Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoinositide-interacting protein

Gene

Pirt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of TRPV1, a molecular sensor of noxious heat and capsaicin. Positively regulates TRPV1 channel activity via phosphatidylinositol 4,5-bisphosphate (PIP2). Binds various phosphoinositide, including phosphatidylinositol 4,5-bisphosphate (PIP2), but not phosphatidylinositol (PI).1 Publication

GO - Molecular functioni

  • ion channel binding Source: MGI
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: MGI
  • phosphatidylinositol bisphosphate binding Source: MGI

GO - Biological processi

  • behavioral response to pain Source: MGI
  • phosphatidylinositol-mediated signaling Source: MGI
  • positive regulation of cation channel activity Source: MGI
  • response to heat Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoinositide-interacting protein
Gene namesi
Name:Pirt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2443635. Pirt.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei54 – 7421HelicalSequence analysisAdd
BLAST
Transmembranei92 – 11221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show impaired responsiveness to noxious heat and capsaicin. Noxious heat- and capsaicin-sensitive currents in DRG neurons are significantly attenuated.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi113 – 1219KKKQKQRQK → AAAQAQAQA: Abolishes phosphoinositide-binding but does not affect the interaction with TRPV1. 1 Publication
Mutagenesisi113 – 1153KKK → QQQ: Abolishes phosphoinositide-binding and ability to activate TRPV1 without affecting the interaction with TRPV1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 135135Phosphoinositide-interacting proteinPRO_0000347061Add
BLAST

Proteomic databases

PaxDbiQ8BFY0.
PRIDEiQ8BFY0.

PTM databases

PhosphoSiteiQ8BFY0.

Expressioni

Tissue specificityi

Strongly expressed in most dorsal root ganglia (DRG) and trigeminal neurons. Expressed by most peptidergic (CGRP+) and non-peptidergic (IB4+) DRG neurons. Weakly expressed in other parts of the peripheral nervous system (PNS) including sympathetic and enteric neurons. Not expressed in the spinal cord.1 Publication

Developmental stagei

First expressed in DRG neurons around embryonic day 11.5, and expression is maintained throughout adulthood.1 Publication

Gene expression databases

BgeeiQ8BFY0.
GenevisibleiQ8BFY0. MM.

Interactioni

Subunit structurei

Interacts with TRPV1.1 Publication

GO - Molecular functioni

  • ion channel binding Source: MGI

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IWQ6. Eukaryota.
ENOG410YYIW. LUCA.
GeneTreeiENSGT00390000016891.
HOGENOMiHOG000082413.
HOVERGENiHBG106144.
InParanoidiQ8BFY0.
OMAiQKSVFFQ.
OrthoDBiEOG718KF5.
PhylomeDBiQ8BFY0.
TreeFamiTF328608.

Family and domain databases

InterProiIPR028068. PIRT.
[Graphical view]
PfamiPF15099. PIRT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BFY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVLPKALEV DERSPESKDL LPSQTASSLC ISSRSESVWT TTPKSNWEIY
60 70 80 90 100
HKPIIIMSVG AAILLFGVAI TCVAYILEEK HKVVQVLRMI GPAFLSLGLM
110 120 130
MLVCGLVWVP IIKKKQKQRQ KSNFFQSLKF FLLNR
Length:135
Mass (Da):15,264
Last modified:March 1, 2003 - v1
Checksum:iE171F42CFEFC86CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU447173 mRNA. Translation: ACC60974.1.
AK041182 mRNA. Translation: BAC30853.1.
AK051285 mRNA. Translation: BAC34593.1.
AK051645 mRNA. Translation: BAC34704.1.
AK084056 mRNA. Translation: BAC39108.1.
CH466601 Genomic DNA. Translation: EDL10416.1.
BC147296 mRNA. Translation: AAI47297.1.
BC147297 mRNA. Translation: AAI47298.1.
CCDSiCCDS24849.1.
RefSeqiNP_848771.1. NM_178656.3.
XP_006532642.1. XM_006532579.2.
UniGeneiMm.440256.

Genome annotation databases

EnsembliENSMUST00000123434; ENSMUSP00000128117; ENSMUSG00000048070.
GeneIDi193003.
KEGGimmu:193003.
UCSCiuc007jln.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU447173 mRNA. Translation: ACC60974.1.
AK041182 mRNA. Translation: BAC30853.1.
AK051285 mRNA. Translation: BAC34593.1.
AK051645 mRNA. Translation: BAC34704.1.
AK084056 mRNA. Translation: BAC39108.1.
CH466601 Genomic DNA. Translation: EDL10416.1.
BC147296 mRNA. Translation: AAI47297.1.
BC147297 mRNA. Translation: AAI47298.1.
CCDSiCCDS24849.1.
RefSeqiNP_848771.1. NM_178656.3.
XP_006532642.1. XM_006532579.2.
UniGeneiMm.440256.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ8BFY0.

Proteomic databases

PaxDbiQ8BFY0.
PRIDEiQ8BFY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000123434; ENSMUSP00000128117; ENSMUSG00000048070.
GeneIDi193003.
KEGGimmu:193003.
UCSCiuc007jln.1. mouse.

Organism-specific databases

CTDi644139.
MGIiMGI:2443635. Pirt.

Phylogenomic databases

eggNOGiENOG410IWQ6. Eukaryota.
ENOG410YYIW. LUCA.
GeneTreeiENSGT00390000016891.
HOGENOMiHOG000082413.
HOVERGENiHBG106144.
InParanoidiQ8BFY0.
OMAiQKSVFFQ.
OrthoDBiEOG718KF5.
PhylomeDBiQ8BFY0.
TreeFamiTF328608.

Miscellaneous databases

NextBioi371406.
PROiQ8BFY0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BFY0.
GenevisibleiQ8BFY0. MM.

Family and domain databases

InterProiIPR028068. PIRT.
[Graphical view]
PfamiPF15099. PIRT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1."
    Kim A.Y., Tang Z., Liu Q., Patel K.N., Maag D., Geng Y., Dong X.
    Cell 133:475-485(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHOINOSITIDE-BINDING, DISRUPTION PHENOTYPE, INTERACTION WITH TRPV1, MUTAGENESIS OF 113-LYS--LYS-115 AND 113-LYS--LYS-121.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Aorta, Spinal ganglion and Vein.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.

Entry informationi

Entry nameiPIRT_MOUSE
AccessioniPrimary (citable) accession number: Q8BFY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: March 1, 2003
Last modified: January 20, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.