27746.1; -; mRNA.
DR EMBL; AK122439; BAC65721.1; -; mRNA.
DR CCDS; CCDS28875.1; -.
DR RefSeq; NP_038908.2; NM_013880.3.
DR RefSeq; XP_006524213.1; XM_006524150.2.
DR RefSeq; XP_006524214.1; XM_006524151.3.
DR RefSeq; XP_006524215.1; XM_006524152.2.
DR AlphaFoldDB; Q8K394; -.
DR SMR; Q8K394; -.
DR BioGRID; 230332; 2.
DR STRING; 10090.ENSMUSP00000046584; -.
DR GlyConnect; 2386; 1 N-Linked glycan (1 site).
DR GlyGen; Q8K394; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q8K394; -.
DR PhosphoSitePlus; Q8K394; -.
DR SwissPalm; Q8K394; -.
DR EPD; Q8K394; -.
DR jPOST; Q8K394; -.
DR MaxQB; Q8K394; -.
DR PaxDb; Q8K394; -.
DR PeptideAtlas; Q8K394; -.
DR PRIDE; Q8K394; -.
DR ProteomicsDB; 289925; -.
DR Antibodypedia; 26950; 154 antibodies from 28 providers.
DR DNASU; 224860; -.
DR Ensembl; ENSMUST00000043938; ENSMUSP00000046584; ENSMUSG00000038910.
DR GeneID; 224860; -.
DR KEGG; mmu:224860; -.
DR UCSC; uc012avf.1; mouse.
DR CTD; 23228; -.
DR MGI; MGI:1352756; Plcl2.
DR VEuPathDB; HostDB:ENSMUSG00000038910; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000155660; -.
DR HOGENOM; CLU_002738_0_1_1; -.
DR InParanoid; Q8K394; -.
DR OMA; NTDSLYE; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q8K394; -.
DR TreeFam; TF313216; -.
DR BioGRID-ORCS; 224860; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Plcl2; mouse.
DR PRO; PR:Q8K394; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K394; protein.
DR Bgee; ENSMUSG00000038910; Expressed in caudate-putamen and 251 other tissues.
DR Genevisible; Q8K394; 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:0002322; P:B cell proliferation involved in immune response; IMP:MGI.
DR GO; GO:0002337; P:B-1a B cell differentiation; IMP:MGI.
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:0050859; P:negative regulation of B cell receptor signaling pathway; IMP:MGI.
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; IGI: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; IPR028382; PLCL2.
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:SF84; PTHR10336:SF84; 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 Acetylation; Cytoplasm; Phosphoprotein; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UPR0"
FT CHAIN 2..1128
FT /note="Inactive phospholipase C-like protein 2"
FT /id="PRO_0000288852"
FT DOMAIN 142..252
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 427..571
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 619..735
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 735..864
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPR0"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPR0"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 585
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 142
FT /note="N -> H (in Ref. 1; BAA89457)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="I -> V (in Ref. 3; AAH27746)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="C -> R (in Ref. 1; BAA89457)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="D -> N (in Ref. 2; BAE32490)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="I -> V (in Ref. 1; BAA89457)"
FT /evidence="ECO:0000305"
FT CONFLICT 797..798
FT /note="EQ -> AD (in Ref. 1; BAA89457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1128 AA; 125772 MW; 08066A8C023E7935 CRC64;
MAECGRGAAG GALPTSPSPA LGAKGALKAG AGEGGGGGGG GRLGHGRARY DSGGVSNGDC
SLGVSGDEAR TSPGRGPLGV ALARTPSPAA GPVPRDSKPG GLPRRSSIIK DGTKQKRERK
KTVSFSSMPT EKKISSASDC INSMVEGSEL KKVRSNSRIY HRYFLLDADM QSLRWEPSKK
DSEKAKIDIK SIKEVRTGKN TDIFRSNGIS EQISEDCAFS VIYGENYESL DLVANSADVA
NIWVTGLRYL ISYGKHTLDM LESSQDNMRT SWISQMFSEI DVDGLGHITL CHAVQCIRNL
NPGLKTSKIE LKFKELHKSK DKAGTEITKE EFIEVFHELC TRPEIYFLLV QFSSNKEFLD
TKDLMMFLEA EQGVAHINEE ISLEIIHKYE PSKEGQEKGW LSIDGFTNYL MSPDCYIFDP
EHKKVCQDMK QPLSHYFINS SHNTYLIEDQ FRGPSDITGY IRALKMGCRS VELDVWDGPD
NEPVIYTGHT MTSQIVFRSV IDIINKYAFF ASEYPLILCL ENHCSIKQQK VMVQHMKKIL
GDKLYTTSPN MEESYLPSPD VLKGKILIKA KKLSSNCSGV EGDVTDEDEG AEMSQRMGKE
NVEQPNHVPV KRFQLCKELS ELVSICKSVQ FKEFQVSFQV QKYWEVCSFN EVLASKYANE
NPGDFVNYNK RFLARVFPSP MRIDSSNMNP QDFWKCGCQI VAMNFQTPGL MMDLNVGWFR
QNGNCGYVLR PAIMREEVSF FSANTKDSVP GVSPQLLHIK IISGQNFPKP KGSGAKGDVV
DPYVYVEIHG IPADCAEQRT KTVNQNGDAP IFDESFEFQI NLPELAMVRF VVLDDDYIGD
EFIGQYTIPF ECLQTGYRHV PLQSLTGEVL AHASLFVHVA ITNRRGGGKP HKRGLSVRKG
KKSREYASLR TLWIKTVDEV FKNAQPPIRD ATDLRENMQN AVVSFKELCG LSSVANLMQC
MLAVSPRFLG PDNNPLVVLN LSEPYPTMEL QAIVPEVLKK IVTTYDMMMQ SLKALIENAD
AVYEKIVHCQ KAAMEFHEHL HSIGTKEGLK ERKLQKAVES FTWNITILKG QADLLKYAKN
ETLENLKQIH FAAVSCGLNK PGTENSEAQK PRRSLEAIPE KASDENGD
