PRIC1_AEDAE
ID PRIC1_AEDAE Reviewed; 916 AA.
AC Q174I2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Protein prickle;
GN Name=pk {ECO:0000250|UniProtKB:A1Z6W3}; ORFNames=AAEL006891;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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; CH477410; EAT41476.1; -; Genomic_DNA.
DR RefSeq; XP_001652308.1; XM_001652258.1.
DR AlphaFoldDB; Q174I2; -.
DR SMR; Q174I2; -.
DR STRING; 7159.AAEL006891-PA; -.
DR VEuPathDB; VectorBase:AAEL022496; -.
DR eggNOG; KOG1704; Eukaryota.
DR HOGENOM; CLU_008937_4_1_1; -.
DR InParanoid; Q174I2; -.
DR OMA; YELPMRR; -.
DR PhylomeDB; Q174I2; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
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; 3.
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..916
FT /note="Protein prickle"
FT /id="PRO_0000288832"
FT DOMAIN 167..275
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 274..338
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 339..399
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 400..462
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 49..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..791
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 101773 MW; 06A3629BB20B4E80 CRC64;
MAKNVRFSIN MFGVMSPMIP PPRHHPVAPM SYPYQKPSSF EYDQLNRVPL SPHHHQQPPY
PKPPLQHPSA SPIHHQPPPP QHSPSVGDFL PPLQPQPHQD AAGGSRSIYS AHALSQAATN
LHPQHLQHLQ HGPFSQQPPP PPMGSSPSPA LSSSITTGGG GVTRGGGGGG HIIPVDDDSG
CALEEYTWVP PGLRPDQVHL YFSAIPEDKV PYVNSIGERH RVRQLLQQLP PHDNEVRYCH
SLTDEERKEL KLFSAQRKRE ALGRGTVKQL ATNQICDGCG ECISSGDMGV YASRFDPGTC
WHPACFVCSV CKELLVDLIY FHREARLYCG RHHAETLKPR CSACDEIILA DECTEAEGRA
WHIKHFACFE CDKQLGGQRY IMRDGKPYCL HCFDAMFAEY CDFCSEPIGV DQGQMSHDGQ
HWHATDSCFA CSTCRCSLLG RPFLPRRGEI YCSIACSKGE PPTPSDGSVP TVLPSRTRLR
APGQRNFDDP SAEYVPNLPK SPEPLQSPIS ERSTPHSSPA KHSHTEMSTN ISSPVPTEFN
DQTYSVSADN DVQTYTGSGA TSPISSRTLP CTEPSDQTDH QHQSLPPLLP NHRRIPQCSP
ELDRLLHKDR SRQPLDLTDL SLSLDNWQAD HNSTVIPGPS IAKTNPALTS SMPELSQSLQ
QQQQQQQQPQ SLLAYDDISP LDKASAITDP DDAIQNASDD ASHSIVELPT PPPIVSNTRD
PENLPKMPLR RFQNSLPRNK FHKSSIIKKE VRFEGIFQDS LPRSKSYCTR SGGSRSRSSK
SKRRSSHHHQ HHRSSGESSS YSGTSYDRHH HSSSGSSSSN RRSPRRRRVP DVEFIEHQDH
HRGDGDDDSD SRSVCSTCSS SSSSADDTVY ELPMRRTYGG TRIHYMPNNS LACARKRKQL
QNSHPYEKDN KNCIIS
