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CRIPT_MOUSE
ID   CRIPT_MOUSE             Reviewed;         101 AA.
AC   O70333; Q99LR6; Q9DBP4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
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   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].
RC   STRAIN=BALB/cJ; TISSUE=Testis;
RA   Sebire K.L., de Kretser D.M., O'Bryan M.K.;
RT   "Cloning and sequencing of mouse testicular CRIPT.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Lung, and Small intestine;
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 MRNA].
RC   STRAIN=Czech II, and FVB/N-3; TISSUE=Mammary tumor;
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).
RN   [4]
RP   INTERACTION WITH DLG4.
RX   PubMed=17474715; DOI=10.1021/bi062088k;
RA   Saro D., Li T., Rupasinghe C., Paredes A., Caspers N., Spaller M.R.;
RT   "A thermodynamic ligand binding study of the third PDZ domain (PDZ3) from
RT   the mammalian neuronal protein PSD-95.";
RL   Biochemistry 46:6340-6352(2007).
CC   -!- FUNCTION: Involved in the cytoskeletal anchoring of DLG4 in excitatory
CC       synapses. {ECO:0000250|UniProtKB:Q792Q4}.
CC   -!- SUBUNIT: Interacts with TUBB1. Interacts strongly with the PDZ3 domain
CC       of members of the DLG4 family. Associates with microtubules (By
CC       similarity). Interacts with DLG4. {ECO:0000250,
CC       ECO:0000269|PubMed:17474715}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}.
CC       Cell projection, dendritic spine {ECO:0000250}. Note=Colocalizes with
CC       DLG4 in asymmetric synapses. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CRIPT family. {ECO:0000305}.
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DR   EMBL; AF151637; AAD38045.1; -; mRNA.
DR   EMBL; AK004828; BAB23596.1; -; mRNA.
DR   EMBL; AK008523; BAB25719.1; -; mRNA.
DR   EMBL; AK029409; BAC26438.1; -; mRNA.
DR   EMBL; BC002258; AAH02258.1; -; mRNA.
DR   EMBL; BC023013; AAH23013.1; -; mRNA.
DR   CCDS; CCDS29012.1; -.
DR   RefSeq; NP_064320.1; NM_019936.3.
DR   AlphaFoldDB; O70333; -.
DR   SMR; O70333; -.
DR   BioGRID; 208145; 1.
DR   IntAct; O70333; 1.
DR   STRING; 10090.ENSMUSP00000024959; -.
DR   iPTMnet; O70333; -.
DR   PhosphoSitePlus; O70333; -.
DR   EPD; O70333; -.
DR   MaxQB; O70333; -.
DR   PaxDb; O70333; -.
DR   PRIDE; O70333; -.
DR   ProteomicsDB; 284170; -.
DR   Antibodypedia; 29983; 101 antibodies from 22 providers.
DR   DNASU; 56724; -.
DR   Ensembl; ENSMUST00000024959; ENSMUSP00000024959; ENSMUSG00000024146.
DR   GeneID; 56724; -.
DR   KEGG; mmu:56724; -.
DR   UCSC; uc008duo.2; mouse.
DR   CTD; 9419; -.
DR   MGI; MGI:1929655; Cript.
DR   VEuPathDB; HostDB:ENSMUSG00000024146; -.
DR   eggNOG; KOG3476; Eukaryota.
DR   GeneTree; ENSGT00950000183100; -.
DR   HOGENOM; CLU_133934_0_0_1; -.
DR   InParanoid; O70333; -.
DR   OMA; KTGFAIC; -.
DR   OrthoDB; 1599604at2759; -.
DR   PhylomeDB; O70333; -.
DR   TreeFam; TF300144; -.
DR   BioGRID-ORCS; 56724; 17 hits in 71 CRISPR screens.
DR   ChiTaRS; Cript; mouse.
DR   PRO; PR:O70333; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; O70333; protein.
DR   Bgee; ENSMUSG00000024146; Expressed in animal zygote and 260 other tissues.
DR   Genevisible; O70333; MM.
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; ISS:UniProtKB.
DR   GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:CAFA.
DR   GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR   GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR   GO; GO:0035372; P:protein localization to microtubule; ISS:UniProtKB.
DR   GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; ISS:CAFA.
DR   InterPro; IPR019367; PDZ-binding_CRIPT.
DR   PANTHER; PTHR11805; PTHR11805; 1.
DR   Pfam; PF10235; Cript; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cytoplasm; Reference proteome; Synapse.
FT   CHAIN           1..101
FT                   /note="Cysteine-rich PDZ-binding protein"
FT                   /id="PRO_0000314564"
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:17474715"
FT   REGION          98..101
FT                   /note="PDZ3-binding"
FT   COMPBIAS        20..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        86
FT                   /note="C -> Y (in Ref. 2; BAB23596)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   101 AA;  11271 MW;  161D694AC81BFDCB CRC64;
     MVCEKCEKKL GRVITPDTWK DGARNTTESG GRKLNENKAL TSKKARFDPY GKNKFSTCRI
     CKSSVHQPGS HYCQGCAYKK GICAMCGKKV LDTKNYKQTS V
 
 
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