ID   PRIC1_HUMAN             Reviewed;         831 AA.
AC   Q96MT3; Q14C83; Q71QF8; Q96N00;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Prickle-like protein 1;
DE   AltName: Full=REST/NRSF-interacting LIM domain protein 1;
DE   Flags: Precursor;
GN   Name=PRICKLE1; Synonyms=RILP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, ISOPRENYLATION AT CYS-828,
RP   MUTAGENESIS OF 828-CYS--SER-831, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   REST.
RC   TISSUE=Brain;
RX   PubMed=14645515; DOI=10.1128/mcb.23.24.9025-9031.2003;
RA   Shimojo M., Hersh L.B.;
RT   "REST/NRSF-interacting LIM domain protein, a putative nuclear translocation
RT   receptor.";
RL   Mol. Cell. Biol. 23:9025-9031(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=12525887;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human PRICKLE1 and PRICKLE2 genes
RT   as well as mouse Prickle1 and Prickle2 genes homologous to Drosophila
RT   tissue polarity gene prickle.";
RL   Int. J. Mol. Med. 11:249-256(2003).
RN   [5]
RP   INTERACTION WITH REST.
RX   PubMed=16442230; DOI=10.1016/j.neulet.2005.12.080;
RA   Shimojo M.;
RT   "Characterization of the nuclear targeting signal of REST/NRSF.";
RL   Neurosci. Lett. 398:161-166(2006).
RN   [6]
RP   ISOPRENYLATION AT CYS-828.
RX   PubMed=17411337; DOI=10.1371/journal.pcbi.0030066;
RA   Maurer-Stroh S., Koranda M., Benetka W., Schneider G., Sirota F.L.,
RA   Eisenhaber F.;
RT   "Towards complete sets of farnesylated and geranylgeranylated proteins.";
RL   PLoS Comput. Biol. 3:634-648(2007).
RN   [7]
RP   TISSUE SPECIFICITY, VARIANT EPM1B GLN-104, AND CHARACTERIZATION OF VARIANT
RP   EPM1B GLN-104.
RX   PubMed=18976727; DOI=10.1016/j.ajhg.2008.10.003;
RA   Bassuk A.G., Wallace R.H., Buhr A., Buller A.R., Afawi Z., Shimojo M.,
RA   Miyata S., Chen S., Gonzalez-Alegre P., Griesbach H.L., Wu S.,
RA   Nashelsky M., Vladar E.K., Antic D., Ferguson P.J., Cirak S., Voit T.,
RA   Scott M.P., Axelrod J.D., Gurnett C., Daoud A.S., Kivity S., Neufeld M.Y.,
RA   Mazarib A., Straussberg R., Walid S., Korczyn A.D., Slusarski D.C.,
RA   Berkovic S.F., El-Shanti H.I.;
RT   "A homozygous mutation in human PRICKLE1 causes an autosomal-recessive
RT   progressive myoclonus epilepsy-ataxia syndrome.";
RL   Am. J. Hum. Genet. 83:572-581(2008).
RN   [8]
RP   FUNCTION, POSSIBLE INVOLVEMENT IN NTD, AND VARIANTS THR-69; HIS-81;
RP   ILE-121; THR-124; MET-275; CYS-682; PHE-739; ASN-771 AND CYS-799.
RX   PubMed=21901791; DOI=10.1002/humu.21589;
RA   Bosoi C.M., Capra V., Allache R., Trinh V.Q., De Marco P., Merello E.,
RA   Drapeau P., Bassuk A.G., Kibar Z.;
RT   "Identification and characterization of novel rare mutations in the planar
RT   cell polarity gene PRICKLE1 in human neural tube defects.";
RL   Hum. Mutat. 32:1371-1375(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   VARIANTS EPM1B GLN-104; HIS-144 AND HIS-472.
RX   PubMed=21276947; DOI=10.1016/j.ajhg.2010.12.012;
RA   Tao H., Manak J.R., Sowers L., Mei X., Kiyonari H., Abe T., Dahdaleh N.S.,
RA   Yang T., Wu S., Chen S., Fox M.H., Gurnett C., Montine T., Bird T.,
RA   Shaffer L.G., Rosenfeld J.A., McConnell J., Madan-Khetarpal S.,
RA   Berry-Kravis E., Griesbach H., Saneto R.P., Scott M.P., Antic D., Reed J.,
RA   Boland R., Ehaideb S.N., El-Shanti H., Mahajan V.B., Ferguson P.J.,
RA   Axelrod J.D., Lehesjoki A.E., Fritzsch B., Slusarski D.C., Wemmie J.,
RA   Ueno N., Bassuk A.G.;
RT   "Mutations in prickle orthologs cause seizures in flies, mice, and
RT   humans.";
RL   Am. J. Hum. Genet. 88:138-149(2011).
