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P13217 (PIPA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase

EC=3.1.4.11
Alternative name(s):
No receptor potential A protein
Phosphoinositide phospholipase C
Gene names
Name:norpA
ORF Names:CG3620
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1095 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential component of the phototransduction pathway. Ref.1

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Subunit structure

Interacts with inaD.

Tissue specificity

Abundantly expressed in the adult retina. Ref.1

Disruption phenotype

Flies have no photoreceptor potential, their eyes lack phospholipase C (PLC) activity and they are completely blind. Ref.1

Sequence similarities

Contains 1 C2 domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Caution

3D structural studies (Ref.6) were performed with a synthetic heptapeptide that contained Cys, corresponding to position 1094, therefore the detected disulfide bridge is an artifact.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
Sensory transduction
Vision
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Transducer
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from mutant phenotype PubMed 16111941. Source: FlyBase

calcium-mediated signaling

Traceable author statement PubMed 10611962. Source: FlyBase

deactivation of rhodopsin mediated signaling

Inferred from direct assay PubMed 18184564. Source: FlyBase

detection of chemical stimulus involved in sensory perception of bitter taste

Inferred from mutant phenotype PubMed 20404155. Source: FlyBase

diacylglycerol biosynthetic process

Traceable author statement PubMed 10611962PubMed 11707492. Source: FlyBase

entrainment of circadian clock

Inferred from mutant phenotype PubMed 16085487. Source: FlyBase

entrainment of circadian clock by photoperiod

Inferred from genetic interaction PubMed 22306971. Source: FlyBase

light-induced release of internally sequestered calcium ion

Traceable author statement PubMed 8570597. Source: FlyBase

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

mucosal immune response

Inferred from mutant phenotype PubMed 19289084. Source: FlyBase

negative regulation of compound eye retinal cell programmed cell death

Inferred from mutant phenotype PubMed 14724249. Source: FlyBase

phosphatidylinositol metabolic process

Inferred from mutant phenotype PubMed 3129419. Source: FlyBase

phospholipid biosynthetic process

Traceable author statement PubMed 10611962. Source: FlyBase

phospholipid metabolic process

Traceable author statement PubMed 11707492. Source: FlyBase

photoreceptor cell maintenance

Inferred from mutant phenotype PubMed 16835270. Source: FlyBase

phototransduction

Inferred from mutant phenotype PubMed 15883198. Source: FlyBase

positive regulation of GTPase activity

Non-traceable author statement PubMed 11707492. Source: GOC

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Traceable author statement PubMed 8570597. Source: FlyBase

rhodopsin mediated signaling pathway

Inferred from mutant phenotype PubMed 18184564PubMed 7759511. Source: FlyBase

thermotaxis

Inferred from mutant phenotype PubMed 21393546. Source: FlyBase

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentinaD signaling complex

Inferred from physical interaction PubMed 9796815. Source: FlyBase

rhabdomere

Inferred from direct assay PubMed 16301334PubMed 1662208. Source: FlyBase

   Molecular_functionGTPase activator activity

Non-traceable author statement PubMed 11707492. Source: FlyBase

calcium ion binding

Inferred from electronic annotation. Source: InterPro

phosphatidylinositol phospholipase C activity

Inferred from mutant phenotype PubMed 7759511. Source: FlyBase

phospholipase C activity

Traceable author statement PubMed 10611962. Source: FlyBase

protein binding

Inferred from physical interaction PubMed 21703451PubMed 9545241. Source: IntAct

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

inaDQ240083EBI-101510,EBI-195326

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P13217-1)

Also known as: B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform C (identifier: P13217-2)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     130-154: SWQKNLRLITHNNRATNVCPRVNLM → IWLDGIRKITHNVKANNICPMMCLR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 109510951-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
PRO_0000088510

Regions

Domain319 – 469151PI-PLC X-box
Domain550 – 666117PI-PLC Y-box
Domain673 – 77199C2

Sites

Active site3341 By similarity
Active site3811 By similarity
Binding site4671Substrate By similarity
Binding site4691Substrate By similarity
Binding site5791Substrate By similarity
Binding site6061Substrate By similarity

Natural variations

Alternative sequence130 – 15425SWQKN…RVNLM → IWLDGIRKITHNVKANNICP MMCLR in isoform C.
VSP_034088

Experimental info

Sequence conflict4461H → R in AAA28724. Ref.1
Sequence conflict9681D → G in AAO25053. Ref.5
Sequence conflict10941Y → C in AAA28724. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A (B) [UniParc].

Last modified June 10, 2008. Version 4.
Checksum: CC712ABF9B065BB6

FASTA1,095124,863
        10         20         30         40         50         60 
MTKKYEFDWI IPVPPELTTG CVFDRWFENE KETKENDFER DALFKVDEYG FFLYWKSEGR 

        70         80         90        100        110        120 
DGDVIELCQV SDIRAGGTPK DPKILDKVTK KNGTNIPELD KRSLTICSNT DYINITYHHV 

       130        140        150        160        170        180 
ICPDAATAKS WQKNLRLITH NNRATNVCPR VNLMKHWMRL SYCVEKSGKI PVKTLAKTFA 

       190        200        210        220        230        240 
SGKTEKLVYT CIKDAGLPDD KNATMTKEQF TFDKFYALYH KVCPRNDIEE LFTSITKGKQ 

       250        260        270        280        290        300 
DFISLEQFIQ FMNDKQRDPR MNEILYPLYE EKRCTEIIND YELDEEKKKN VQMSLDGFKR 

       310        320        330        340        350        360 
YLMSDENAPV FLDRLDFYME MDQPLAHYYI NSSHNTYLSG RQIGGKSSVE MYRQTLLAGC 

