A1Z6W3 (PRIC1_DROME) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein prickle Alternative name(s): Protein spiny legs | ||||
| Gene names |
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| Organism | Drosophila melanogaster (Fruit fly) [Reference proteome] | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora › ![]() |
Protein attributes
| Sequence length | 1299 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Acts in a planar cell polarity (PCP) complex; polarization along the apical/basal axis of epithelial cells. Correct expression of the alternative isoforms is required for PCP signaling in imaginal disks. PCP signaling in the wing disk requires the receptor fz and the cytoplasmic proteins dsh and pk. These act in a feedback loop leading to activation of the jnk cascade and subsequent polarized arrangement of hairs and bristles. Dgo and pk compete with one another for dsh binding, thereby modulating fz dsh activity and ensuring tight control over fz PCP signaling. Vang, stan and pk function together to regulate the establishment of tissue polarity in the adult eye. Ref.4 Ref.6 Ref.7 |
| Subunit structure | Interacts with dsh; PET and LIM domains interact with dsh DEP domain, in wing cells. Interacts with Vang in photoreceptor cells. Ref.4 Ref.5 Ref.6 Ref.7 |
| Subcellular location | Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Localized to the proximal wing cell boundary where fz and dsh localization is antagonized by binding the dsh DEP domain and preventing dsh cortical localization. Localization to the anterior photoreceptor cell membrane. Ref.4 Ref.5 Ref.6 Ref.7 |
| Tissue specificity | Expressed in the wing, leg and eye imaginal disks. Expressed within the photoreceptors of the eye. Ref.1 Ref.4 Ref.6 Ref.7 |
| Developmental stage | Expressed both maternally and zygotically. Isoform B is expressed in embryos only. Isoform A and isoform C are expressed in embryos and pupae. Ref.1 |
| Disruption phenotype | Flies exhibit aberrant hair and bristle orientation on the wings and aberrant ommatidial arrangement in the compound eye. Ref.4 Ref.6 Ref.7 |
| Sequence similarities | Belongs to the prickle / espinas / testin family. Contains 3 LIM zinc-binding domains. Contains 1 PET domain. |
Ontologies
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform C Ref.2 (identifier: A1Z6W3-1) Also known as: sple; 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 A Ref.2 (identifier: A1Z6W3-2) Also known as: pk; The sequence of this isoform differs from the canonical sequence as follows: 2-13: SSLSTGGGAGGS → DTPNQMPVELER 14-349: Missing. | ||||||
| Isoform B Ref.2 (identifier: A1Z6W3-3) Also known as: pkM; The sequence of this isoform differs from the canonical sequence as follows: 2-80: SSLSTGGGAG...RQLYSKAAAQ → NDSTDNLHAD...KAIIKSAEVR 81-349: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1299 | 1299 | Protein prickle | PRO_0000288834 | |||||
Regions | |||||||||
| Domain | 515 – 623 | 109 | PET | ||||||
| Domain | 622 – 686 | 65 | LIM zinc-binding 1 | ||||||
| Domain | 687 – 747 | 61 | LIM zinc-binding 2 | ||||||
| Domain | 748 – 810 | 63 | LIM zinc-binding 3 | ||||||
| Compositional bias | 245 – 292 | 48 | Pro-rich | ||||||
| Compositional bias | 412 – 490 | 79 | Pro-rich | ||||||
| Compositional bias | 857 – 877 | 21 | Gln-rich | ||||||
| Compositional bias | 1157 – 1249 | 93 | Ser-rich | ||||||
Natural variations | |||||||||
| Alternative sequence | 2 – 80 | 79 | SSLST…KAAAQ → NDSTDNLHADCDGRVSNNNN GNSNTNDGPNNDGDSDEEVI EGMALLEGNYQVLRQWVPPA PNYWDAPPKAIIKSAEVR in isoform B. Ref.1 | VSP_052412 | |||||
| Alternative sequence | 2 – 13 | 12 | SSLST…GAGGS → DTPNQMPVELER in isoform A. Ref.1 | VSP_052413 | |||||
| Alternative sequence | 14 – 349 | 336 | Missing in isoform A. Ref.1 | VSP_052414 | |||||
| Alternative sequence | 81 – 349 | 269 | Missing in isoform B. Ref.1 | VSP_052415 | |||||
Experimental info | |||||||||
| Sequence conflict | 175 – 177 | 3 | ESS → VSN in CAB57345. Ref.1 | ||||||
| Sequence conflict | 188 | 1 | V → A in CAB57345. Ref.1 | ||||||
| Sequence conflict | 279 | 1 | Q → P in CAB57345. Ref.1 | ||||||
| Sequence conflict | 715 | 1 | A → G in CAB57344. Ref.1 | ||||||
| Sequence conflict | 715 | 1 | A → G in CAB57345. Ref.1 | ||||||
| Sequence conflict | 715 | 1 | A → G in CAB99211. Ref.1 | ||||||
| Sequence conflict | 746 | 1 | A → G in CAB57344. Ref.1 | ||||||
| Sequence conflict | 746 | 1 | A → G in CAB57345. Ref.1 | ||||||
| Sequence conflict | 746 | 1 | A → G in CAB99211. Ref.1 | ||||||
| Sequence conflict | 755 | 1 | A → G in CAB57344. Ref.1 | ||||||
| Sequence conflict | 755 | 1 | A → G in CAB57345. Ref.1 | ||||||
| Sequence conflict | 755 | 1 | A → G in CAB99211. Ref.1 | ||||||
