PRIC1_ANOGA
ID PRIC1_ANOGA Reviewed; 923 AA.
AC Q7QJT4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 4.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Protein prickle;
GN Name=pk {ECO:0000250|UniProtKB:A1Z6W3}; ORFNames=AGAP007648;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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; AAAB01008807; EAA04128.4; -; Genomic_DNA.
DR RefSeq; XP_308221.4; XM_308221.4.
DR AlphaFoldDB; Q7QJT4; -.
DR SMR; Q7QJT4; -.
DR STRING; 7165.AGAP007648-PA; -.
DR PaxDb; Q7QJT4; -.
DR PRIDE; Q7QJT4; -.
DR GeneID; 1269578; -.
DR KEGG; aga:AgaP_AGAP007648; -.
DR CTD; 1269578; -.
DR VEuPathDB; VectorBase:AGAP007648; -.
DR eggNOG; KOG1704; Eukaryota.
DR HOGENOM; CLU_008937_4_2_1; -.
DR InParanoid; Q7QJT4; -.
DR OMA; YELPMRR; -.
DR OrthoDB; 116531at2759; -.
DR PhylomeDB; Q7QJT4; -.
DR Proteomes; UP000007062; Chromosome 2L.
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..923
FT /note="Protein prickle"
FT /id="PRO_0000288833"
FT DOMAIN 275..383
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 382..446
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 447..507
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 508..570
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 99620 MW; 9482D2312C68F572 CRC64;
MSYPYQKSHH QTQQPQQNGH PQHQLMLQQQ QQADHSPHHH HHHHVHHATA HAYPYELGRS
PLRSPQSPPL YSGKPPPPPP QSYHSYQQPP TAAHPPVSLS GAPTSMPGMM PGQQPPGMTL
SLGGGGGGGG GGSAGDCFML PPLQPQSPDG LSTVTNTSST ATNAPSARSV YPQHHQPSYP
SIGSSHHPFH SPASAAALIG PSMPQHAQQQ QQHQMQPHHY SSMHLLGPAG GPPSSVGPAS
MVGMMGPGGH GGGGVGGGAG GIAGGVGGGP GGGMGGGHNY SQSDDDSGCA LEEYTWVPPG
LRPDQVHLYF SAIPEDKVPY VNSIGERHRV RQLLQQLPPH DNEVRYCHSL TDEERKELKL
FSAQRKREAL GRGTVKQITT TLICERCGEC ASSGDMMVFA SRFEPNTCWH PACFACCVCK
ELLVDLIYFH RENRLYCGRH HAETLKPRCS ACDEIILADE CTEAEGRAWH IKHFACFECD
KQLGGQRYIM RDGKPYCLHC FDAMFAEYCD YCSEPIGVDQ GQMSHDGQHW HATDQCFACS
TCRCSLLGRP FLPRRGEIYC SIACSKGEPP TPSDEYAHRS SQPSHTAARS PEPLRSPERG
TGRLSPPHTE HEVQSHEAAS TVGSDRDHQL RSPASNGTAT DNGTGTAGGG VGDSNRHRIP
HRQPLDLTDL GHSLEQHWQS ERTGSETISI TTATATVRTQ VTGPIAGANG NGPTGGGPIL
TSSMPELNRC LAAAGSGESP SFSGTNSPTP MPIEDSVVAN GGDDADEQNQ NASDASHSIK
EVRFEGDFQD SLPRTKSYCQ RNGGQRNRAA KSSSYASDDD ELAEDETDNY HHRRHHHSHQ
REQQRPVDDS DARSVCSTCS SSSSSADDDV YELPLRRTSY GGTRIHYMPN NSLACARKRK
QLQTSSGVAG QHYEKDNKNC IIS
