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A1Z6W3 (PRIC1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein prickle
Alternative name(s):
Protein spiny legs
Gene names
Name:pk
ORF Names:CG11084
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1299 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Molecular functionDevelopmental protein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior axis specification

Inferred from mutant phenotype Ref.4. Source: UniProtKB

establishment of imaginal disc-derived wing hair orientation

Inferred from mutant phenotype PubMed 21379328. Source: FlyBase

establishment of ommatidial planar polarity

Inferred from mutant phenotype PubMed 7555730. Source: FlyBase

establishment of planar polarity

Inferred from mutant phenotype Ref.4. Source: UniProtKB

establishment of protein localization

Traceable author statement PubMed 12414186. Source: FlyBase

establishment of tissue polarity

Inferred from mutant phenotype Ref.4. Source: UniProtKB

establishment or maintenance of cell polarity

Inferred from mutant phenotype Ref.4. Source: FlyBase

imaginal disc-derived leg joint morphogenesis

Inferred from mutant phenotype PubMed 22736244. Source: FlyBase

maintenance of protein location

Traceable author statement PubMed 12414186. Source: FlyBase

morphogenesis of a polarized epithelium

Inferred from mutant phenotype PubMed 16326392. Source: FlyBase

negative regulation of Notch signaling pathway

Inferred from mutant phenotype PubMed 22736244. Source: FlyBase

protein localization

Traceable author statement PubMed 12127767. Source: FlyBase

   Cellular_componentcytoplasm

Traceable author statement PubMed 12414186. Source: FlyBase

membrane

Non-traceable author statement PubMed 12414186. Source: FlyBase

plasma membrane

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.4Ref.5. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12991299Protein prickle
PRO_0000288834

Regions

Domain515 – 623109PET
Domain622 – 68665LIM zinc-binding 1
Domain687 – 74761LIM zinc-binding 2
Domain748 – 81063LIM zinc-binding 3
Compositional bias245 – 29248Pro-rich
Compositional bias412 – 49079Pro-rich
Compositional bias857 – 87721Gln-rich
Compositional bias1157 – 124993Ser-rich

Natural variations

Alternative sequence2 – 8079SSLST…KAAAQ → NDSTDNLHADCDGRVSNNNN GNSNTNDGPNNDGDSDEEVI EGMALLEGNYQVLRQWVPPA PNYWDAPPKAIIKSAEVR in isoform B. Ref.1
VSP_052412
Alternative sequence2 – 1312SSLST…GAGGS → DTPNQMPVELER in isoform A. Ref.1
VSP_052413
Alternative sequence14 – 349336Missing in isoform A. Ref.1
VSP_052414
Alternative sequence81 – 349269Missing in isoform B. Ref.1
VSP_052415

Experimental info

Sequence conflict175 – 1773ESS → VSN in CAB57345. Ref.1
Sequence conflict1881V → A in CAB57345. Ref.1
Sequence conflict2791Q → P in CAB57345. Ref.1
Sequence conflict7151A → G in CAB57344. Ref.1
Sequence conflict7151A → G in CAB57345. Ref.1
Sequence conflict7151A → G in CAB99211. Ref.1
Sequence conflict7461A → G in CAB57344. Ref.1
Sequence conflict7461A → G in CAB57345. Ref.1
Sequence conflict7461A → G in CAB99211. Ref.1
Sequence conflict7551A → G in CAB57344. Ref.1
Sequence conflict7551A → G in CAB57345. Ref.1
Sequence conflict7551A → G in CAB99211. Ref.1
Sequence conflict7971A → G in CAB57344. Ref.1
Sequence conflict7971A → G in CAB57345. Ref.1
Sequence conflict7971A → G in CAB99211. Ref.1
Sequence conflict8301R → G in CAB57344. Ref.1
Sequence conflict8301R → G in CAB57345. Ref.1
Sequence conflict8301R → G in CAB99211. Ref.1
Sequence conflict9701S → P in CAB57344. Ref.1
Sequence conflict9701S → P in CAB57345. Ref.1
Sequence conflict9701S → P in CAB99211. Ref.1
Sequence conflict10291L → V in CAB57344. Ref.1
Sequence conflict10291L → V in CAB57345. Ref.1
Sequence conflict10291L → V in CAB99211. Ref.1
Sequence conflict11341G → S in CAB57344. Ref.1
Sequence conflict11341G → S in CAB57345. Ref.1
Sequence conflict11341G → S in CAB99211. Ref.1
Sequence conflict12311E → K in CAB57344. Ref.1
Sequence conflict12311E → K in CAB57345. Ref.1
Sequence conflict12311E → K in CAB99211. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform C (sple) [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 8BFAF1F75F352485

FASTA1,299140,722
        10         20         30         40         50         60 
MSSLSTGGGA GGSSGGPGGA DAAAAPAAGQ ATVTATGNME PAMVPRTANL LACKQWWRVC 

        70         80         90        100        110        120 
FLYGDQQKYY RQLYSKAAAQ RLADANQEPD NARDREYDTV DCDLIAGQLD AVEDADDGID 

       130        140        150        160        170        180 
LGDHSSTPKG GATTAGRPLF PHSSSPRRSK KLLRSLRAHV RGEKLPKNDT TTANESSEVT 

       190        200        210        220        230        240 
QRNARVTVLD DPFLFGIDAD HLGDLVVRGK RYSTLDATEN MARFYAEQEA TAQVLEIIEQ 

       250        260        270        280        290        300 
EEESPEQEAP KPALPPKQKQ QRPVPPLPPP PANRVTQDQG TQPAAPQVPL QPLTAGDLQF 

       310        320        330        340        350        360 
LNLSLRQRSL PRSMKPFKDA HDISFTFNEL DTSAEPEVAT GAAQQESNEP ISRTPLTQIS 

       370        380        390        400        410        420 
YLQKIPTLPR HFSPSGQGLA TPPALGSGGM GLPSSSSASA LYAAQAAAGI LPTSPLPLQR 

       430        440        450        460        470        480 
HQQYLPPHHQ QHPGAGMGPG PGSGAAAGPP LGPQYSPGCS ANPKYSNAQL PPPPHHHHQL 

       490        500        510        520        530        540 
SPALSTPSPP SLLHHPAGGT SSASAHAPFL GGPHMDMQRQ SHSDDDSGCA LEEYTWVPPG 

       550        560        570        580        590        600 
LRPDQVRLYF SQIPDDKVPY VNSPGEQYRV RQLLHQLPPH DNEVRYCHSL TDEERKELRL 

       610        620        630        640        650        660 
FSTQRKRDAL GRGNVRQLMS ARPCDGCDDL ISTGDIAVFA TRLGPNASWH PACFACSVCR 

       670        680        690        700        710        720 
ELLVDLIYFH RDGRMYCGRH HAETLKPRCS ACDEIILADE CTEAEGRAWH MNHFACHECD 

       730        740        750        760        770        780 
KQLGGQRYIM REGKPYCLHC FDAMFAEYCD YCGEAIGVDQ GQMSHDGQHW HATDECFSCN 

       790        800        810        820        830        840 
TCRCSLLGRA FLPRRGAIYC SIACSKGEPP TPSDSSGTGM YTTPTPPTQR VRPHPQAPLP 

       850        860        870        880        890        900 
ARIPSSHASS SPPMSPQQQQ QHQATFNQAM YQMQSQQMEA AGGLVDQSKS YAASDSDAGV 

       910        920        930        940        950        960 
VKDLEHGGHM GGGDLTDFSG GRASSTSQNL SPLNSPGDFQ PHFLPKPMEL QRDGVYNFNE 

       970        980        990       1000       1010       1020 
MSSNLDAAWS AKPTNSYHLQ RQLLENPHTA SMPELAGKLV APPAHMQHLS QLHAVSSHQF 

      1030       1040       1050       1060       1070       1080 
QQHEYADILH PPPPPPGEIP ELPTPNLSVA STALPPELMG SPTHSAGDRS LNTPMSTQSA 

      1090       1100       1110       1120       1130       1140 
SHAPPHPVSI LSGASSSSPM SGEPAKKKGV RFEGIPDTLP RSRSYSGNGA GTSGGGERER 

      1150       1160       1170       1180       1190       1200 
DRDKDKEGGG RHGHGHSSRR RRRRKSSSSS SHHRSGSGHR SHSTTRADTY APAQPLSSSY 

      1210       1220       1230       1240       1250       1260 
QGPPSVLQAA NLVHESPSRQ QRERERERER EESEESDVCS TCSSSSSSSE DYMMMYQLPQ 

      1270       1280       1290 
RRHYGGVRVS YVPNDALAYD RKRKPSELGG DKDKNCIIS 

« Hide

Isoform A (pk) [UniParc].

Checksum: C01685B61EA4C367
Show »

FASTA963104,682
Isoform B (pkM) [UniParc].

Checksum: D532D80FFFDAC461
Show »

FASTA1,029111,765

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. 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]"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.
RefSeqNP_724534.1. NM_165508.2. [A1Z6W3-2]
NP_724535.1. NM_165509.2. [A1Z6W3-3]
NP_724538.1. NM_165512.2. [A1Z6W3-1]
UniGeneDm.3470.

3D structure databases

ProteinModelPortalA1Z6W3.
SMRA1Z6W3. Positions 624-805.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid69608. 8 interactions.
DIPDIP-59584N.
IntActA1Z6W3. 2 interactions.

Proteomic databases

PaxDbA1Z6W3.
PRIDEA1Z6W3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089044; FBpp0088115; FBgn0003090. [A1Z6W3-1]
GeneID45343.
KEGGdme:Dmel_CG11084.

Organism-specific databases

CTD18745.
FlyBaseFBgn0003090. pk.

Phylogenomic databases

eggNOGNOG314122.
GeneTreeENSGT00550000074438.
InParanoidA1Z6W3.
KOK04511.
OMAWHATDEC.
OrthoDBEOG7P8P7M.
PhylomeDBA1Z6W3.

Gene expression databases

BgeeA1Z6W3.

Family and domain databases

Gene3D2.10.110.10. 3 hits.
InterProIPR010442. PET_domain.
IPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 2 hits.
PF06297. PET. 1 hit.
[Graphical view]
SMARTSM00132. LIM. 3 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS51303. PET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi45343.
NextBio838057.

Entry information

Entry namePRIC1_DROME
AccessionPrimary (citable) accession number: A1Z6W3
Secondary accession number(s): A1Z6V4 expand/collapse secondary AC list , A1Z6V8, Q9N9H6, Q9U5X0, Q9U5X1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: February 6, 2007
Last modified: July 9, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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