(data stored in ACNUC5448 zone)

HOGENOM: MOUSE15_PE185

ID   MOUSE15_PE185                        STANDARD;      PRT;   1849 AA.
AC   MOUSE15_PE185; Q0KL02; Q3U522; Q6P9K6; Q80W23;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Triple functional domain protein; EC=2.7.11 1;
DE   (MOUSE15.PE185).
GN   Name=Trio;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE15.PE185.
CC       Mus musculus chromosome 15 NCBIM37  sequence 1..103494974 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:TRIO_MOUSE
CC   -!- FUNCTION: Promotes the exchange of GDP by GTP. Together with
CC       leukocyte antigen-related (LAR) protein, it could play a role in
CC       coordinating cell-matrix and cytoskeletal rearrangements necessary
CC       for cell migration and cell growth (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts to form a complex with leukocyte antigen
CC       related protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Isoform 2 localizes to early
CC       endosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q0KL02-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0KL02-2; Sequence=VSP_023308, VSP_023309;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q0KL02-3; Sequence=VSP_037863, VSP_037864, VSP_037865;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q0KL02-4; Sequence=VSP_037863;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widespread in the brain, with more intense
CC       signals in the hippocampus, olfactory bulb, cortical layers and
CC       cerebellum. Isoform 2 is predominantly expressed in Purkinje
CC       neurons of brain.
CC   -!- DOMAIN: The N-terminal DBL/GEF domain specifically catalyzes
CC       nucleotide exchange for RAC1, leading to the activation of Jun
CC       kinase and the production of membrane ruffles. The second DBL/GEF
CC       domain is an exchange factor for rhoa and induces the formation of
CC       stress fibers (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SIMILARITY: Contains 2 DH (DBL-homology) domains.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
CC   -!- SIMILARITY: Contains 4 spectrin repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE32258.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000044462 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000022263;ENSMUST00000100733;ENSMUSP00000098299.
DR   EMBL; AB106872; - ;
DR   EMBL; AC107452; - ;
DR   EMBL; AC116808; - ;
DR   EMBL; AC120373; - ;
DR   EMBL; AC130219; - ;
DR   EMBL; AK153924; - ;
DR   EMBL; BC051169; - ;
DR   EMBL; BC060724; - ;
DR   UniProtKB/Swiss-Prot; Q0KL02; Q3U522; Q6P9K6; Q80W23; -.
DR   EMBL; AB106872; BAF30811.1; -; mRNA.
DR   EMBL; AC107452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC130219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC051169; AAH51169.1; -; mRNA.
DR   EMBL; BC060724; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK153924; BAE32258.1; ALT_INIT; mRNA.
DR   IPI; IPI00604947; -.
DR   IPI; IPI00605176; -.
DR   IPI; IPI00943997; -.
DR   IPI; IPI00944152; -.
DR   RefSeq; NP_001074771.1; NM_001081302.1.
DR   UniGene; Mm.485422; -.
DR   ProteinModelPortal; Q0KL02; -.
DR   SMR; Q0KL02; 217-445, 565-715, 754-1011, 1255-1594, 1655-1721, 1960-2291, 2558-2783, 2791-3089.
DR   STRING; Q0KL02; -.
DR   PhosphoSite; Q0KL02; -.
DR   PRIDE; Q0KL02; -.
DR   Ensembl; ENSMUST00000090247; ENSMUSP00000087714; ENSMUSG00000022263.
DR   GeneID; 223435; -.
DR   KEGG; mmu:223435; -.
DR   UCSC; uc007vjw.1; mouse.
