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Protein

Cysteine-rich PDZ-binding protein

Gene

Cript

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses.2 Publications

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD
  • scaffold protein binding Source: Ensembl

GO - Biological processi

  • cytoplasmic microtubule organization Source: RGD
  • establishment of protein localization Source: RGD
  • protein localization to microtubule Source: UniProtKB
  • regulation of postsynaptic density protein 95 clustering Source: UniProtKB

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine-rich PDZ-binding protein
Alternative name(s):
Cysteine-rich interactor of PDZ three
Short name:
Cysteine-rich interactor of PDZ3
Gene namesi
Name:Cript
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi621545. Cript.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB-SubCell
  • dendrite Source: RGD
  • dendritic shaft Source: RGD
  • dendritic spine Source: RGD
  • neuronal cell body Source: RGD
  • nucleolus Source: Ensembl
  • postsynaptic density Source: RGD

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi98Q → E: Abolishes interaction with DLG4. Strongly abolishes interaction with DLG4; when associated with D-100. 1 Publication1
Mutagenesisi100S → D: Abolishes interaction with DLG4. Strongly abolishes interaction with DLG4; when associated with E-98. 1 Publication1
Mutagenesisi101V → A: Abolishes interaction with DLG4. Does not redistribute DLG4 to microtubules. Associates with microtubules. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003145651 – 101Cysteine-rich PDZ-binding proteinAdd BLAST101

Proteomic databases

PaxDbiQ792Q4.

PTM databases

iPTMnetiQ792Q4.
PhosphoSitePlusiQ792Q4.

Expressioni

Tissue specificityi

Expressed in striatum, cortex, midbrain, Purkinje cells of the cerebellum, pyramidal neurons of the hippocampus and neuropil. Expressed in heart, brain, lung, liver, kidney and testis.1 Publication

Gene expression databases

BgeeiENSRNOG00000015215.
GenevisibleiQ792Q4. RN.

Interactioni

Subunit structurei

Interacts with DLG4 and TUBB1. Interacts strongly with the PDZ3 domain of members of the DLG4 family. Associates with microtubules.1 Publication

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • PDZ domain binding Source: RGD
  • protein complex binding Source: RGD
  • scaffold protein binding Source: Ensembl

Protein-protein interaction databases

BioGridi248569. 1 interactor.
ELMiQ792Q4.
IntActiQ792Q4. 1 interactor.
STRINGi10116.ENSRNOP00000020534.

Structurei

Secondary structure

1101
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi98 – 100Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HEBX-ray1.65B93-101[»]
5HEDX-ray1.70B93-101[»]
5HEYX-ray1.50B93-101[»]
5HF1X-ray1.75B93-101[»]
5HFBX-ray1.62B93-101[»]
5HFCX-ray1.85B93-101[»]
5HFEX-ray1.80B93-101[»]
5HFFX-ray1.75B93-101[»]
SMRiQ792Q4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni95 – 101Sufficient for interaction with DLG41 Publication7
Regioni98 – 101PDZ3-binding4

Sequence similaritiesi

Belongs to the CRIPT family.Curated

Phylogenomic databases

eggNOGiKOG3476. Eukaryota.
ENOG4111RAI. LUCA.
GeneTreeiENSGT00390000002260.
HOGENOMiHOG000242625.
HOVERGENiHBG097641.
InParanoidiQ792Q4.
OMAiKYCHGCA.
OrthoDBiEOG091G0YCT.
PhylomeDBiQ792Q4.
TreeFamiTF300144.

Family and domain databases

InterProiView protein in InterPro
IPR019367. PDZ-binding_CRIPT.
PANTHERiPTHR11805. PTHR11805. 1 hit.
PfamiView protein in Pfam
PF10235. Cript. 1 hit.

Sequencei

Sequence statusi: Complete.

Q792Q4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVCEKCEKKL GRVITPDTWK DGARNTTESG GRKLNENKAL TSKKARFDPY
60 70 80 90 100
GKNKFSTCRI CKSSVHQPGS HYCQGCAYKK GICAMCGKKV LDTKNYKQTS

V
Length:101
Mass (Da):11,271
Last modified:July 5, 2004 - v1
Checksum:i161D694AC81BFDCB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047384 mRNA. Translation: AAC40102.1.
RefSeqiNP_063972.1. NM_019907.1.
UniGeneiRn.30508.

Genome annotation databases

EnsembliENSRNOT00000020534; ENSRNOP00000020534; ENSRNOG00000015215.
GeneIDi56725.
KEGGirno:56725.
UCSCiRGD:621545. rat.

Similar proteinsi

Entry informationi

Entry nameiCRIPT_RAT
AccessioniPrimary (citable) accession number: Q792Q4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: August 30, 2017
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families