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0TRIO_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTRIO
DescriptionTriple functional domain protein (ptprf interacting protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005085 guanyl-nucleotide exchange factor activity (TAS)
0004674 protein serine/threonine kinase activity (TAS)
0007185 transmembrane receptor protein tyrosine pho... (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . CAUTION: Despite SMART having created two different HMMs for Serine/Threonine protein kinase and for Tyrosine protein kinase.arge number of proteins match both signatures.s SMART considers it to be natural for these two closely related families.
  IPR002290:Serine/threonine protein kinase
This entry defines the C-terminal of various retinaldehyde/retinal-binding proteins that may befunctional components of the visual cycle. Cellular retinaldehyde-binding protein (CRALBP) carries 11-cis-retinol or 11-cis-retinaldehyde as endogenous ligands and may function as a substrate carrier protein that modulates interaction of these retinoids with visual cycle enzymes . The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase.ontains a protein kinase domain.nd has separate rac-specific and rho-specific guanine nucleotide exchange factor domains . Trio is a multifunctional protein that integrates and amplifies signals involved in coordinating actin remodeling.hich is necessary for cell migration and growth.Other members of the family are transfer proteins that include.uanine nucleotide exchange factor that may function as an effector of RAC1.hosphatidylinositol/phosphatidylcholine transfer protein that is required for the transport of secretory proteins from the golgicomplex and alpha-tocopherol transfer protein that enhances the transfer of the ligand between separate membranes.
  IPR001251:Cellular retinaldehyde-binding/triple function, C-terminal
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents I-set domains.hich are found in several cell adhesion molecules.ncluding vascular (VCAM).ntercellular (ICAM).eural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules.s well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families.ncluding several tyrosine-protein kinase receptors.he hemolymph protein hemolin.he muscle proteins titin.elokin.nd twitchin.he neuronal adhesion molecule axonin-1 .nd the signalling molecule semaphorin 4D that is involved in axonal guidance.mmune function and angiogenesis .
  IPR013098:Immunoglobulin I-set
The pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like vav.bl.oS and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
  IPR001849:Pleckstrin-like
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents a subtype of the immunoglobulin domain.nd is found in a diverse range of protein families that includes glycoproteins.ibroblast growth factor receptors.ascular endothelial growth factor receptors.nterleukin-6 receptor.nd neural cell adhesion molecules. It also includes proteins that are classified as unassigned proteinase inhibitors belonging to MEROPS inhibitor families I2.17 and I43 .
  IPR003598:Immunoglobulin subtype 2
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
Spectrin repeats are found in several proteins involved incytoskeletal structure. These include spectrin.lpha-actininand dystrophin. The spectrin repeat forms athree helix bundle. The second helix is interrupted by prolinein some sequences. The repeats are defined by a characteristictryptophan (W) residue at position 17 in helix A and a leucine(L) at 2 residues from the carboxyl end of helix C.
  IPR002017:Spectrin repeat
The Rho family GTPases Rho.ac and CDC42 regulate a diverse array of cellularprocesses. Like all members of the Ras superfamily.he Rho proteins cycle between active GTP-bound and inactive GDP-bound conformational states.Activation of Rho proteins through release of bound GDP and subsequentbinding of GTP.s catalyzed by guanine nucleotide exchange factors (GEFs) inthe Dbl family. The proteins encoded by members of the Dbl family share acommon domain.resented in this entry.f about 200 residues (designated the Dbl homology or DH domain)that has been shown to encode a GEF activity specific for a number of Rhofamily members. In addition.ll family members possess a second.hareddomain designated the pleckstrin homology (PH) domain (). Trioand its homolog UNC-73 are unique within the Dbl family insomuch as theyencode two distinct DH/PH domain modules. The PH domain is invariably locatedimmediately C-terminal to the DH domain and this invariant topography suggestsa functional interdependence between these two structural modules. Biochemicaldata have established the role of the conserved DH domain in Rho GTPaseinteraction and activation.nd the role of the tandem PH domain inintracellular targeting and/or regulation of DH domain function. The DH domainof Dbl has been shown to mediate oligomerization that is mostly homophilic innature. In addition to the tandem DH/PH domains Dbl family GEFs containdiverse structural motifs like serine/threonine kinase.BD.DZ.GS.Q.EM.dc25RasGEF.H.H2.H3.F.pectrin or Ig.The DH domain is composed of three structurally conserved regions separated bymore variable regions. It does not share significant sequence homology withother subtypes of small G-protein GEF motifs such as the Cdc25 domain and theSec7 domain.hich specifically interact with Ras and ARFfamily small GTPases.espectively.or with other Rho protein interactivemotifs.ndicating that the Dbl family proteins are evolutionarily unique. TheDH domain is composed of 11 alpha helices that are folded into a flattened.longated alpha-helix bundle in which two of the three conserved regions.onserved region 1 (CR1) and conserved region 3 (CR3).re exposed near thecenter of one surface. CR1 and CR3.ogether with a part of alpha-6 and theDH/PH junction site.onstitute the Rho GTPase interacting pocket.