| Sequence conflict | 797 | 1 | A → G in CAB57344. Ref.1 | ||||||
| Sequence conflict | 797 | 1 | A → G in CAB57345. Ref.1 | ||||||
| Sequence conflict | 797 | 1 | A → G in CAB99211. Ref.1 | ||||||
| Sequence conflict | 830 | 1 | R → G in CAB57344. Ref.1 | ||||||
| Sequence conflict | 830 | 1 | R → G in CAB57345. Ref.1 | ||||||
| Sequence conflict | 830 | 1 | R → G in CAB99211. Ref.1 | ||||||
| Sequence conflict | 970 | 1 | S → P in CAB57344. Ref.1 | ||||||
| Sequence conflict | 970 | 1 | S → P in CAB57345. Ref.1 | ||||||
| Sequence conflict | 970 | 1 | S → P in CAB99211. Ref.1 | ||||||
| Sequence conflict | 1029 | 1 | L → V in CAB57344. Ref.1 | ||||||
| Sequence conflict | 1029 | 1 | L → V in CAB57345. Ref.1 | ||||||
| Sequence conflict | 1029 | 1 | L → V in CAB99211. Ref.1 | ||||||
| Sequence conflict | 1134 | 1 | G → S in CAB57344. Ref.1 | ||||||
| Sequence conflict | 1134 | 1 | G → S in CAB57345. Ref.1 | ||||||
| Sequence conflict | 1134 | 1 | G → S in CAB99211. Ref.1 | ||||||
| Sequence conflict | 1231 | 1 | E → K in CAB57344. Ref.1 | ||||||
| Sequence conflict | 1231 | 1 | E → K in CAB57345. Ref.1 | ||||||
| Sequence conflict | 1231 | 1 | E → K in CAB99211. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The balance between isoforms of the prickle LIM domain protein is critical for planar polarity in Drosophila imaginal discs." Gubb D., Green C., Huen D., Coulson D., Johnson G., Tree D.R.P., Collier S., Roote J. Genes Dev. 13:2315-2327(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: DP CN BW. Tissue: Embryo. |
| [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. 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. Lewis S.E.Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley. |
| [4] | "Prickle mediates feedback amplification to generate asymmetric planar cell polarity signaling." Tree D.R.P., Shulman J.M., Rousset R., Scott M.P., Gubb D., Axelrod J.D. Cell 109:371-381(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DSH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE. |
| [5] | "Prickle and Strabismus form a functional complex to generate a correct axis during planar cell polarity signaling." Jenny A., Darken R.S., Wilson P.A., Mlodzik M. EMBO J. 22:4409-4420(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VANG, SUBCELLULAR LOCATION. |
| [6] | "Strabismus requires Flamingo and Prickle function to regulate tissue polarity in the Drosophila eye." Rawls A.S., Wolff T. Development 130:1877-1887(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH VANG, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE. |
| [7] | "Diego and Prickle regulate Frizzled planar cell polarity signalling by competing for Dishevelled binding." Jenny A., Reynolds-Kenneally J., Das G., Burnett M., Mlodzik M. Nat. Cell Biol. 7:691-697(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DSH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ243708 mRNA. Translation: CAB57344.3. AJ243710 mRNA. Translation: CAB57345.3. AJ243709 mRNA. Translation: CAB99211.2. AE013599 Genomic DNA. Translation: AAF59281.2. AE013599 Genomic DNA. Translation: AAF59284.2. AE013599 Genomic DNA. Translation: AAM68908.1. |
| RefSeq | NP_724534.1. NM_165508.2. NP_724535.1. NM_165509.2. NP_724538.1. NM_165512.2. |
| UniGene | Dm.3470. |
3D structure databases | |
| ProteinModelPortal | A1Z6W3. |
| SMR | A1Z6W3. Positions 624-806. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-59584N. |
| IntAct | A1Z6W3. 2 interactions. |
Proteomic databases | |
| PaxDb | A1Z6W3. |
| PRIDE | A1Z6W3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | FBtr0089044; FBpp0088115; FBgn0003090. |
| GeneID | 45343. |
| KEGG | dme:Dmel_CG11084. |
Organism-specific databases | |
| CTD | 18745. |
| FlyBase | FBgn0003090. pk. |
Phylogenomic databases | |
| eggNOG | NOG314122. |
| GeneTree | ENSGT00550000074438. |
| InParanoid | A1Z6W3. |
| KO | K04511. |
| OMA | WHATDEC. |
| OrthoDB | EOG4T1G2F. |
| PhylomeDB | A1Z6W3. |
Gene expression databases | |
| Bgee | A1Z6W3. |
Family and domain databases | |
| Gene3D | 2.10.110.10. 3 hits. |
| InterPro | IPR010442. PET_domain. IPR001781. Znf_LIM. [Graphical view] |
| Pfam | PF00412. LIM. 2 hits. PF06297. PET. 1 hit. [Graphical view] |
| SMART | SM00132. LIM. 3 hits. [Graphical view] |
| PROSITE | PS00478. LIM_DOMAIN_1. 2 hits. PS50023. LIM_DOMAIN_2. 3 hits. PS51303. PET. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| GenomeRNAi | 45343. |
| NextBio | 838057. |
Entry information
| Entry name | PRIC1_DROME | ||||||||
| Accession | Primary (citable) accession number: A1Z6W3 Secondary accession number(s): A1Z6V4 Q9U5X1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with
