ID   CRIPT_RAT               Reviewed;         101 AA.
AC   Q792Q4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Cysteine-rich PDZ-binding protein;
DE   AltName: Full=Cysteine-rich interactor of PDZ three;
DE            Short=Cysteine-rich interactor of PDZ3;
GN   Name=Cript;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DLG4 AND TUBB1,
RP   MUTAGENESIS OF GLN-98; SER-100 AND VAL-101, AND TISSUE SPECIFICITY.
RX   PubMed=9581762; DOI=10.1016/s0896-6273(00)81009-0;
RA   Niethammer M., Valtschanoff J.G., Kapoor T.M., Allison D.W., Weinberg R.J.,
RA   Craig A.M., Sheng M.;
RT   "CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of
RT   PSD-95/SAP90.";
RL   Neuron 20:693-707(1998).
RN   [2]
RP   FUNCTION, ASSOCIATION WITH MICROTUBULE, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF VAL-101.
RX   PubMed=10570482; DOI=10.1038/15990;
RA   Passafaro M., Sala C., Niethammer M., Sheng M.;
RT   "Microtubule binding by CRIPT and its potential role in the synaptic
RT   clustering of PSD-95.";
RL   Nat. Neurosci. 2:1063-1069(1999).
CC   -!- FUNCTION: Involved in the cytoskeletal anchoring of DLG4 in excitatory
CC       synapses. {ECO:0000269|PubMed:10570482, ECO:0000269|PubMed:9581762}.
CC   -!- SUBUNIT: Interacts with DLG4 and TUBB1. Interacts strongly with the
CC       PDZ3 domain of members of the DLG4 family. Associates with
CC       microtubules. {ECO:0000269|PubMed:9581762}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10570482}. Synapse
CC       {ECO:0000269|PubMed:10570482}. Cell projection, dendritic spine
CC       {ECO:0000269|PubMed:10570482}. Note=Colocalizes with DLG4 in asymmetric
CC       synapses.
CC   -!- TISSUE SPECIFICITY: Expressed in striatum, cortex, midbrain, Purkinje
CC       cells of the cerebellum, pyramidal neurons of the hippocampus and
CC       neuropil. Expressed in heart, brain, lung, liver, kidney and testis.
CC       {ECO:0000269|PubMed:9581762}.
CC   -!- SIMILARITY: Belongs to the CRIPT family. {ECO:0000305}.
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DR   EMBL; AF047384; AAC40102.1; -; mRNA.
DR   RefSeq; NP_063972.1; NM_019907.1.
DR   PDB; 5HEB; X-ray; 1.65 A; B=93-101.
DR   PDB; 5HED; X-ray; 1.70 A; B=93-101.
DR   PDB; 5HEY; X-ray; 1.50 A; B=93-101.
DR   PDB; 5HF1; X-ray; 1.75 A; B=93-101.
DR   PDB; 5HFB; X-ray; 1.62 A; B=93-101.
DR   PDB; 5HFC; X-ray; 1.85 A; B=93-101.
DR   PDB; 5HFE; X-ray; 1.80 A; B=93-101.
DR   PDB; 5HFF; X-ray; 1.75 A; B=93-101.
DR   PDBsum; 5HEB; -.
DR   PDBsum; 5HED; -.
DR   PDBsum; 5HEY; -.
DR   PDBsum; 5HF1; -.
DR   PDBsum; 5HFB; -.
DR   PDBsum; 5HFC; -.
DR   PDBsum; 5HFE; -.
DR   PDBsum; 5HFF; -.
DR   AlphaFoldDB; Q792Q4; -.
DR   SMR; Q792Q4; -.
DR   BioGRID; 248569; 1.
DR   ELM; Q792Q4; -.
DR   IntAct; Q792Q4; 1.
DR   STRING; 10116.ENSRNOP00000020534; -.
DR   iPTMnet; Q792Q4; -.
DR   PhosphoSitePlus; Q792Q4; -.
DR   PaxDb; Q792Q4; -.
DR   PRIDE; Q792Q4; -.
DR   Ensembl; ENSRNOT00000020534; ENSRNOP00000020534; ENSRNOG00000015215.
DR   GeneID; 56725; -.
DR   KEGG; rno:56725; -.
DR   UCSC; RGD:621545; rat.
DR   CTD; 9419; -.
DR   RGD; 621545; Cript.
DR   eggNOG; KOG3476; Eukaryota.
DR   GeneTree; ENSGT00950000183100; -.
DR   HOGENOM; CLU_133934_0_0_1; -.
DR   InParanoid; Q792Q4; -.
DR   OMA; KTGFAIC; -.
DR   OrthoDB; 1599604at2759; -.
DR   PhylomeDB; Q792Q4; -.
DR   TreeFam; TF300144; -.
DR   PRO; PR:Q792Q4; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000015215; Expressed in thymus and 20 other tissues.
DR   Genevisible; Q792Q4; RN.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR   GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR   GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR   GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IDA:RGD.
DR   GO; GO:0045184; P:establishment of protein localization; IDA:RGD.
DR   GO; GO:0035372; P:protein localization to microtubule; IMP:UniProtKB.
DR   GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; IMP:UniProtKB.
DR   InterPro; IPR019367; PDZ-binding_CRIPT.
DR   PANTHER; PTHR11805; PTHR11805; 1.
DR   Pfam; PF10235; Cript; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell projection; Cytoplasm; Reference proteome; Synapse.
FT   CHAIN           1..101
FT                   /note="Cysteine-rich PDZ-binding protein"
FT                   /id="PRO_0000314565"
FT   REGION          19..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..101
FT                   /note="Sufficient for interaction with DLG4"
FT                   /evidence="ECO:0000269|PubMed:9581762"
FT   REGION          98..101
FT                   /note="PDZ3-binding"
FT   COMPBIAS        20..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         98
FT                   /note="Q->E: Abolishes interaction with DLG4. Strongly
FT                   abolishes interaction with DLG4; when associated with D-
FT                   100."
FT                   /evidence="ECO:0000269|PubMed:9581762"
FT   MUTAGEN         100
FT                   /note="S->D: Abolishes interaction with DLG4. Strongly
FT                   abolishes interaction with DLG4; when associated with E-
FT                   98."
FT                   /evidence="ECO:0000269|PubMed:9581762"
FT   MUTAGEN         101
FT                   /note="V->A: Abolishes interaction with DLG4. Does not
FT                   redistribute DLG4 to microtubules. Associates with
FT                   microtubules."
FT                   /evidence="ECO:0000269|PubMed:10570482,
FT                   ECO:0000269|PubMed:9581762"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:5HEY"
SQ   SEQUENCE   101 AA;  11271 MW;  161D694AC81BFDCB CRC64;
     MVCEKCEKKL GRVITPDTWK DGARNTTESG GRKLNENKAL TSKKARFDPY GKNKFSTCRI
     CKSSVHQPGS HYCQGCAYKK GICAMCGKKV LDTKNYKQTS V