DR   UCSC; uc007vjx.1; mouse.
DR   CTD; 7204; -.
DR   MGI; MGI:1927230; Trio.
DR   eggNOG; roNOG06885; -.
DR   GeneTree; ENSGT00560000076675; -.
DR   InParanoid; Q0KL02; -.
DR   OrthoDB; EOG4H462T; -.
DR   NextBio; 376714; -.
DR   ArrayExpress; Q0KL02; -.
DR   Bgee; Q0KL02; -.
DR   CleanEx; MM_TRIO; -.
DR   Genevestigator; Q0KL02; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 2.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00621; RhoGEF; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 2.
DR   SMART; SM00150; SPEC; 6.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF48065; DH-domain; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   HOGENOMDNA; MOUSE15.PE185; -.
KW   ENSMUSG000000222635old_1320000031; ENSMUSP000000982991old_1320000031;
KW   AB106872; AC107452; AC116808; AC120373; AC130219; AK153924; BC051169;
KW   BC060724;
KW   Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
KW   Disulfide bond; Guanine-nucleotide releasing factor;
KW   Immunoglobulin domain; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase;
KW   SH3 domain; Transferase.
SQ   SEQUENCE   1849 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKAMDVLPIL KEKVAYLSGG RDKRGGPILT FPARSNHDRI RQEDLRRLIS YLACIPSEEV
     CKRGFTVIVD MRGSKWDSIK PLLKILQESF PCCIHIALII KPDNFWQKQR TNFGSSKFEF
     ETNMVSLEGL TKVVDPSQLT PEFDGCLEYN HEEWIEIRVA FEEYISNAAH MLSRLEELQD
     VLAKKELPQD LEGARNMIDE HSQLKKKVIK APIEDLDLEG QKLLQRIQSS DSFPKKNSGS
     GNADLQNLLP KVSTMLDRLH STRQHLHQMW HVRKLKLDQC FQLRLFEQDA EKMFDWITHN
     KGLFLNSYTE IGTSHPHAME LQTQHNHFAM NCMNVYVNIN RIMSVANRLV ESGHYASQQI
     KQIANQLEQE WKAFAAALDE RSTLLDMSSI FHQKAEKYMS NVDSWCKACG EVDLPSELQD
     LEDAIHHHQG IYEHITLAYS EVSQDGKSLL DKLQRPLTPG SSDSLTASAN YSKAVHHVLD
     VIHEVLHHQR QLENIWQHRK VRLHQRLQLC VFQQDVQQVL DWIENHGEAF LSKHTGVGKS
     LHRARALQKR HEDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYQAA HQLEDRIQDF
     VRRVEQRKIL LDMSVSFHTH VKELWTWLEE LQKELLDDVY AESVEAVQDL IKRFGQQQQT
     TLQVTVNVIK EGEDLIQQLR DSAISSNKTP HNSSINHIET VLQQLDEAQS QMEELFQERK
     IKLELFLQLR IFERDAIDII SDLESWNDEL SQQMNDFDTE DLTIAEQRLQ HHADKALTMN
     NLTFDVIHQG QDLLQYVNEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ QELDLAAEQH
     RKHLEQCVQL RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQRE HEQFQHAIEK
     THQSALQVQQ KAEAMLQANH YDMDMIRDCA EKVASHWQQL MLKMEDRLKL VNASVAFYKT
     SEQVCSVLES LEQEYKREED WCGGADKLGP NSETDHVTPM ISKHLEQKEA FLKACTLARR
     NADVFLKYLH RNSVSMPGMV THIKAPEQQV KNILNELFQR ENRVLHYWTM RKRRLDQCQQ
     YVVFERSAKQ ALEWIHDNGE FYLSTHTSTG SSIQHTQELL KEHEEFQITA KQTKERVKLL
     IQLADGFCEK GHAHAAEIKK CVTAVDKRYR DFSLRMEKYR TSLEKALGIS SDSNKSSKSL
     QLDIIPASIP GSEVKLRDAA HELNEEKRKS ARRKEFIMAE LIQTEKAYVR DLRECMDTYL
     WEMTSGVEEI PPGIVNKELI IFGNMQEIYE FHNNIFLKEL EKYEQLPEDV GHCFVTWADK
     FQMYVTYCKN KPDSTQLILE HAGSYFDEIQ QRHGLANSIS SYLIKPVQRI TKYQLLLKEL
     LTCCEEGKGE IKDGLEVMLS VPKRANDAMH LSMLEGFDEN IESQGELILQ ESFQVWDPKT
     LIRKGRERHL FLFEMSLVFS KEVKDSSGRS KYLYKSKLFT SELGVTEHVE GDPCKFALWV
     GRTPTSDNKI VLKASSIENK QDWIKHIREV IQERTVHLRG ALKEPIHIPK TAPAARQKGR
     RDGEDLDSQG DGSSQPDTIS IASRTSQNTL DSDKLSGGCE LTVVIHDFTA CNSNELTIRR
     GQTVEVLERP HDKPDWCLVR TTDRSPAAEG LVPCGSLCIA HSRSSMEMEG IFNHKDSLSV
     SSNDASPPAS VASLQPHMIG AQSSPGPKRP GNTLRKWLTS PVRRLSSGKA DGHAKKLAHK
     HKKSREVRKS ADAGSQKDSD DSAATPQDET IEERGRNEGL SSGTLSKSSS SGMQSCGEEE
     GEEGADAVPL PPPMAIQQHS LLQPDSQDDK HYVDLCSVSV LAQFPYLSI
//

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