CC   -!- FUNCTION: Involved in the planar cell polarity pathway that controls
CC       convergent extension during gastrulation and neural tube closure.
CC       Convergent extension is a complex morphogenetic process during which
CC       cells elongate, move mediolaterally, and intercalate between
CC       neighboring cells, leading to convergence toward the mediolateral axis
CC       and extension along the anteroposterior axis. Necessary for nuclear
CC       localization of REST. May serve as nuclear receptor.
CC       {ECO:0000269|PubMed:21901791}.
CC   -!- SUBUNIT: Interacts with REST. {ECO:0000269|PubMed:14645515,
CC       ECO:0000269|PubMed:16442230}.
CC   -!- INTERACTION:
CC       Q96MT3; Q13895: BYSL; NbExp=3; IntAct=EBI-2348662, EBI-358049;
CC       Q96MT3; Q92997: DVL3; NbExp=3; IntAct=EBI-2348662, EBI-739789;
CC       Q96MT3; O75564-2: JRK; NbExp=3; IntAct=EBI-2348662, EBI-17181882;
CC       Q96MT3; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-2348662, EBI-8472129;
CC       Q96MT3; Q8WWY3: PRPF31; NbExp=6; IntAct=EBI-2348662, EBI-1567797;
CC       Q96MT3; Q08E77: UTP14C; NbExp=3; IntAct=EBI-2348662, EBI-10225961;
CC       Q96MT3; Q8VIG1: Rest; Xeno; NbExp=4; IntAct=EBI-2348662, EBI-2312802;
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:14645515}.
CC       Cytoplasm, cytosol {ECO:0000269|PubMed:14645515}. Note=A smaller amount
CC       is detected in the cytosol.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in placenta and at
CC       lower levels in lung, liver, kidney and pancreas. Expressed in
CC       thalamus, hippocampus, cerebral cortex, and cerebellum (in neurons
CC       rather than glia). {ECO:0000269|PubMed:12525887,
CC       ECO:0000269|PubMed:14645515, ECO:0000269|PubMed:18976727}.
CC   -!- DISEASE: Epilepsy, progressive myoclonic 1B (EPM1B) [MIM:612437]: A
CC       form of progressive myoclonic epilepsy, a clinically and genetically
CC       heterogeneous group of disorders defined by the combination of action
CC       and reflex myoclonus, other types of epileptic seizures, and
CC       progressive neurodegeneration and neurocognitive impairment. EPM1B is
CC       an autosomal recessive form characterized by myoclonus that progressed
CC       in severity over time, tonic-clonic seizures and ataxia.
CC       {ECO:0000269|PubMed:18976727, ECO:0000269|PubMed:21276947}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital
CC       malformations of the central nervous system and adjacent structures
CC       related to defective neural tube closure during the first trimester of
CC       pregnancy. Failure of neural tube closure can occur at any level of the
CC       embryonic axis. Common NTD forms include anencephaly, myelomeningocele
CC       and spina bifida, which result from the failure of fusion in the
CC       cranial and spinal region of the neural tube. NTDs have a
CC       multifactorial etiology encompassing both genetic and environmental
CC       components. {ECO:0000269|PubMed:21901791}. Note=Disease susceptibility
CC       may be associated with variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC       {ECO:0000305}.
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DR   EMBL; AF399844; AAQ03035.1; -; mRNA.
DR   EMBL; AK056189; BAB71116.1; -; mRNA.
DR   EMBL; AK056499; BAB71198.1; -; mRNA.
DR   EMBL; BC114939; AAI14940.1; -; mRNA.
DR   EMBL; BC114940; AAI14941.1; -; mRNA.
DR   CCDS; CCDS8742.1; -.
DR   RefSeq; NP_001138353.1; NM_001144881.1.
DR   RefSeq; NP_001138354.1; NM_001144882.1.
