PRIC1_MOUSE
ID PRIC1_MOUSE Reviewed; 832 AA.
AC Q3U5C7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Prickle-like protein 1;
DE Flags: Precursor;
GN Name=Prickle1;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-592; SER-595 AND
RP SER-684, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, and Testis;
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).
CC -!- FUNCTION: Involved in the planar cell polarity pathway that controls
CC convergent extension during gastrulation and neural tube closure (By
CC similarity). Convergent extension is a complex morphogenetic process
CC during which cells elongate, move mediolaterally, and intercalate
CC between neighboring cells, leading to convergence toward the
CC mediolateral axis and extension along the anteroposterior axis.
CC Necessary for nuclear localization of REST. May serve as nuclear
CC receptor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with REST. {ECO:0000250|UniProtKB:Q96MT3}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}. Cytoplasm,
CC cytosol {ECO:0000250}. Note=A smaller amount is detected in the
CC cytosol. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; AK153711; BAE32152.1; -; mRNA.
DR EMBL; BC117892; AAI17893.1; -; mRNA.
DR EMBL; BC117893; AAI17894.1; -; mRNA.
DR CCDS; CCDS27769.1; -.
DR RefSeq; NP_001028389.1; NM_001033217.4.
DR RefSeq; XP_006520327.1; XM_006520264.3.
DR RefSeq; XP_006520328.1; XM_006520265.1.
DR RefSeq; XP_006520329.1; XM_006520266.3.
DR AlphaFoldDB; Q3U5C7; -.
DR SMR; Q3U5C7; -.
DR BioGRID; 222980; 44.
DR IntAct; Q3U5C7; 1.
DR MINT; Q3U5C7; -.
DR STRING; 10090.ENSMUSP00000104878; -.
DR iPTMnet; Q3U5C7; -.
DR PhosphoSitePlus; Q3U5C7; -.
DR EPD; Q3U5C7; -.
DR jPOST; Q3U5C7; -.
DR MaxQB; Q3U5C7; -.
DR PaxDb; Q3U5C7; -.
DR PeptideAtlas; Q3U5C7; -.
DR PRIDE; Q3U5C7; -.
DR ProteomicsDB; 291559; -.
DR Antibodypedia; 13204; 140 antibodies from 23 providers.
DR Ensembl; ENSMUST00000048982; ENSMUSP00000049204; ENSMUSG00000036158.
DR Ensembl; ENSMUST00000109255; ENSMUSP00000104878; ENSMUSG00000036158.
DR GeneID; 106042; -.
DR KEGG; mmu:106042; -.
DR UCSC; uc007xja.1; mouse.
DR CTD; 144165; -.
DR MGI; MGI:1916034; Prickle1.
DR VEuPathDB; HostDB:ENSMUSG00000036158; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000157529; -.
DR HOGENOM; CLU_008937_5_0_1; -.
DR InParanoid; Q3U5C7; -.
DR OMA; PFCCNCF; -.
DR OrthoDB; 997264at2759; -.
DR PhylomeDB; Q3U5C7; -.
DR TreeFam; TF313265; -.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR BioGRID-ORCS; 106042; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Prickle1; mouse.
DR PRO; PR:Q3U5C7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3U5C7; protein.
DR Bgee; ENSMUSG00000036158; Expressed in digit and 300 other tissues.
DR Genevisible; Q3U5C7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:2000691; P:negative regulation of cardiac muscle cell myoblast differentiation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0001843; P:neural tube closure; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR CDD; cd09418; LIM2_Prickle; 1.
DR CDD; cd09420; LIM3_Prickle; 1.
DR CDD; cd09827; PET_Prickle; 1.
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 Cytoplasm; LIM domain; Lipoprotein; Membrane; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc.
FT CHAIN 1..829
FT /note="Prickle-like protein 1"
FT /id="PRO_0000283027"
FT PROPEP 830..832
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396713"
FT DOMAIN 14..122
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 124..188
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 250..313
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 314..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 765..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..832
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 829
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 829
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 832 AA; 94131 MW; 8E664AAEA2E23CEA CRC64;
MPLEMEPKMS KLVFGCQRSS TSDDDSGCAL EEYAWVPPGL RPEQIQLYFA CLPEEKVPYV
NSPGEKHRIK QLLYQLPPHD NEVRYCQSLS EEEKKELQVF SAQRKKEALG RGTIKLLSRA
VMHAVCEQCG LQMNGGEVAV FASRAGPGVC WHPSCFVCFT CNELLVDLIY FYQDGKIHCG
RHHAELLKPR CSACDEIIFA DECTEAEGRH WHMKHFCCLE CETVLGGQRY IMKDGRPFCC
GCFESLYAEY CETCGEHIGV DHAQMTYDGQ HWHATEACFS CAQCKASLLG CPFLPKQGQI
YCSKTCSLGE DIHASDSSDS AFQSARSRDS RRSVRMGRSS RSADQCRQSL LLSPALNYKF
PGLSGNADDT LSRKLDDVSL ASRQGAGFAN EEFWKARVEQ EASEDPEEWA EHEDYMTQLL
LKFGDKNLFQ QQSSEVDPRA SEHWIPDNMV TNKPEVKPNH QGLASKKYQS DMYWAQSQDG
LGDSAYGSHP GPASSRRLQE LDLDHGAAGY THDQSQWYED SLECLSDLKP EQSIRDSMDS
LALSNITGAS VDGESKPRPS LYSLQNFEEI EAEDCEKMSN MGTLNSSMLH RSAESLQSLN
SGLCPEKILP EEKPAHLPVL RRSKSQSRPQ QVKFSDDVID NGSYDIEIRQ PPMSERTRRR
AYHFEERGSR PHHHRHRRSR KSRSDNALNL VTERKYSAKD RLRLYTPDNY EKFIQNKSAR
ELQAYMQNAN LYSQYAHATS DYALQNPGMN RFLGLCGEDD DSWCSSSTSS SDSEEEGYFL
GQPIPQPRPQ RFTYYTDDLS SPASALPTPQ FTQRTTKSKK KKGHKGKNCI IS
