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Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase

Gene

norpA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei334 – 3341PROSITE-ProRule annotation
Active sitei381 – 3811PROSITE-ProRule annotation
Binding sitei467 – 4671SubstrateBy similarity
Binding sitei469 – 4691SubstrateBy similarity
Binding sitei579 – 5791SubstrateBy similarity
Binding sitei606 – 6061SubstrateBy similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • GTPase activator activity Source: FlyBase
  • phosphatidylinositol phospholipase C activity Source: FlyBase
  • phospholipase C activity Source: FlyBase
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • adult locomotory behavior Source: FlyBase
  • calcium-mediated signaling Source: FlyBase
  • deactivation of rhodopsin mediated signaling Source: FlyBase
  • detection of chemical stimulus involved in sensory perception of bitter taste Source: FlyBase
  • diacylglycerol biosynthetic process Source: FlyBase
  • entrainment of circadian clock Source: FlyBase
  • entrainment of circadian clock by photoperiod Source: FlyBase
  • light-induced release of internally sequestered calcium ion Source: FlyBase
  • lipid catabolic process Source: UniProtKB-KW
  • mucosal immune response Source: FlyBase
  • negative regulation of compound eye retinal cell programmed cell death Source: FlyBase
  • phosphatidylinositol metabolic process Source: FlyBase
  • phospholipid biosynthetic process Source: FlyBase
  • phospholipid metabolic process Source: FlyBase
  • photoreceptor cell maintenance Source: FlyBase
  • phototransduction Source: FlyBase
  • positive regulation of clathrin-mediated endocytosis Source: FlyBase
  • positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: FlyBase
  • positive regulation of GTPase activity Source: GOC
  • rhodopsin mediated signaling pathway Source: FlyBase
  • thermotaxis Source: FlyBase
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism, Sensory transduction, Vision

Enzyme and pathway databases

ReactomeiREACT_282109. G alpha (q) signalling events.
REACT_288405. Synthesis of IP3 and IP4 in the cytosol.
REACT_349107. PLC beta mediated events.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase (EC:3.1.4.11)
Alternative name(s):
No receptor potential A protein
Phosphoinositide phospholipase C
Gene namesi
Name:norpA
ORF Names:CG3620
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0262738. norpA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GOC
  • inaD signaling complex Source: FlyBase
  • intracellular Source: GOC
  • rhabdomere Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 109510951-phosphatidylinositol 4,5-bisphosphate phosphodiesterasePRO_0000088510Add
BLAST

Proteomic databases

PaxDbiP13217.
PRIDEiP13217.

Expressioni

Tissue specificityi

Abundantly expressed in the adult retina.1 Publication

Gene expression databases

BgeeiP13217.
ExpressionAtlasiP13217. differential.
GenevisibleiP13217. DM.

Interactioni

Subunit structurei

Interacts with inaD.

Binary interactionsi

WithEntry#Exp.IntActNotes
inaDQ240083EBI-101510,EBI-195326

Protein-protein interaction databases

BioGridi57893. 10 interactions.
DIPiDIP-45N.
IntActiP13217. 8 interactions.
MINTiMINT-770866.
STRINGi7227.FBpp0070618.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHJX-ray1.80A/B211-214[»]
ProteinModelPortaliP13217.
SMRiP13217. Positions 13-840.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13217.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini319 – 469151PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini550 – 666117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini673 – 77199C2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00760000118936.
InParanoidiP13217.
KOiK05858.
OMAiSFTYMVA.
OrthoDBiEOG7WDN1N.
PhylomeDBiP13217.