DR   RefSeq; NP_001138355.1; NM_001144883.1.
DR   RefSeq; NP_694571.2; NM_153026.2.
DR   RefSeq; XP_011536248.1; XM_011537946.1.
DR   RefSeq; XP_011536249.1; XM_011537947.2.
DR   RefSeq; XP_016874327.1; XM_017018838.1.
DR   RefSeq; XP_016874328.1; XM_017018839.1.
DR   RefSeq; XP_016874329.1; XM_017018840.1.
DR   AlphaFoldDB; Q96MT3; -.
DR   SMR; Q96MT3; -.
DR   BioGRID; 126835; 25.
DR   IntAct; Q96MT3; 12.
DR   STRING; 9606.ENSP00000345064; -.
DR   GlyConnect; 2062; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q96MT3; 1 site, 2 glycans.
DR   GlyGen; Q96MT3; 1 site, 2 N-linked glycans (1 site).
DR   iPTMnet; Q96MT3; -.
DR   PhosphoSitePlus; Q96MT3; -.
DR   BioMuta; PRICKLE1; -.
DR   DMDM; 59800163; -.
DR   EPD; Q96MT3; -.
DR   jPOST; Q96MT3; -.
DR   MassIVE; Q96MT3; -.
DR   MaxQB; Q96MT3; -.
DR   PaxDb; 9606-ENSP00000345064; -.
DR   PeptideAtlas; Q96MT3; -.
DR   ProteomicsDB; 77402; -.
DR   Antibodypedia; 13204; 146 antibodies from 23 providers.
DR   DNASU; 144165; -.
DR   Ensembl; ENST00000345127.9; ENSP00000345064.3; ENSG00000139174.12.
DR   Ensembl; ENST00000445766.7; ENSP00000398947.2; ENSG00000139174.12.
DR   Ensembl; ENST00000455697.6; ENSP00000401060.1; ENSG00000139174.12.
DR   Ensembl; ENST00000548696.6; ENSP00000448359.1; ENSG00000139174.12.
DR   Ensembl; ENST00000552240.6; ENSP00000449819.1; ENSG00000139174.12.
DR   Ensembl; ENST00000639566.1; ENSP00000492332.1; ENSG00000139174.12.
DR   Ensembl; ENST00000639589.1; ENSP00000491051.1; ENSG00000139174.12.
DR   Ensembl; ENST00000639958.1; ENSP00000492644.1; ENSG00000139174.12.
DR   Ensembl; ENST00000640055.1; ENSP00000492763.1; ENSG00000139174.12.
DR   Ensembl; ENST00000640132.1; ENSP00000491228.1; ENSG00000139174.12.
DR   GeneID; 144165; -.
DR   KEGG; hsa:144165; -.
DR   MANE-Select; ENST00000345127.9; ENSP00000345064.3; NM_153026.3; NP_694571.2.
DR   UCSC; uc001rnl.4; human.
DR   AGR; HGNC:17019; -.
DR   CTD; 144165; -.
DR   DisGeNET; 144165; -.
DR   GeneCards; PRICKLE1; -.
DR   GeneReviews; PRICKLE1; -.
DR   HGNC; HGNC:17019; PRICKLE1.
DR   HPA; ENSG00000139174; Low tissue specificity.
DR   MalaCards; PRICKLE1; -.
DR   MIM; 182940; phenotype.
DR   MIM; 608500; gene.
DR   MIM; 612437; phenotype.
DR   neXtProt; NX_Q96MT3; -.
DR   OpenTargets; ENSG00000139174; -.
DR   Orphanet; 308; Progressive myoclonic epilepsy type 1.
DR   PharmGKB; PA134906946; -.
DR   VEuPathDB; HostDB:ENSG00000139174; -.
DR   eggNOG; KOG1704; Eukaryota.
DR   GeneTree; ENSGT00940000157529; -.
DR   HOGENOM; CLU_008937_5_0_1; -.
DR   InParanoid; Q96MT3; -.
DR   OMA; NLVFGCQ; -.
DR   OrthoDB; 370973at2759; -.
DR   PhylomeDB; Q96MT3; -.
DR   TreeFam; TF313265; -.
DR   PathwayCommons; Q96MT3; -.
DR   Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR   SignaLink; Q96MT3; -.
DR   SIGNOR; Q96MT3; -.
