Q4G017 · NISCH_RAT

Function

function

Acts either as the functional imidazoline-1 receptor (I1R) candidate or as a membrane-associated mediator of the I1R signaling. Binds numerous imidazoline ligands that induces initiation of cell-signaling cascades triggering to cell survival, growth and migration. Its activation by the agonist rilmenidine induces an increase in phosphorylation of mitogen-activated protein kinases MAPK1 and MAPK3 in rostral ventrolateral medulla (RVLM) neurons that exhibited rilmenidine-evoked hypotension. Blocking its activation with efaroxan abolished rilmenidine-induced mitogen-activated protein kinase phosphorylation in RVLM neurons. Acts as a modulator of Rac-regulated signal transduction pathways (By similarity).
Suppresses Rac1-stimulated cell migration by interacting with PAK1 and inhibiting its kinase activity (By similarity).
Also blocks Pak-independent Rac signaling by interacting with RAC1 and inhibiting Rac1-stimulated NF-kB response element and cyclin D1 promoter activation (By similarity).
Inhibits also LIMK1 kinase activity by reducing LIMK1 'Tyr-508' phosphorylation (By similarity).
Inhibits Rac-induced cell migration and invasion in breast and colon epithelial cells (By similarity).
Inhibits lamellipodia formation, when overexpressed (By similarity).
Plays a role in protection against apoptosis (By similarity).
Involved in association with IRS4 in the enhancement of insulin activation of MAPK1 and MAPK3 (By similarity).
When overexpressed, induces a redistribution of cell surface ITGA5 integrin to intracellular endosomal structures (By similarity).

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentearly endosome
Cellular Componentplasma membrane
Cellular Componentrecycling endosome
Molecular Functionalpha-tubulin binding
Molecular Functiondynein heavy chain binding
Molecular Functionidentical protein binding
Molecular Functionintegrin binding
Molecular Functionphosphatidylinositol binding
Biological Processactin cytoskeleton organization
Biological Processapoptotic process
Biological Processglucose metabolic process
Biological Processnegative regulation of cell migration
Biological Processnorepinephrine secretion
Biological Processouter dynein arm assembly
Biological ProcessRac protein signal transduction
Biological Processregulation of blood pressure
Biological Processregulation of synaptic transmission, GABAergic

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nischarin
  • Alternative names
    • Imidazoline receptor 1 (I-1; IR1)
    • Imidazoline-1 receptor (I1R)

Gene names

    • Name
      Nisch

Organism names

  • Taxonomic identifier
  • Strain
    • Brown Norway
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q4G017

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
Cytoplasm
Early endosome
Recycling endosome
Note: Enriched in the early/sorting and recycling endosomes. Colocalized in early/sorting endosomes with EEA1 and SNX2 and in recycling endosomes with transferrin receptor. Detected in the perinuclear region partially associated with punctate structures. Colocalizes with PAK1 in cytoplasm, vesicular structures in the perinuclear area and membrane ruffles. Colocalizes with RAC1 in the cytoplasm and vesicles structures (By similarity).
Colocalized with MAPK1 and MAPK3 in RVLM neurons

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003482671-1502Nischarin
Modified residue542Phosphoserine
Modified residue544Phosphoserine
Modified residue547Phosphoserine
Modified residue1280Phosphothreonine
Modified residue1282Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homooligomer. Interacts with GRB2. Interacts with PIK3R1; probably associates with the PI3-kinase complex. Interacts with IRS4. Found in a complex with ITGA5 and PAK1. Found in a complex with LIMK1 and PAK1. Interacts with ITGA5 (via cytoplasmic domain); this interaction is direct. Interacts with PAK1 (via kinase domain); this interaction is direct and is increased upon activation of PAK1. Interacts with LIMK1 (via PDZ and kinase domain); this interaction is direct. Interacts with LIMK2; this interaction depends on LIMK2 activity. Interacts with RAC1 (activated state) (By similarity).
Interacts with STK11; this interaction may increase STK11 activity (By similarity).

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Features

Showing features for region, domain, repeat, coiled coil, compositional bias.

