TRIO_DANRE
ID TRIO_DANRE Reviewed; 3028 AA.
AC Q1LUA6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Triple functional domain protein;
DE EC=2.7.11.1;
GN Name=trio; ORFNames=si:dkey-158b13.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Promotes the exchange of GDP by GTP. Together with leukocyte
CC antigen-related (LAR) protein, it could play a role in coordinating
CC cell-matrix and cytoskeletal rearrangements necessary for cell
CC migration and cell growth (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The N-terminal DBL/GEF domain specifically catalyzes nucleotide
CC exchange for RAC1, leading to the activation of Jun kinase and the
CC production of membrane ruffles. The second DBL/GEF domain is an
CC exchange factor for rhoa and induces the formation of stress fibers (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine residue(s). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BX957244; CAK04109.1; -; Genomic_DNA.
DR EMBL; BX950864; CAK04109.1; JOINED; Genomic_DNA.
DR EMBL; BX950864; CAK05186.1; -; Genomic_DNA.
DR EMBL; BX957244; CAK05186.1; JOINED; Genomic_DNA.
DR SMR; Q1LUA6; -.
DR STRING; 7955.ENSDARP00000081489; -.
DR PaxDb; Q1LUA6; -.
DR ZFIN; ZDB-GENE-060503-334; trioa.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG4240; Eukaryota.
DR InParanoid; Q1LUA6; -.
DR PhylomeDB; Q1LUA6; -.
DR PRO; PR:Q1LUA6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 6.
DR Gene3D; 1.20.900.10; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR028570; Kalirin/TRIO.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF104; PTHR22826:SF104; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00409; IG; 1.
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; 7.
DR SUPFAM; SSF48065; SSF48065; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF52087; SSF52087; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Disulfide bond;
KW Guanine-nucleotide releasing factor; Immunoglobulin domain; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; SH3 domain; Transferase.
FT CHAIN 1..3028
FT /note="Triple functional domain protein"
FT /id="PRO_0000278475"
FT DOMAIN 5..151
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REPEAT 162..288
FT /note="Spectrin 1"
FT REPEAT 294..396
FT /note="Spectrin 2"
FT REPEAT 399..514
FT /note="Spectrin 3"
FT REPEAT 517..623
FT /note="Spectrin 4"
FT REPEAT 624..735
FT /note="Spectrin 5"
FT REPEAT 858..963
FT /note="Spectrin 6"
FT REPEAT 1089..1195
FT /note="Spectrin 7"
FT DOMAIN 1243..1418
FT /note="DH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1430..1542
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1606..1671
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1920..2096
FT /note="DH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 2108..2223
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 2480..2545
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 2615..2705
FT /note="Ig-like C2-type"
FT DOMAIN 2726..2980
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 227..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1834..1858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2242..2368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2391..2481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2566..2589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1881..1906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2345..2359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2400..2419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2453..2481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2845
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 2732..2740
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2755
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DISULFID 2636..2689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 3028 AA; 342362 MW; DD9984AD9BEFEA6D CRC64;
MKAMEVLPIL KEKVAFLSGG RDKRGGPVLT FPSRTNHDRI RHEDLRRLIA YLAGIPSEDV
CKHGFTVIVD MRGSKWDSIK PLLKILQESF PCCIHIALII KPDNFWQKQR TNFGSSKFEF
ETTMVSLEGL SKVVDPSQLT ADFEGSLDYN HEEWIEIRVA FEDFTGNARH LLARLEEMHE
TVTRKDLPQD LDGARRMIEE HAALKKRVIK APVEEVDNEG QRLLQRIQSS ESYANRTVPV
PPGQREGQGQ PNADTQGLVP RITALLEKLH STRQNLHQSW HIRKLQLDQC FQLRLFEQDA
EKMFDWIMHN KGLFLAGYTE IGNNHPHAME LQTQHNHFAM NCMNVYVNIN RIMSVGNRLL
EAGHYASQQI KQISGQLEQE WKAFAAALDE RSALLEMSAT FHQKCDQYMS NVDSWCKACG
EVDLPSELQE LEDAIHHHQG LYEHITAAYS EVSQDGKALL DKLQRPLTPG SADSLTASAN
YTKAVNHVLD IIHEVLHHQR QLENIWQHRK VRLHQRLQLC VFQQDVQQVL DWIENHGEAF
LSKHTGVGKS LHRARALQKR HEDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYQAA
HQLEDRIQDF VRRVEQRKVL LDMSVAFHTH VKELWTWLEE LQKELLDDVY AESVEAVQDL
IKRFGQQQQT TLQFTVNVIK EGEDLIQQLR DLAISSNKTP HNSSINHIES VLQQLDEAQA
QMEELFQERK IKLELFLQLR IFERDAIDII SDLDSWNEEL SQQMNEFDTE DLTLAEQRLQ
HHADKALTMN NLAFHVIHQG QELLQYVNEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ
QELDVAAEQH RRHLEQCVQL RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQRE
HEQFQHAIEK THQSALQVQQ KAEALLQANH YDMDMIRDCA ENVASHWQQL MLKMEDRLKL
VNASVAFYKT SEQVCSVLES LEQEYKREED WCGGADKLGP NCESDHVTPM ISKHLEQKEA
FLKACTLARR NADVFLKYMH RNSVSMPGML SHVKAPEQQV KNILNELLQR ENRVLHFWTM
RKRRLDQCQQ YVVFERSAKQ ALEWIHDTGE FYLSTHTSTG SSIHHTQELL KEHEDFHITA
KQTKERVKLL IQLADGFCDK GHSHAAEIKK WVTAVDKRYR DFSLRMDKYR TSLEKALGIS
SDSNKASKDL QLDIIPASAP GSEVKLRDAA HELNEEKRKS ARRKDFIMAE LIQTEKAYVR
DLRECMDTYL WEMTSGVEEI PPGIVNKEHI IFGNMQDLYE FHHNIFLKEL EKYEQLPEDV
GHCFVTWADK FQMYVNYCKN KPDSTQLILE HAGGYFDEIQ QRHRLANSIS SYLIKPVQRI
TKYQLLLKEL LTCCEEGKGE IKDGLEVMLS VPKRANDAMH LSMLEGFDEN IESQGELILQ
EAFQVWDPKT LIRKGRERHL FLFEMSLIFS KEVKDSNGRS KYIYKSKLFT SELGVTEHVE
GDPCKFALWV GRTPTSDNKI VLKASGIENK QDWIKHIREV IQERTVHLKG ALKEPIHIPK
ASTAKHKGRR DGEDLDSQGD GSSQPDTISL ASRTSQNTLD SDKLSGGCEL TVVIHDFMAG
NSNELTIRRG QTVEVLERLH DKPDWCLVRT TDRSPALEGL VPCAMLCIAH SRSSMEMEGI
FNHKDALSVC SNDAIMPGSS ATLQPGHVMG SQSSPGPKRP GNTLRKWLTS PVRRLSSGKA
DGHVKKLAHK HKKSRDVRKS ADAGSQKDSD DSAATPQDET LEERVRNEGL SSGTLSKSSS
SGMQSCGEEE GEEGADAVPL PPPMAIQQHS LLQPDAQDDK TSSRLSVRPS SSETPSAAEL
VSAIEELVKS KMALEDRPST LSVEQGDSSS PSFNPSDNSL LSSSSPIDEI EERKTGFFKK
RHYVLLELIE TERDYVRDLS LVVEGYMARM REDGVPDDMK GKDKIVFGNI QQIYDWHKDF
FLGELEKCLE DPDRLGPLFL KHERRLHMYI VYCQNKPKSE HIVSEYIDTY FEDLKQRLGH
RLQITDLLIK PVQRIMKYQL LLKDFLKFSK KIGTDSIELE KAVEVMCIVP KRCNDMMNVG
RLQGFDGKIV AQGRLLLQDT FMVAEPEGGL LNRMKERRVF LFEQIVIFSE PLDKKRGFSM
PGYLYKYSIK VNCLGLEDSV DGDPCKFALT SRTSNSSKDA FILHSSHPGV RQVWMLQISQ
ILESQRNFLN ALTSPIDYQR NHVEGPGVSG SGVQAGGSGG QMMAPGGGVG VPAGPGSRSR
PSRIPQPSRL PQPLRHHSPA LGPGAHEHDG PDKLSGMSPR PLSRGPSPSC TTEPEPKVKL
PASPHPKQTD SQQTESPAKE IPRATVAPLA LVKPRPGTVS PMASPLATPA FKDSIPPCSP
GPKTGSSSFW SSVPASPASR PASFTFPGDA CDTLSRPNHN QSQRHSTHSK DADRMSTCSS
TSEQSIQSTQ SNGSESSSSS NISTMLVTQD YVALKEDEIN VGQGEVVQIL ASNQQNMFLV
FRAATEQCPA AEGWIPGYVL GHTSAIIPDA PDGTIKKSSS SWHTSLRIRK KSEKREKDNK
KEAKLENGYR KSREGLTNKV SVKLLNPNYI YDVLPEFLVP LSDVTCDKGE CVTLRCKVCG
RPKATVTWKG PEQKTLTNNG HFSIAYSETG EATLRIVGVT SEDDGSYTCI ATNDIGSVAS
SASLRVLGTT SDGIRVMWKD NFESFYTEVA ELGRGRFSVV KRCDQRGSKR TVAVKFVNKK
LMKRDQVTHE FSVLQRLQHP HLVRLLDTFE TSSSYALVLE MSDQGRLLDY IVSWGNLTEE
KVAFYLRDIL EALQYLHNCR IVHLDLKPEN LVVEQSPSQP LVKLTDFGDA VQLNSTPYVH
PLLGSPEFAA PELVLGDPVS LSSDLWSLGV LTYVMLSGAS PFLDESVEET CLNICRLDFS
FPDDYFQGVS QAARDFMCLL LRMEPSKRPP ATSCLQEPWL RAGGGRRSAE CIDTSRLISF
IDRRKHQNDL RPLTGIRAFL QTRLQPRI