DR   BioGRID-ORCS; 144165; 15 hits in 1151 CRISPR screens.
DR   ChiTaRS; PRICKLE1; human.
DR   GenomeRNAi; 144165; -.
DR   Pharos; Q96MT3; Tbio.
DR   PRO; PR:Q96MT3; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q96MT3; Protein.
DR   Bgee; ENSG00000139174; Expressed in buccal mucosa cell and 184 other cell types or tissues.
DR   ExpressionAtlas; Q96MT3; baseline and differential.
DR   GO; GO:0031254; C:cell trailing edge; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:1905070; P:anterior visceral endoderm cell migration; IEA:Ensembl.
DR   GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR   GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR   GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR   GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR   GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR   GO; GO:0061303; P:cornea development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IEA:Ensembl.
DR   GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR   GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
DR   GO; GO:0035880; P:embryonic nail plate morphogenesis; IEA:Ensembl.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0061159; P:establishment of bipolar cell polarity involved in cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR   GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR   GO; GO:0120181; P:focal adhesion disassembly; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0060485; P:mesenchyme development; IEA:Ensembl.
DR   GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR   GO; GO:2000691; P:negative regulation of cardiac muscle cell myoblast differentiation; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL.
DR   GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR   GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; IEA:Ensembl.
DR   GO; GO:0061865; P:polarized secretion of basement membrane proteins in epithelium; IEA:Ensembl.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR   GO; GO:0090009; P:primitive streak formation; IEA:Ensembl.
DR   GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR   GO; GO:0061326; P:renal tubule development; IEA:Ensembl.
DR   GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0070075; P:tear secretion; IEA:Ensembl.
DR   GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:Ensembl.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR   CDD; cd09483; LIM1_Prickle_1; 1.
DR   CDD; cd09418; LIM2_Prickle; 1.
DR   CDD; cd09420; LIM3_Prickle; 1.
DR   CDD; cd09827; PET_Prickle; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 3.
DR   InterPro; IPR033726; LIM2_prickle.
DR   InterPro; IPR033727; LIM3_prickle.
DR   InterPro; IPR010442; PET_domain.
DR   InterPro; IPR033723; PET_prickle.
DR   InterPro; IPR047120; Pk/Esn/Tes.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24211; LIM DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24211:SF15; PRICKLE-LIKE PROTEIN 1; 1.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF06297; PET; 1.
DR   SMART; SM00132; LIM; 3.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS51303; PET; 1.
DR   Genevisible; Q96MT3; HS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Disease variant; Epilepsy; LIM domain; Lipoprotein; Membrane;
KW   Metal-binding; Methylation; Neurodegeneration; Nucleus; Phosphoprotein;
KW   Prenylation; Reference proteome; Repeat; Zinc.
FT   CHAIN           1..828
FT                   /note="Prickle-like protein 1"
FT                   /id="PRO_0000075889"
FT   PROPEP          829..831
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000396712"
FT   DOMAIN          14..122
FT                   /note="PET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT   DOMAIN          124..189
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          189..249
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          249..313
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          313..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..831
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT   MOD_RES         591
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT   MOD_RES         594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT   MOD_RES         683
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT   MOD_RES         828
