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Protein

Inactive phospholipase C-like protein 1

Gene

Plcl1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Acts as a inhibitor of PPP1C.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive phospholipase C-like protein 1
Short name:
PLC-L1
Alternative name(s):
PRIP1
Phospholipase C-related but catalytically inactive protein
p130
Gene namesi
Name:Plcl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi708420. Plcl1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3364.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10961096Inactive phospholipase C-like protein 1PRO_0000319416Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei78 – 781PhosphoserineBy similarity
Modified residuei94 – 941PhosphothreonineCombined sources
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei557 – 5571PhosphothreonineCombined sources
Modified residuei570 – 5701PhosphoserineCombined sources
Modified residuei1080 – 10801PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation of Thr-94 resulted in dissociation of PPP1C from PRIP1 (By similarity). In vitro, phosphorylated by the catalytic subunit of PKA.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ62688.
PRIDEiQ62688.

PTM databases

iPTMnetiQ62688.
PhosphoSiteiQ62688.

Expressioni

Tissue specificityi

Expressed in brain. Found in the granular cell and Purkinje cell layers in the cerebellum; and in the hippocampal pyramidal cells, dentate granule cells and pyramidal granule cells of the cerebral cortex in the cerebrum.1 Publication

Interactioni

Subunit structurei

Interacts with PPP2CA, GABA receptor beta subunits, GABA receptor gamma-2 subunits (By similarity). Interacts with Ins(1,4,5)P3, Ins(1,4,5,6)P4, GABARAP, 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.By similarity3 Publications

GO - Molecular functioni

  • GABA receptor binding Source: MGI

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050087.

Chemistry

BindingDBiQ62688.

Structurei

3D structure databases

ProteinModelPortaliQ62688.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 224111PHPROSITE-ProRule annotationAdd
BLAST
Domaini399 – 543145PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini586 – 702117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini709 – 814106C2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 222140Interaction with PPP1CAdd
BLAST
Regioni544 – 56825Interaction with GABA A beta subunitAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1040 – 106021Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the PRIP family.Curated
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0169. Eukaryota.
ENOG410XPSW. LUCA.
HOGENOMiHOG000006871.
HOVERGENiHBG108265.
InParanoidiQ62688.
KOiK15375.
PhylomeDBiQ62688.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLC_EF-hand-like.
IPR028382. PLCL1.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF102. PTHR10336:SF102. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF16457. PH_12. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q62688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEGAASREA PAPLDVAGGE DDPRAGADAA SGDAAPEASG GRMRDRRSGV
60 70 80 90 100
ALPGNAGVPA DSEAGLLEAA RATPRRTSII KDPSNQKCGG RKKTVSFSSM
110 120 130 140 150
PSEKKISSAH DCISFMQAGC ELKKVRPNSR IYNRFFTLDT DLQALRWEPS
160 170 180 190 200
KKDLEKAKLD ISAIKEIRLG KNTETFRNNG LADQICEDCA FSILHGENYE
210 220 230 240 250
SLDLVANSAD VANIWVSGLR YLVSRSKQPL DFMEGNQNTP RFMWLKTVFE
260 270 280 290 300
AADVDGNGIM LEDTSVELIK QLNPTLKESK IRLKFKEIQK SKEKLTTRVT
310 320 330 340 350
EEEFCEAFCE LCTRPEVYFL LVQISKNKEY LDANDLMLFL EVEQGVTHVT
360 370 380 390 400
EDMCLDIIRR YELSEDGRQK GFLAIDGFTQ YLLSPECDIF DPEQKKVAQD
410 420 430 440 450
MTQPLSHYYI NASHNTYLIE DQFRGPADIN GYVRALKMGC RSIELDVSDG
460 470 480 490 500
PDNEPILCNR NNMAMLLSFR SVLEVINKFA FVASEYPLIL CLGNHCSLPQ
510 520 530 540 550
QRVMVQQMKK VFGNKLYTEA PLSSESYLPS PEKLKHMIIV KGKKLPSESD
560 570 580 590 600
LLEGEVTDED EEAEMSRRVS GDYNGEQKHI WLCRELSDLV SICKSVQYRD
610 620 630 640 650
FELSMKTQNY WEICSFSETL ASRIANEYPE DFVNYNKKFL SRVYPSAMRI
660 670 680 690 700
DSSNLNPQDF WNCGCQIVAM NFQTPGPMMD LHTGWFLQNG GCGYVLRPSI
710 720 730 740 750
MRDEVSYFSA NTKGIVPGVS PLLLHIKIIS GQNFPKPKGA CAKGDVIDPY
760 770 780 790 800
VCVEIHGIPA DCSEQRTKTV QQNSDNPIFD ETFEFQVNLP ELTMVRFVIL
810 820 830 840 850
DDDYIGDEFI GQYTIPFECL QPGYRHVPLR SFVGDIMEHV TLFVHIAITN
860 870 880 890 900
RSGGGKAQKR SLSVRMGKKV REYTMLRNIG LKTIDDIFKI AVHPLREAID
910 920 930 940 950
MRENMQNAIV SVKELCGLPP IASLKQCLLT LSSRLITSDS TPSVSLVMKD
960 970 980 990 1000
CFPYLEPLGT IPDVQKRMLA AYDLMIQESR VLIEMADTVQ EKIVQCQKAG
1010 1020 1030 1040 1050
MEFHEELHNL GAKEGLKGRK LNKAIESFAW NITVLKGQGD LLKNAKNEAV
1060 1070 1080 1090
ENIKQIQLAC LSCGLSKGPG SAAEAKGKRS LEAIEEKESS EENGKL
Length:1,096
Mass (Da):122,772
Last modified:November 1, 1996 - v1
Checksum:i06F13B580660A01F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45920 mRNA. Translation: BAA08351.1.
PIRiS62358.
RefSeqiNP_445908.1. NM_053456.1.
UniGeneiRn.10684.

Genome annotation databases

GeneIDi84587.
KEGGirno:84587.
UCSCiRGD:708420. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45920 mRNA. Translation: BAA08351.1.
PIRiS62358.
RefSeqiNP_445908.1. NM_053456.1.
UniGeneiRn.10684.

3D structure databases

ProteinModelPortaliQ62688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050087.

Chemistry

BindingDBiQ62688.
ChEMBLiCHEMBL3364.

PTM databases

iPTMnetiQ62688.
PhosphoSiteiQ62688.

Proteomic databases

PaxDbiQ62688.
PRIDEiQ62688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi84587.
KEGGirno:84587.
UCSCiRGD:708420. rat.

Organism-specific databases

CTDi5334.
RGDi708420. Plcl1.

Phylogenomic databases

eggNOGiKOG0169. Eukaryota.
ENOG410XPSW. LUCA.
HOGENOMiHOG000006871.
HOVERGENiHBG108265.
InParanoidiQ62688.
KOiK15375.
PhylomeDBiQ62688.

Miscellaneous databases

PROiQ62688.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLC_EF-hand-like.
IPR028382. PLCL1.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF102. PTHR10336:SF102. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF16457. PH_12. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLCL1_RAT
AccessioniPrimary (citable) accession number: Q62688
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

In the PI-PLC X-box Asn-459 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.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.