TypeIDPosition(s)Description
Region1-134Necessary for binding to phosphoinositide-3-P; not sufficient for targeting to endosomes
Domain12-122PX
Region121-693Necessary for homooligomerization and targeting to endosomes
Region246-867Interaction with PAK1
Repeat289-310LRR 1
Repeat312-333LRR 2
Repeat334-355LRR 3
Repeat357-378LRR 4
Repeat379-400LRR 5
Repeat404-425LRR 6
Region481-501Disordered
Region524-549Disordered
Coiled coil623-692
Region628-684Disordered
Compositional bias635-650Acidic residues
Region659-867Interaction with LIMK
Compositional bias660-684Acidic residues
Region707-805Interaction with ITGA5
Region1014-1101Disordered

Domain

Both the presence of the PX domain and the coiled coil region are necessary for its endosomal targeting.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,502
  • Mass (Da)
    166,503
  • Last updated
    2008-09-02 v2
  • Checksum
    E89025E32450ECF8
MAAATLSFGPEREAEPAKEARVVGSELVDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKIDKTLLPPKKIIGKNSRSLVEKREKDLEVYLQTLLKTFPDVAPRVLAHFLHFHLYEINGVTAALAEELFEKGEQLLGAGEVFAIRPLQLYAITEQLQQGKPTCASGDAKTDLGHILDFTCRLKYLKVSGTEGPFGTSNIREQLLPFDLSIFKSLHQVEMSHCDAKHVRGLVTSKPTLATMSVRFSAASMKEVLVPEASEFDEWEPEGTTLGGPVTAVIPTWQALTTLDLSHNSISEIDESVKLIPKIEYLDLSHNGVLVVDNLQHLYNLVHLDLSYNKLSSLEGVHTKLGNVKTLNLAGNFLERLSGLHKLYSLVNLDLRDNRIEQLDEVKSIGNLPCLEHVALLNNPLSIIPDYRTKVLSQFGERASEICLDDVATTEKELDTVEVLKAIQKAKDVKSKLSSTEKKVGEDFRLPTAPCIRPSSSPPTAVPTSASLPQPILSNQGIMFVQEEALASSLSSTDSLPPDDRPIAQACSNSMGSLPTGQVAAEDLRDLPGAVGGVSPDHAEPEVQVVPGSGQIIFLPFTCIGYTATNQDFIQRLSTLIRQAIERQLPAWIEAANQREEAHGEQGEEEEEEEEEDVAESRYFEMGPPDAEEEEGSGQGEEDEEDEDEEAEEERLALEWALGADEDFLLEHIRILKVLWCFLIHVQGSIRQFAACLVLTDFGIAVFEIPHQESRGSSQHILSSLRFVFCFPHGDLTEFGFLMPELCLVLKVRHSENTLFIISDAANLHEFHADLRSCFAPQHMAMLCSPILYGSHTSLQEFLRQLLTFYKVAGGSQERSQGCFPVYLVYSDKRMVQTAAGDYSGNIEWASCTLCSAVRRSCCAPSEAVKSAAIPYWLLLTSQHLNVIKADFNPMPSRGTHNCRNRNSFKLSRVPLSTVLLDPTRSCTQPRGAFADGHVLELLVGYRFVTAIFVLPHEKFHFLRVYNQLRASLKDLKTVVIAKNPSARPRTQGPLAGGQPAKSRVSAEQRLQETPAEAPAPAPAAAESAAEAPAAAEASAPAGAPAPAGAPAPAGAPAGAQAPAPAQAEVPAQYPSERLIQSTSEENQIPSHLPVCPSLQHIARLRGRAIIDLFHSSIAEVENEELRHLLWSSVVFYQTPGLEVTACVLLSTKAVYFILHDGLRRYFSEPLQDFWHQKNTDYNNSPFHISQCFVLKLSDLQSVNVGLFDQYFRLTGSSPTQVVTCLTRDSYLTHCFLQHLMLVLSSLERTPSPEPIDKDFYSEFGDKNTGKMENYELIHSSRVKFTYPSEEEVGDLTYVVAQKMADPAKNPALSILLYIQAFQVITPQLGRGRGPLRPKTLLLTSAEIFLLDEDYIHYPLPEFAKEPPQRDRYRLDDGRRVRDLDRVLMGYNPYPQALTLVFDDTQGHDLMGSVTLDHFGEMPGGPGRAGQGREVQWQVFVPSAESREKLISLLARQWEALCGRELPVELTG

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6AMT4A0A8I6AMT4_RATNisch1624
A0A8I6ATD2A0A8I6ATD2_RATNisch516
A0A8I5ZTG9A0A8I5ZTG9_RATNisch1646
A0A8L2QGU1A0A8L2QGU1_RATNisch1495

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias635-650Acidic residues
Compositional bias660-684Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AABR03100261
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC098837
EMBL· GenBank· DDBJ
AAH98837.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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