PRIC2_MOUSE
ID PRIC2_MOUSE Reviewed; 845 AA.
AC Q80Y24; A6H652;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Prickle-like protein 2;
DE Flags: Precursor;
GN Name=Prickle2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP IDENTIFICATION, AND CHARACTERIZATION.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-321; SER-322;
RP THR-535; THR-537; THR-540; SER-544; SER-547; SER-608; SER-643 AND SER-732,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus and cerebral cortex.
CC {ECO:0000269|PubMed:21276947}.
CC -!- DISRUPTION PHENOTYPE: Null mice are viable, but show an increased
CC seizure rate compared to heterozygous mice, indicating a dosage effect.
CC Heterozygous Prickle2 +/- mice have a decreased seizure threshold
CC compared to wild-type. {ECO:0000269|PubMed:21276947}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50793.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH466523; EDK99322.1; -; Genomic_DNA.
DR EMBL; BC145754; AAI45755.1; -; mRNA.
DR EMBL; BC050793; AAH50793.1; ALT_INIT; mRNA.
DR CCDS; CCDS51854.1; -.
DR RefSeq; NP_001127931.1; NM_001134459.1.
DR RefSeq; NP_001127932.1; NM_001134460.2.
DR RefSeq; NP_001127933.1; NM_001134461.1.
DR AlphaFoldDB; Q80Y24; -.
DR SMR; Q80Y24; -.
DR BioGRID; 232537; 54.
DR IntAct; Q80Y24; 2.
DR MINT; Q80Y24; -.
DR STRING; 10090.ENSMUSP00000109073; -.
DR iPTMnet; Q80Y24; -.
DR MaxQB; Q80Y24; -.
DR PaxDb; Q80Y24; -.
DR PRIDE; Q80Y24; -.
DR ProteomicsDB; 291560; -.
DR Antibodypedia; 50866; 76 antibodies from 20 providers.
DR DNASU; 243548; -.
DR Ensembl; ENSMUST00000113445; ENSMUSP00000109072; ENSMUSG00000030020.
DR Ensembl; ENSMUST00000113446; ENSMUSP00000109073; ENSMUSG00000030020.
DR Ensembl; ENSMUST00000113447; ENSMUSP00000109074; ENSMUSG00000030020.
DR GeneID; 243548; -.
DR KEGG; mmu:243548; -.
DR UCSC; uc009cyx.2; mouse.
DR CTD; 166336; -.
DR MGI; MGI:1925144; Prickle2.
DR VEuPathDB; HostDB:ENSMUSG00000030020; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000153629; -.
DR HOGENOM; CLU_008937_5_0_1; -.
DR InParanoid; Q80Y24; -.
DR OMA; LHQSFDF; -.
DR OrthoDB; 997264at2759; -.
DR TreeFam; TF313265; -.
DR BioGRID-ORCS; 243548; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Prickle2; mouse.
DR PRO; PR:Q80Y24; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80Y24; protein.
DR Bgee; ENSMUSG00000030020; Expressed in piriform cortex and 236 other tissues.
DR ExpressionAtlas; Q80Y24; baseline and differential.
DR Genevisible; Q80Y24; MM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IDA:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
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 1: Evidence at protein level;
KW LIM domain; Lipoprotein; Membrane; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc.
FT CHAIN 1..842
FT /note="Prickle-like protein 2"
FT /id="PRO_0000075892"
FT PROPEP 843..845
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396719"
FT DOMAIN 18..126
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 128..193
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 193..253
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 253..317
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 314..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 535
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 842
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 842
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 273
FT /note="G -> D (in Ref. 2; AAH50793)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 845 AA; 95781 MW; 234C14897AD3F261 CRC64;
MVTVMPLEME KTISKLMFDF QRSSTSDDDS GCALEEYAWV PPGLKPEQVH QYYSCLPEEK
VPYVNSAGEK LRIKQLLHQL PPHDNEVRYC NSLDEEEKRE LKLFSNQRKR ENLGRGNVRP
FPVTMTGAIC EQCGGQIKGG DIAVFASRAG HGICWHPPCF VCTVCNELLV DLIYFYQDGK
IYCGRHHAEC LKPRCAACDE IIFADECTEA EGRHWHMRHF CCFECETVLG GQRYIMKEGR
PYCCHCFESL YAEYCDTCAQ HIGIDQGQMT YDGQHWHATE TCFCCAHCKK SLLGRPFLPK
QGQIFCSRAC SAGEDPNGSD SSDSAFQNAR AKESRRSAKI GKNKGKTEEA MLNQHSQLQV
SSNRLSADVD PLSVQMDLLS LSSQTPSLNR DPIWRSREEP FHYGNKMEQN QSQSPLQLLS
QCNIRTSYSP GGQGAGAQPD MWAKHFSNPK RSSSMALKGH GGSFIQECRE DYYPGRLMSQ
ESYSDMSSQS FNETRGSIPV PKYEEEEEEE EGGISTQQCR PRRPLSSLKY TEDMTPTEQT
PRGSMESLAL SNATGLSAEG GAKRQEHLSR FSMPDLSKDS GMNVSEKLSN MGTLNSSMQF
RSAESVRSLL SAQQYQEMEG NLHQLSNPLG YRDLQSHGRM HQSFDFDGGI ASSKLPGQEG
VHIQPMSERT RRRTTSRDDN RRFRPHRSRR SRRSRSDNAL HLASEREVIA RLKERPPLRA
REDYDQFMRQ RSFQESLGQG SRRDLYSQCP RTVSDLALQN AFGERWGPYF TEYDWCSTCS
SSSESDNEGY FLGEPIPQPA RLRYVTSDEL LHKYSSYGVP KSSTLGGRGQ LHSRKRQKSK
NCIIS