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000305"
FT   LIPID           828
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:14645515,
FT                   ECO:0000269|PubMed:17411337"
FT   VARIANT         69
FT                   /note="I -> T (probable risk factor for NTD;
FT                   dbSNP:rs141795695)"
FT                   /evidence="ECO:0000269|PubMed:21901791"
FT                   /id="VAR_066850"
FT   VARIANT         81
FT                   /note="N -> H (probable risk factor for NTD;
FT                   dbSNP:rs796052934)"
FT                   /evidence="ECO:0000269|PubMed:21901791"
FT                   /id="VAR_066851"
FT   VARIANT         104
FT                   /note="R -> Q (in EPM1B; affects interaction with REST;
FT                   dbSNP:rs113994140)"
FT                   /evidence="ECO:0000269|PubMed:18976727,
FT                   ECO:0000269|PubMed:21276947"
FT                   /id="VAR_054663"
FT   VARIANT         121
FT                   /note="V -> I (probable risk factor for NTD;
FT                   dbSNP:rs371720624)"
FT                   /evidence="ECO:0000269|PubMed:21901791"
FT                   /id="VAR_066852"
FT   VARIANT         124
FT                   /note="A -> T (in dbSNP:rs79087668)"
FT                   /evidence="ECO:0000269|PubMed:21901791"
FT                   /id="VAR_066853"
FT   VARIANT         144
FT                   /note="R -> H (in EPM1B; dbSNP:rs281865563)"
FT                   /evidence="ECO:0000269|PubMed:21276947"
FT                   /id="VAR_065580"
FT   VARIANT         275
FT                   /note="T -> M (probable risk factor for NTD;
FT                   dbSNP:rs559947948)"
FT                   /evidence="ECO:0000269|PubMed:21901791"
FT                   /id="VAR_066854"
FT   VARIANT         472
FT                   /note="Y -> H (in EPM1B; dbSNP:rs281865564)"
FT                   /evidence="ECO:0000269|PubMed:21276947"
FT                   /id="VAR_065581"
FT   VARIANT         682
FT                   /note="R -> C (probable risk factor for NTD;
FT                   dbSNP:rs768954477)"
FT                   /evidence="ECO:0000269|PubMed:21901791"
FT                   /id="VAR_066855"
FT   VARIANT         739
FT                   /note="S -> F (probable risk factor for NTD;
FT                   dbSNP:rs138452760)"
FT                   /evidence="ECO:0000269|PubMed:21901791"
FT                   /id="VAR_066856"
FT   VARIANT         746
FT                   /note="P -> S (in dbSNP:rs3827522)"
FT                   /id="VAR_056164"
FT   VARIANT         771
FT                   /note="D -> N (probable risk factor for NTD;
FT                   dbSNP:rs146670726)"
FT                   /evidence="ECO:0000269|PubMed:21901791"
FT                   /id="VAR_066857"
FT   VARIANT         799
FT                   /note="S -> C (probable risk factor for NTD)"
FT                   /evidence="ECO:0000269|PubMed:21901791"
FT                   /id="VAR_066858"
FT   MUTAGEN         828..831
FT                   /note="Missing: Abolishes localization to the nuclear
FT                   membrane."
FT                   /evidence="ECO:0000269|PubMed:14645515"
FT   CONFLICT        739
FT                   /note="S -> P (in Ref. 2; BAB71198)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   831 AA;  94300 MW;  753D68BD5A4D0935 CRC64;
     MPLEMEPKMS KLAFGCQRSS TSDDDSGCAL EEYAWVPPGL RPEQIQLYFA CLPEEKVPYV
     NSPGEKHRIK QLLYQLPPHD NEVRYCQSLS EEEKKELQVF SAQRKKEALG RGTIKLLSRA
     VMHAVCEQCG LKINGGEVAV FASRAGPGVC WHPSCFVCFT CNELLVDLIY FYQDGKIHCG
     RHHAELLKPR CSACDEIIFA DECTEAEGRH WHMKHFCCLE CETVLGGQRY IMKDGRPFCC
     GCFESLYAEY CETCGEHIGV DHAQMTYDGQ HWHATEACFS CAQCKASLLG CPFLPKQGQI
     YCSKTCSLGE DVHASDSSDS AFQSARSRDS RRSVRMGKSS RSADQCRQSL LLSPALNYKF
     PGLSGNADDT LSRKLDDLSL SRQGTSFASE EFWKGRVEQE TPEDPEEWAD HEDYMTQLLL
     KFGDKSLFQP QPNEMDIRAS EHWISDNMVK SKTELKQNNQ SLASKKYQSD MYWAQSQDGL
     GDSAYGSHPG PASSRRLQEL ELDHGASGYN HDETQWYEDS LECLSDLKPE QSVRDSMDSL
     ALSNITGASV DGENKPRPSL YSLQNFEEME TEDCEKMSNM GTLNSSMLHR SAESLKSLSS
     ELCPEKILPE EKPVHLPVLR RSKSQSRPQQ VKFSDDVIDN GNYDIEIRQP PMSERTRRRV
     YNFEERGSRS HHHRRRRSRK SRSDNALNLV TERKYSPKDR LRLYTPDNYE KFIQNKSARE
     IQAYIQNADL YGQYAHATSD YGLQNPGMNR FLGLYGEDDD SWCSSSSSSS DSEEEGYFLG
     QPIPQPRPQR FAYYTDDLSS PPSALPTPQF GQRTTKSKKK KGHKGKNCII S
//