       370        380        390        400        410        420 
RCVELDCWNG KGEDEEPIVT HGHAYCTEIL FKDCIQAIAD CAFVSSEYPV ILSFENHCNR 

       430        440        450        460        470        480 
AQQYKLAKYC DDFFGDLLLK EPLPDHPLDP GLPLPPPCKL KRKILIKNKR MKPEVEKVEL 

       490        500        510        520        530        540 
ELWLKGELKT DDDPEEDASA GKPPEAAAAP APAPEAAAAA EGAAEGGGGA EAEAAAANYS 

       550        560        570        580        590        600 
GSTTNVHPWL SSMVNYAQPI KFQGFDKAIE KNIAHNMSSF AESAGMNYLK QSSIDFVNYN 

       610        620        630        640        650        660 
KRQMSRIYPK GTRADSSNYM PQVFWNAGCQ MVSLNFQSSD LPMQLNQGKF EYNGGCGYLL 

       670        680        690        700        710        720 
KPDFMRRADK DFDPFADAPV DGVIAAQCSV KVIAGQFLSD KKVGTYVEVD MFGLPSDTVK 

       730        740        750        760        770        780 
KEFRTRLVAN NGLNPVYNED PFVFRKVVLP DLAVLRFGVY EESGKILGQR ILPLDGLQAG 

       790        800        810        820        830        840 
YRHVSLRTEA NFPMSLPMLF VNIELKIYVP DGFEDFMAML SDPRGFAGAA KQQNEQMKAL 

       850        860        870        880        890        900 
GIEEQSGGAA RDAGKAKEEE KKEPPLVFEP VTLESLRQEK GFQKVGKKQI KELDTLRKKH 

       910        920        930        940        950        960 
AKERTSVQKT QNAAIDKLIK GKSKDDIRND ANIKNSINDQ TKQWTDMIAR HRKEEWDMLR 

       970        980        990       1000       1010       1020 
QHVQDSQDAM KALMLTVQAA QIKQLEDRHA RDIKDLNAKQ AKMSADTAKE VQNDKTLKTK 

      1030       1040       1050       1060       1070       1080 
NEKDRRLREK RQNNVKRFME EKKQIGVKQG RAMEKLKLAH SKQIEEFSTD VQKLMDMYKI 

      1090 
EEEAYKTQGK TEFYA 

« Hide

Isoform C (D) [UniParc].

Checksum: 6F09204041C4FF74
Show »

FASTA1,095124,824

References

« Hide 'large scale' references
[1]"Isolation of a putative phospholipase C gene of Drosophila, norpA, and its role in phototransduction."
Bloomquist B.T., Shortridge R.D., Schneuwly S., Perdew M.H., Montell C., Steller H., Rubin G., Pak W.L.
Cell 54:723-733(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"A Drosophila complementary DNA resource."
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.
Science 287:2222-2224(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Head.
[5]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Head.
[6]"Functional relevance of the disulfide-linked complex of the N-terminal PDZ domain of InaD with NorpA."
Kimple M.E., Siderovski D.P., Sondek J.
EMBO J. 20:4414-4422(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1089-1095 IN A COMPLEX WITH INAD.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03138 mRNA. Translation: AAA28724.1.
AE014298 Genomic DNA. Translation: AAF45942.2.
AE014298 Genomic DNA. Translation: AAN09121.1.
AE014298 Genomic DNA. Translation: AAX52474.1.
AE014298 Genomic DNA. Translation: AAX52475.1.
AF181641 mRNA. Translation: AAD55427.1.
BT003293 mRNA. Translation: AAO25053.1.
PIRA31225.
RefSeqNP_001014720.1. NM_001014720.1. [P13217-2]
NP_001014721.1. NM_001014721.2. [P13217-2]
NP_001162661.1. NM_001169190.1. [P13217-1]
NP_525069.2. NM_080330.3. [P13217-1]
NP_726925.1. NM_167008.1. [P13217-1]
UniGeneDm.7394.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHJX-ray1.80A/B211-214[»]
ProteinModelPortalP13217.
SMRP13217. Positions 13-840.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid57893. 10 interactions.
DIPDIP-45N.
IntActP13217. 2 interactions.
MINTMINT-770866.

Proteomic databases

PaxDbP13217.
PRIDEP13217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070650; FBpp0070618; FBgn0262738. [P13217-1]
FBtr0070651; FBpp0070619; FBgn0262738. [P13217-1]
FBtr0301475; FBpp0290690; FBgn0262738. [P13217-1]
GeneID31376.
KEGGdme:Dmel_CG3620.

Organism-specific databases

CTD31376.
FlyBaseFBgn0262738. norpA.

Phylogenomic databases

eggNOGNOG149692.
GeneTreeENSGT00730000110266.
InParanoidP13217.
KOK05858.
OMASFTYMVA.
OrthoDBEOG7WDN1N.
PhylomeDBP13217.

Gene expression databases

BgeeP13217.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016280. PLC-beta.
IPR009535. PLC-beta_CS.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PfamPF00168. C2. 1 hit.
PF06631. DUF1154. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PIRSFPIRSF000956. PLC-beta. 1 hit.
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13217.
GenomeRNAi31376.
NextBio773325.
PROP13217.

Entry information

Entry namePIPA_DROME
AccessionPrimary (citable) accession number: P13217
Secondary accession number(s): A4V3Y2 expand/collapse secondary AC list , Q59E70, Q86P93, Q9U4G4, Q9W4K9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 10, 2008
Last modified: July 9, 2014
This is version 162 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase