ID A0A2K6Q9X8_RHIRO Unreviewed; 3073 AA.
AC A0A2K6Q9X8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=TRIO {ECO:0000313|Ensembl:ENSRROP00000025597.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000025597.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000025597.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR STRING; 61622.ENSRROP00000025597; -.
DR Ensembl; ENSRROT00000049815.1; ENSRROP00000025597.1; ENSRROG00000036518.1.
DR GeneTree; ENSGT00940000154766; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11852; SH3_Kalirin_1; 1.
DR CDD; cd11853; SH3_Kalirin_2; 1.
DR CDD; cd00176; SPEC; 6.
DR CDD; cd14113; STKc_Trio_C; 1.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR028570; Kalirin_TRIO_SH3_1.
DR InterPro; IPR047053; Kalirin_TRIO_SH3_2.
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; 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; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF104; TRIPLE FUNCTIONAL DOMAIN PROTEIN; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 1.
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; 6.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
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; 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 {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 42..187
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1269..1444
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1456..1568
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1633..1698
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1946..2122
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2134..2248
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2527..2592
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2661..2751
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2772..3026
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1578..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1756..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1904..1942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2264..2528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2615..2636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 734..761
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1605..1627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1908..1932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2328..2350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2351..2365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2372..2389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2456..2489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2500..2528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3073 AA; 345812 MW; 0C56201356F8A579 CRC64;
LCLRALLCPG HDICGHGCGN GRKHAFSHLR FRKNDEMKAM DVLPILKEKV AYLSGGRDKR
GGPILTFPAR SNHDRIRQED LRRLISYLAY IPSEEVCKRG FTVIVDMRGS KWDSIKPLLK
ILQESFPCCI HVALIIKPDN FWQKQRTNFG SSKFEFETNM VSLEGLTKVV DPSQLTPEFD
GCLEYNHEEW IEIRVAFEDY ISNATHMLSR LEELQDILAK KELPQDLEGA RNMIEEHSQL
KKKVIKAPIE DLDLEGQKLL QRIQSSESFP KKNSGSGNAD LQNLLPKVST MLDRLHSTRQ
HLHQMWHVRK LKLDQCFQLR LFEQDAEKMF DWITHNKGLF LNSYTEIGTS HPHAMELQTQ
HNHFAMNCMN VYVNINRIMS VANRLVESGH YASQQIRQIA SQLEQEWKAF AAALDERSTL
LDMSSIFHQK AEKYMSNVDS WCKACGEVDL PSELQDLEDA IHHHQGIYEH ITLAYSEVSQ
DGKSLLDKLQ RPLTPGSSDS LTASANYSKA VHHVLDVIHE VLHHQRQLEN IWQHRKVRLH
QRLQLCVFQQ DVQQVLDWIE NHGEAFLSKH TGVGKSLHRA RALQKRHEDF EEVAQNTYTN
ADKLLEAAEQ LAQTGECDPE EIYQAAHQLE DRIQDFVRRV EQRKILLDMS VSFHTHVKEL
WTWLEELQKE LLDDVYAESV EAVQDLIKRF GQQQQTTLQV TVNVIKEGED LIQQLRDSAI
SSNKTPHNSS INHIETVLQQ LDEAQSQMEE LFQERKIKLE LFLQLRIFER DAIDIISDLE
SWNDELSQQM NDFDTEDLTI AEQRLQHHAD KALTMNNLTF DVIHQGQDLL QYVNEVQASG
VELLCDRDVD MATRVQDLLE FLHEKQQELD LAAEQHRKHL EQCVQLRHLQ AEVKQVLGWI
RNGESMLNAG LITASSLQEA EQLQREHEQF QHAIEKTHQS ALQVQQKAEA MLQANHYDMD
MIRDCAEKVA SHWQQLMLKM EDRLKLVNAS VAFYKTSEQV CSVLESLEQE YKREEDWCGG
ADKLGPNSET DHVTPMISKH LEQKEAFLKA CTLARRNADV FLKYLHRNSV NMPGMVTHIK
APEQQVKNIL NELFQRENRV LHYWTMRKRR LDQCQQYVVF ERSAKQALEW IHDNGEFYLS
THTSTGSSIQ HTQELLKEHE EFQITAKQTK ERVKLLIQLA DGFCEKGHAH AAEIKKCVTA
VDKRYRDFSL RMEKYRTSLE KALGISSDSN KSSKSLQLDI IPASIPGSEV KLRDAAHELN
EEKRKSARRK EFIMAELIQT EKAYVRDLRE CMDTYLWEMT SGVEEIPPGI VNKELIIFGN
MQEIYEFHNN IFLKELEKYE QLPEDVGHCF VTWADKFQMY VTYCKNKPDS TQLILEHAGS
YFDEIQQRHG LANSISSYLI KPVQRITKYQ LLLKELLTCC EEGKGEIKDG LEVMLSVPKR
ANDAMHLSML EGFDENIESQ GELILQESFQ VWDPKTLIRK GRERHLFLFE MSLVFSKEVK
DSSGRSKYLY KSKLFTSELG VTEHVEGDPC KFALWVGRTP TSDNKIVLKA SSIENKQDWI
KHIREVIQER TIHLKGALKE PIHIPKTAPA TRQKGRRDGE DLDSQGDGSS QPDTISIASR
TSQNTLDSDK LSGGCELTVV IHDFTACNSN ELTIRRGQTV EVLERPHDKP DWCLVRTTDR
SPAAEGLVPC GSLCIAHSRS SMEMEGIFNH KDSLSVSSND ASPPASVASL QPHMIGAQSS
PGPKRPGNTL RKWLTSPVRR LSSGKADGHV KKLAHKHKKS REVRKSADAG SQKDSDDSAA
TPQDETVEER GRNEGLSSGT LSKSSSSGMQ SCGEEEGEEG ADAVPLPPPM AIQQHSLLQP
DSQDDKASSR LLVRPTSSET PSAAELVSAI EELVKSKMAL EDRPSSLLVD QGDSSSPSFN
PSDNSLLSSS SPIDEMEERK SSSLKRRHYV LQELVETERD YVRDLGYVVE GYMALMKEDG
VPDDMKGKDK IVFGNIHQIY DWHRDFFLGE LEKCLEDPEK LGSLFVKHER RLHMYIVYCQ
NKPKSEHIVS EYIDTFFEDL KQRLGHRLQL TDLLIKPVQR IMKYQLLLKD FLKYSKKASL
DTSELERAVE VMCIVPRRCN DMMNVGRLQG FDGKIVAQGK LLLQDTFLVT DQDAGLLPRC
RERRIFLFEQ IVIFSEPLDK KKGFSMPGFL FKNSIKVSCL CLEENVENDP CKFALTSRTG
DVVETFILHS SSPSVRQTWI HEINQILENQ RNFLNALTSP IEYQRNHSGG GGGSGGSGGG
GGSGGSGAPS GSSGHSGGPG SCGGAPSTSR SRPSRIPQPV RHHPPVLVSS AASSQAEADK
MSGTSTPGPS LPTPGAAPEA GPSAPSRRPP GADSEGSERE AEPIPKMKVL ESPRKCAANA
SGPSPDAHAK DARASLGALP LGKPRPGAAS PLNSPLSSAV PSPLGKEPFP PSSPLQKGGS
FWSSIPASPA SRPGSFTFPG DSDSLQRQTP RHAAPGKDTD RMSTCSSASE QSVQSTQSNG
SESSSSSNIS TMLVTHDYTA VKEDEINVYQ GEVVQILASN QQNMFLVFRA ATDQCPAAEG
WIPGFVLGHT SAVIVENPDG TLKKSTSWHT ALRLRKKSEK KDKDGKREGK LENGYRKSRE
GLSNKVSVKL LNPNYIYDVP PEFVIPLSEV TCETGETVVL RCRVCGRPKA SITWKGPEHN
TLNNDGHYSI SYSDLGEATL KIVGVTTEDD GIYTCIAVND MGSASSSASL RVLGPGMDGI
MVTWKDNFDS FYSEVAELGR GRFSVVKKCD QKGTKRAVAT KFVNKKLMKR DQVTHELGIL
QSLQHPLLVG LLDTFETPTS YVLVLEMADQ GRLLDCVVRW GSLTEGKIRA HLGEVLEAVR
YLHNCRIAHL DLKPENILVD ESLAKPTIKL ADFGDAVQLN TTYYIHQLLG NPEFAAPEII
LGNPVSLTSD TWSVGVLTYV LLSGVSPFLD DSVEETCLNI CRLDFSFPDD YFKGVSQKAK
EFVCFLLQED PAKRPSAALA LQEQWLQAGN GRSTGVLDTS RLTSFIERRK HQNDVRPIRS
IKNFLQSRLL PRV
//
