PRIC1_DROPS
ID PRIC1_DROPS Reviewed; 1353 AA.
AC Q292U2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 3.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein prickle;
GN Name=pk {ECO:0000250|UniProtKB:A1Z6W3}; ORFNames=GA10748;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Acts in a planar cell polarity (PCP) complex; polarization
CC along the apical/basal axis of epithelial cells. PCP signaling in the
CC wing disk requires the receptor fz and the cytoplasmic proteins dsh and
CC pk. These act in a feedback loop leading to activation of the jnk
CC cascade and subsequent polarized arrangement of hairs and bristles. Dgo
CC and pk compete with one another for dsh binding, thereby modulating fz
CC dsh activity and ensuring tight control over fz PCP signaling. Vang,
CC stan and pk function together to regulate the establishment of tissue
CC polarity in the adult eye (By similarity).
CC {ECO:0000250|UniProtKB:A1Z6W3}.
CC -!- SUBUNIT: Interacts with dsh; PET and LIM domains interact with dsh DEP
CC domain, in wing cells. Interacts with Vang in photoreceptor cells (By
CC similarity). {ECO:0000250|UniProtKB:A1Z6W3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; CM000071; EAL24769.2; -; Genomic_DNA.
DR AlphaFoldDB; Q292U2; -.
DR SMR; Q292U2; -.
DR STRING; 7237.FBpp0277336; -.
DR eggNOG; KOG1704; Eukaryota.
DR HOGENOM; CLU_008937_0_0_1; -.
DR InParanoid; Q292U2; -.
DR OMA; WPAKPTN; -.
DR Proteomes; UP000001819; Genome assembly.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009948; P:anterior/posterior axis specification; ISS:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; ISS:UniProtKB.
DR GO; GO:0007164; P:establishment of tissue polarity; ISS:UniProtKB.
DR CDD; cd09415; LIM1_Prickle; 1.
DR CDD; cd09418; LIM2_Prickle; 1.
DR CDD; cd09420; LIM3_Prickle; 1.
DR CDD; cd09827; PET_Prickle; 1.
DR InterPro; IPR033725; LIM1_prickle.
DR InterPro; IPR033726; LIM2_prickle.
DR InterPro; IPR033727; LIM3_prickle.
DR InterPro; IPR010442; PET_domain.
DR InterPro; IPR033723; PET_prickle.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS51303; PET; 1.
PE 3: Inferred from homology;
KW Cell membrane; Developmental protein; LIM domain; Membrane; Metal-binding;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..1353
FT /note="Protein prickle"
FT /id="PRO_0000288835"
FT DOMAIN 548..656
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 655..719
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 720..780
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 781..843
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 130..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1224
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1353 AA; 145645 MW; AA18C037456DBB9A CRC64;
MSSLSAPPGG CGGDVAAAPA TATSTATATA TATATATATG SMEPAMVPRT ANLLACKQWW
RVCFLYGDQQ KYYRQLYSKA AAQRLAGANQ ENDNAARGAG AGEGEGQEYD TVAMGDGDFI
AAQLDAGEDV DDGIDLGDSS QPGGGATPTA TATAGRPLFP LSSSPRRSKK LLRSLRAHVK
GESRPEKPAK AAKPQSEPSS ELTKRNARVT VLDDPFLFGI DADHLGDLVR GKQYSPLEAT
ENIAKFYELQ LETTEATAQV LEIIEQEEEP PEPPKPALPP KQKQPRPVPP LPARITQPAV
LQPLTAGDLQ FLNLSLRHRS LPRSMKPFKD PHDISFTFNE LDTSTSATAA AAAAAVAAAD
VATGVGVGSS QQESNEPISR TPLTQISYLQ KIPTLPRHFS PSGCPQGLPP PPALAGCGSA
LGLPSSSSAS ALYAAQNGGM LPTSPLPLQR HQQYLPPHHQ QLPPLGAGPG QGQGHGLALG
PGGAGLPQYS PAVSGCSSTA KYSNAQLPPH HHQLSPALST PSPPSLLHHP AAGTSASAHA
PFLAGPHMDM QRQSHSDDDS GCALEEYTWV PPGLRPDQVR LYFSQIPDDK VPYVNSPGEQ
YRVRQLLHQL PPHDNEVRYC HSLTDEERKE LRLFSTQRKR DALGRGNVRQ LMSARPCDGC
DELISTGDIA VFATRLGPNA SWHPACFTCC ICRELLVDLI YFHRDGRMYC GRHHAETLKP
RCSACDEIIL ADECTEAEGR AWHMNHFACH ECDKQLGGQR YIMREGKPYC LHCFDAMFAE
YCDYCGEAIG VDQGQMSHDG QHWHATDECF SCNTCRCSLL GRAFLPRRGA IYCSIACSKG
EPPTPSDSSG TGMYTTPTPP TQRVRPQTRI TSSHASSSPP MSPQQQQQHQ ASFNQAMYQL
QTQQLEAAGG PVSQSQSYAT SDSDAGVVKD LEHCRSGDHA GGGDFTDFSG GRASSTSHNM
SPLNSPGDFQ PHLMPKPMEL QRDGVYNFNE MSSNLDTAWP AKPPLGATHS YQLQRQLMEN
QHTSSMPELA GKGPMLQHQM AAHFGQQPAL HSSAQQFQHE YADIMHPPPP PPERGAVGEV
PELPTPNLSV ASTALPPELM GSPTHSAGDR SLNTPLSAHS ATHGPTHPVS ILSGASSSSP
MSGEPAKKKG VRFEGIPDTL PRSRSYSGNG AGTSGGGDKD RDRDRERDRD RDRDKGGDKD
RESGRHGPGH SSRRRRRRKS TSSTSSGNHH RSGSGHRSHS TTRADTYAPA QPLSSSYQGP
PSVLQADSET AHKSPRQQRE REREESAEES DVCSTCSSSS SSSEDYMMMY QLPQRRHYGG
VRVSYVPNDA LAYDRKRKPA EMAGDKDKNC IIS