  IPR000219:DH
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR002290:S_TKc 
Evalue:-71.8860566476932 
Location:2737-2991IPR000219:RhoGEF 
Evalue:-63.8239087409443 
Location:1914-2085IPR000219:RhoGEF 
Evalue:-52.568636235841 
Location:1237-1407IPR001251:SEC14 
Evalue:-25.7447274948967 
Location:9-148IPR013098:I-set 
Evalue:-24.5376014709473 
Location:2626-2717IPR002017:SPEC 
Evalue:-17.1611509092627 
Location:1082-1184IPR001849:PH 
Evalue:-16.1307678222656 
Location:1421-1532IPR002017:SPEC 
Evalue:-14.4559319556497 
Location:284-386IPR002017:SPEC 
Evalue:-12.7212463990472 
Location:510-612IPR002017:SPEC 
Evalue:-11.5850266520292 
Location:851-952IPR001849:PH 
Evalue:-10.6575775146484 
Location:2099-2212IPR002017:SPEC 
Evalue:-8.30102999566398 
Location:162-278IPR001452:SH3 
Evalue:-7.74472749489669 
Location:1600-1661IPR002017:SPEC 
Evalue:-5.92081875395237 
Location:615-724IPR001452:SH3 
Evalue:-0.431798275933005 
Location:2495-2564IPR000719:PROTEIN_KINASE_ATP 
Evalue:0 
Location:0-0
SequencesProtein: TRIO_HUMAN (3038 aa)
mRNA: AF091395 NM_007118
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 55 residues, 14196828-14196991Exon2: 27 residues, 14323933-14324008Exon3: 40 residues, 14333430-14333545Exon4: 66 residues, 14339979-14340172Exon5: 173 residues, 14343824-14344337Exon6: 43 residues, 14346120-14346243Exon7: 66 residues, 14350180-14350372Exon8: 46 residues, 14357569-14357701Exon9: 79 residues, 14369621-14369852Exon10: 43 residues, 14383886-14384009Exon11: 66 residues, 14389644-14389836Exon12: 58 residues, 14411286-14411456Exon13: 60 residues, 14412465-14412640Exon14: 67 residues, 14416840-14417036Exon15: 57 residues, 14417758-14417925Exon16: 42 residues, 14419968-14420088Exon17: 66 residues, 14421816-14422008Exon18: 52 residues, 14422482-14422632Exon19: 40 residues, 14427337-14427452Exon20: 40 residues, 14431120-14431236Exon21: 43 residues, 14434238-14434361Exon22: 67 residues, 14440546-14440741Exon23: 40 residues, 14440840-14440956Exon24: 24 residues, 14441721-14441788Exon25: 38 residues, 14442397-14442507Exon26: 25 residues, 14443339-14443409Exon27: 32 residues, 14444009-14444099Exon28: 33 residues, 14447146-14447239Exon29: 39 residues, 14450151-14450263Exon30: 65 residues, 14451988-14452179Exon31: 36 residues, 14454071-14454173Exon32: 49 residues, 14458956-14459099Exon33: 35 residues, 14459681-14459781Exon34: 83 residues, 14472886-14473130Exon35: 99 residues, 14514127-14514420Exon36: 59 residues, 14515863-14516034Exon37: 34 residues, 14518653-14518749Exon38: 51 residues, 14524426-14524575Exon39: 24 residues, 14525700-14525767Exon40: 36 residues, 14527102-14527206Exon41: 25 residues, 14530002-14530072Exon42: 32 residues, 14532369-14532459Exon43: 33 residues, 14533027-14533120Exon44: 19 residues, 14534342-14534393Exon45: 