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_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]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PfamiPF00168. 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]
PIRSFiPIRSF000956. PLC-beta. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P13217-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTKKYEFDWI IPVPPELTTG CVFDRWFENE KETKENDFER DALFKVDEYG
60 70 80 90 100
FFLYWKSEGR DGDVIELCQV SDIRAGGTPK DPKILDKVTK KNGTNIPELD
110 120 130 140 150
KRSLTICSNT DYINITYHHV ICPDAATAKS WQKNLRLITH NNRATNVCPR
160 170 180 190 200
VNLMKHWMRL SYCVEKSGKI PVKTLAKTFA SGKTEKLVYT CIKDAGLPDD
210 220 230 240 250
KNATMTKEQF TFDKFYALYH KVCPRNDIEE LFTSITKGKQ DFISLEQFIQ
260 270 280 290 300
FMNDKQRDPR MNEILYPLYE EKRCTEIIND YELDEEKKKN VQMSLDGFKR
310 320 330 340 350
YLMSDENAPV FLDRLDFYME MDQPLAHYYI NSSHNTYLSG RQIGGKSSVE
360 370 380 390 400
MYRQTLLAGC RCVELDCWNG KGEDEEPIVT HGHAYCTEIL FKDCIQAIAD
410 420 430 440 450
CAFVSSEYPV ILSFENHCNR AQQYKLAKYC DDFFGDLLLK EPLPDHPLDP
460 470 480 490 500
GLPLPPPCKL KRKILIKNKR MKPEVEKVEL ELWLKGELKT DDDPEEDASA
510 520 530 540 550
GKPPEAAAAP APAPEAAAAA EGAAEGGGGA EAEAAAANYS GSTTNVHPWL
560 570 580 590 600
SSMVNYAQPI KFQGFDKAIE KNIAHNMSSF AESAGMNYLK QSSIDFVNYN
610 620 630 640 650
KRQMSRIYPK GTRADSSNYM PQVFWNAGCQ MVSLNFQSSD LPMQLNQGKF
660 670 680 690 700
EYNGGCGYLL KPDFMRRADK DFDPFADAPV DGVIAAQCSV KVIAGQFLSD
710 720 730 740 750
KKVGTYVEVD MFGLPSDTVK KEFRTRLVAN NGLNPVYNED PFVFRKVVLP
760 770 780 790 800
DLAVLRFGVY EESGKILGQR ILPLDGLQAG YRHVSLRTEA NFPMSLPMLF
810 820 830 840 850
VNIELKIYVP DGFEDFMAML SDPRGFAGAA KQQNEQMKAL GIEEQSGGAA
860 870 880 890 900
RDAGKAKEEE KKEPPLVFEP VTLESLRQEK GFQKVGKKQI KELDTLRKKH
910 920 930 940 950
AKERTSVQKT QNAAIDKLIK GKSKDDIRND ANIKNSINDQ TKQWTDMIAR
960 970 980 990 1000
HRKEEWDMLR QHVQDSQDAM KALMLTVQAA QIKQLEDRHA RDIKDLNAKQ
1010 1020 1030 1040 1050
AKMSADTAKE VQNDKTLKTK NEKDRRLREK RQNNVKRFME EKKQIGVKQG
1060 1070 1080 1090
RAMEKLKLAH SKQIEEFSTD VQKLMDMYKI EEEAYKTQGK TEFYA
Length:1,095
Mass (Da):124,863
Last modified:June 10, 2008 - v4
Checksum:iCC712ABF9B065BB6
GO
Isoform C (identifier: P13217-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:1,095
Mass (Da):124,824
Checksum:i6F09204041C4FF74
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti446 – 4461H → R in AAA28724 (PubMed:2457447).Curated
Sequence conflicti968 – 9681D → G in AAO25053 (Ref. 5) Curated
Sequence conflicti1094 – 10941Y → C in AAA28724 (PubMed:2457447).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei130 – 15425SWQKN…RVNLM → IWLDGIRKITHNVKANNICP MMCLR in isoform C. CuratedVSP_034088Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA31225.
RefSeqiNP_001014720.1. NM_001014720.2. [P13217-2]
NP_001014721.1. NM_001014721.3. [P13217-2]
NP_001162661.1. NM_001169190.2. [P13217-1]
NP_001284860.1. NM_001297931.1. [P13217-2]
NP_525069.2. NM_080330.4. [P13217-1]
NP_726925.1. NM_167008.2. [P13217-1]
UniGeneiDm.7394.

Genome annotation databases

EnsemblMetazoaiFBtr0070650; FBpp0070618; FBgn0262738. [P13217-1]
FBtr0070651; FBpp0070619; FBgn0262738. [P13217-1]
FBtr0301475; FBpp0290690; FBgn0262738. [P13217-1]
GeneIDi31376.
KEGGidme:Dmel_CG3620.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA31225.
RefSeqiNP_001014720.1. NM_001014720.2. [P13217-2]
NP_001014721.1. NM_001014721.3. [P13217-2]
NP_001162661.1. NM_001169190.2. [P13217-1]
NP_001284860.1. NM_001297931.1. [P13217-2]
NP_525069.2. NM_080330.4. [P13217-1]
NP_726925.1. NM_167008.2. [P13217-1]
UniGeneiDm.7394.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHJX-ray1.80A/B211-214[»]
ProteinModelPortaliP13217.
SMRiP13217. Positions 13-840.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57893. 10 interactions.
DIPiDIP-45N.
IntActiP13217. 8 interactions.
MINTiMINT-770866.
STRINGi7227.FBpp0070618.

Proteomic databases

PaxDbiP13217.
PRIDEiP13217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070650; FBpp0070618; FBgn0262738. [P13217-1]
FBtr0070651; FBpp0070619; FBgn0262738. [P13217-1]
FBtr0301475; FBpp0290690; FBgn0262738. [P13217-1]
GeneIDi31376.
KEGGidme:Dmel_CG3620.

Organism-specific databases

CTDi31376.
FlyBaseiFBgn0262738. norpA.

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00760000118936.
InParanoidiP13217.
KOiK05858.
OMAiSFTYMVA.
OrthoDBiEOG7WDN1N.
PhylomeDBiP13217.

Enzyme and pathway databases

ReactomeiREACT_282109. G alpha (q) signalling events.
REACT_288405. Synthesis of IP3 and IP4 in the cytosol.
REACT_349107. PLC beta mediated events.

Miscellaneous databases

ChiTaRSinorpA. fly.
EvolutionaryTraceiP13217.
GenomeRNAii31376.
NextBioi773325.
PROiP13217.

Gene expression databases

BgeeiP13217.
ExpressionAtlasiP13217. differential.
GenevisibleiP13217. DM.

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_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]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PfamiPF00168. 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]
PIRSFiPIRSF000956. PLC-beta. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Head.
  5. 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.

Entry informationi

Entry nameiPIPA_DROME
AccessioniPrimary (citable) accession number: P13217
Secondary accession number(s): A4V3Y2
, Q59E70, Q86P93, Q9U4G4, Q9W4K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 10, 2008
Last modified: June 24, 2015
This is version 170 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

3D structural studies were performed with a synthetic heptapeptide that contained Cys, corresponding to position 1094, therefore the detected disulfide bridge is an artifact.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.