PIRT_MOUSE
ID PIRT_MOUSE Reviewed; 135 AA.
AC Q8BFY0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphoinositide-interacting protein;
GN Name=Pirt;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, PHOSPHOINOSITIDE-BINDING, DISRUPTION PHENOTYPE, INTERACTION WITH
RP TRPV1, AND MUTAGENESIS OF 113-LYS--LYS-115 AND 113-LYS--LYS-121.
RX PubMed=18455988; DOI=10.1016/j.cell.2008.02.053;
RA Kim A.Y., Tang Z., Liu Q., Patel K.N., Maag D., Geng Y., Dong X.;
RT "Pirt, a phosphoinositide-binding protein, functions as a regulatory
RT subunit of TRPV1.";
RL Cell 133:475-485(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, Spinal ganglion, and Vein;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Regulatory subunit of TRPV1, a molecular sensor of noxious
CC heat and capsaicin. Positively regulates TRPV1 channel activity via
CC phosphatidylinositol 4,5-bisphosphate (PIP2). Binds various
CC phosphoinositide, including phosphatidylinositol 4,5-bisphosphate
CC (PIP2), but not phosphatidylinositol (PI).
CC {ECO:0000269|PubMed:18455988}.
CC -!- SUBUNIT: Interacts with TRPV1. {ECO:0000269|PubMed:18455988}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in most dorsal root ganglia
CC (DRG) and trigeminal neurons. Expressed by most peptidergic (CGRP+) and
CC non-peptidergic (IB4+) DRG neurons. Weakly expressed in other parts of
CC the peripheral nervous system (PNS) including sympathetic and enteric
CC neurons. Not expressed in the spinal cord.
CC {ECO:0000269|PubMed:18455988}.
CC -!- DEVELOPMENTAL STAGE: First expressed in DRG neurons around embryonic
CC day 11.5, and expression is maintained throughout adulthood.
CC {ECO:0000269|PubMed:18455988}.
CC -!- DISRUPTION PHENOTYPE: Mice show impaired responsiveness to noxious heat
CC and capsaicin. Noxious heat- and capsaicin-sensitive currents in DRG
CC neurons are significantly attenuated. {ECO:0000269|PubMed:18455988}.
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DR EMBL; EU447173; ACC60974.1; -; mRNA.
DR EMBL; AK041182; BAC30853.1; -; mRNA.
DR EMBL; AK051285; BAC34593.1; -; mRNA.
DR EMBL; AK051645; BAC34704.1; -; mRNA.
DR EMBL; AK084056; BAC39108.1; -; mRNA.
DR EMBL; CH466601; EDL10416.1; -; Genomic_DNA.
DR EMBL; BC147296; AAI47297.1; -; mRNA.
DR EMBL; BC147297; AAI47298.1; -; mRNA.
DR CCDS; CCDS24849.1; -.
DR RefSeq; NP_848771.1; NM_178656.3.
DR RefSeq; XP_006532642.1; XM_006532579.3.
DR AlphaFoldDB; Q8BFY0; -.
DR SMR; Q8BFY0; -.
DR STRING; 10090.ENSMUSP00000128117; -.
DR PhosphoSitePlus; Q8BFY0; -.
DR PaxDb; Q8BFY0; -.
DR PRIDE; Q8BFY0; -.
DR ProteomicsDB; 289501; -.
DR Antibodypedia; 47967; 33 antibodies from 8 providers.
DR Ensembl; ENSMUST00000123434; ENSMUSP00000128117; ENSMUSG00000048070.
DR GeneID; 193003; -.
DR KEGG; mmu:193003; -.
DR UCSC; uc007jln.1; mouse.
DR CTD; 644139; -.
DR MGI; MGI:2443635; Pirt.
DR VEuPathDB; HostDB:ENSMUSG00000048070; -.
DR eggNOG; ENOG502S54V; Eukaryota.
DR GeneTree; ENSGT00940000154322; -.
DR HOGENOM; CLU_1906059_0_0_1; -.
DR InParanoid; Q8BFY0; -.
DR OMA; WIPIIRK; -.
DR PhylomeDB; Q8BFY0; -.
DR TreeFam; TF328608; -.
DR BioGRID-ORCS; 193003; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8BFY0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BFY0; protein.
DR Bgee; ENSMUSG00000048070; Expressed in dorsal root ganglion and 68 other tissues.
DR Genevisible; Q8BFY0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IDA:MGI.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:MGI.
DR GO; GO:2001259; P:positive regulation of cation channel activity; IMP:MGI.
DR GO; GO:0009408; P:response to heat; IMP:MGI.
DR InterPro; IPR028068; PIRT.
DR Pfam; PF15099; PIRT; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..135
FT /note="Phosphoinositide-interacting protein"
FT /id="PRO_0000347061"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 113..121
FT /note="KKKQKQRQK->AAAQAQAQA: Abolishes phosphoinositide-
FT binding but does not affect the interaction with TRPV1."
FT /evidence="ECO:0000269|PubMed:18455988"
FT MUTAGEN 113..115
FT /note="KKK->QQQ: Abolishes phosphoinositide-binding and
FT ability to activate TRPV1 without affecting the interaction
FT with TRPV1."
FT /evidence="ECO:0000269|PubMed:18455988"
SQ SEQUENCE 135 AA; 15264 MW; E171F42CFEFC86CC CRC64;
MEVLPKALEV DERSPESKDL LPSQTASSLC ISSRSESVWT TTPKSNWEIY HKPIIIMSVG
AAILLFGVAI TCVAYILEEK HKVVQVLRMI GPAFLSLGLM MLVCGLVWVP IIKKKQKQRQ
KSNFFQSLKF FLLNR