28 residues, 14534649-14534727Exon46: 66 residues, 14535690-14535882Exon47: 61 residues, 14538177-14538355Exon48: 267 residues, 14540572-14541369Exon49: 84 residues, 14545675-14545923Exon50: 48 residues, 14549987-14550126Exon51: 11 residues, 14550955-14550983Exon52: 56 residues, 14551197-14551360Exon53: 42 residues, 14551627-14551749Exon54: 28 residues, 14555687-14555766Exon55: 69 residues, 14557501-14557702Exon56: 48 residues, 14560230-14560369Exon57: 489 residues, 14560988-14562450Exon58: 2 residues, -Jump to TRIO_HUMANExon1: 16 residues, 14196945-14196991Exon2: 27 residues, 14323933-14324008Exon3: 40 residues, 14333430-14333545Exon4: 66 residues, 14339979-14340172Exon5: 173 residues, 14343824-14344337Exon6: 43 residues, 14346120-14346243Exon7: 66 residues, 14350180-14350372Exon8: 46 residues, 14357569-14357701Exon9: 79 residues, 14369621-14369852Exon10: 43 residues, 14383886-14384009Exon11: 66 residues, 14389644-14389836Exon12: 58 residues, 14411286-14411456Exon13: 60 residues, 14412465-14412640Exon14: 67 residues, 14416840-14417036Exon15: 57 residues, 14417758-14417925Exon16: 42 residues, 14419968-14420088Exon17: 66 residues, 14421816-14422008Exon18: 52 residues, 14422482-14422632Exon19: 40 residues, 14427337-14427452Exon20: 40 residues, 14431120-14431236Exon21: 43 residues, 14434238-14434361Exon22: 67 residues, 14440546-14440741Exon23: 40 residues, 14440840-14440956Exon24: 24 residues, 14441721-14441788Exon25: 38 residues, 14442397-14442507Exon26: 25 residues, 14443339-14443409Exon27: 32 residues, 14444009-14444099Exon28: 33 residues, 14447146-14447239Exon29: 39 residues, 14450151-14450263Exon30: 65 residues, 14451988-14452179Exon31: 36 residues, 14454071-14454173Exon32: 49 residues, 14458956-14459099Exon33: 35 residues, 14459681-14459781Exon34: 83 residues, 14472886-14473130Exon35: 99 residues, 14514127-14514420Exon36: 59 residues, 14515863-14516034Exon37: 34 residues, 14518653-14518749Exon38: 51 residues, 14524426-14524575Exon39: 24 residues, 14525700-14525767Exon40: 36 residues, 14527102-14527206Exon41: 25 residues, 14530002-14530072Exon42: 32 residues, 14532369-14532459Exon43: 33 residues, 14533027-14533120Exon44: 19 residues, 14534342-14534393Exon45: 28 residues, 14534649-14534727Exon46: 66 residues, 14535690-14535882Exon47: 61 residues, 14538177-14538355Exon48: 267 residues, 14540572-14541369Exon49: 84 residues, 14545675-14545923Exon50: 48 residues, 14549987-14550126Exon51: 11 residues, 14550955-14550983Exon52: 56 residues, 14551197-14551360Exon53: 42 residues, 14551627-14551749Exon54: 28 residues, 14555687-14555766Exon55: 69 residues, 14557501-14557702Exon56: 48 residues, 14560230-14560369Exon57: 267 residues, 14560988-14561785Exon58: 2 residues, -Jump to TRIO_HUMAN  
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