ID A0A669ERS6_ORENI Unreviewed; 2989 AA.
AC A0A669ERS6;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 10-JUN-2026, entry version 30.
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:ENSONIP00000075669.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000075669.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000075669.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-2026) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSONIT00000050048.1; ENSONIP00000075669.1; ENSONIG00000007788.2.
DR GeneTree; ENSGT00940000154766; -.
DR Proteomes; UP000005207; Linkage group LG22.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0007411; P:axon guidance; IEA:TreeGrafter.
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 FunFam; 1.20.900.10:FF:000001; Guanine nucleotide exchange factor DBS; 1.
DR FunFam; 1.10.510.10:FF:000152; kalirin isoform X1; 1.
DR FunFam; 2.30.30.40:FF:000038; kalirin isoform X1; 1.
DR FunFam; 2.30.30.40:FF:000040; kalirin isoform X1; 1.
DR FunFam; 2.60.40.10:FF:000368; kalirin isoform X1; 1.
DR FunFam; 1.20.58.60:FF:000034; kalirin isoform X2; 1.
DR FunFam; 3.40.525.10:FF:000003; kalirin isoform X2; 1.
DR FunFam; 1.20.58.60:FF:000024; Kalirin RhoGEF kinase a; 1.
DR FunFam; 1.20.58.60:FF:000023; Kalirin RhoGEF kinase b; 1.
DR FunFam; 1.20.58.60:FF:000032; Kalirin RhoGEF kinase b; 1.
DR FunFam; 1.20.900.10:FF:000008; rho guanine nucleotide exchange factor 25; 1.
DR FunFam; 1.20.58.60:FF:000015; triple functional domain protein-like; 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; 3.30.200.20; Phosphorylase Kinase, domain 1; 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_dom.
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; IPR058918; KALRN/TRIO-like_spectrin.
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; IPR051336; RhoGEF_Guanine_NuclExch_SF.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR055251; SOS1_NGEF_PH.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF106; TRIO, ISOFORM A; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF07679; I-set; 1.
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; PF23587; SH3_KALRN; 1.
DR Pfam; PF22697; SOS1_NGEF_PH; 2.
DR Pfam; PF00435; Spectrin; 4.
DR Pfam; PF23323; Spectrin_6; 1.
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; 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; 5.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 12..158
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1234..1409
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1587..1652
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1903..2079
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2091..2206
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2446..2511
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2580..2671
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2684..2939
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1679..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1858..1891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2222..2448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2532..2552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 695..725
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1726..1737
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1789
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1826..1835
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1870..1888
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2239..2267
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2364..2378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2431..2448
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2538..2552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2989 AA; 337756 MW; 2E47249408BF694A CRC64;
GFRRNEEMRA MEVLPILKEK VAFLSGGRDR RGGPVLTFPS RSNHDRIRTD DLRRLIAYLA
GIPSEEVCKH GFTVIVDMRG SKWDSIKPLL KILQESFPSC IHIALIIKPD NFWQKQRTNF
GSSKFEFETT MVSLEGLTKV VDPSQLTADF DGSLDYNHEE WIEVRVAFED FSGHATQMLA
RLEEMQETVS RKDFPQDLEG ARRMIEEHAT LKKKVIKAPI EELDTEGQRL LQRIQSSDGV
CNADTQGLVP RITQLLDKLH STRQHLHQAW HVRKLQLDQC FQLRLFEQDA EKMFDWIMHN
KGLFLAGYTE IGNNHPHAVE LQTQHSHFAM NCMNVYVNIN RIMSVGNRLL ESGHYASQQI
KQISSQLEQE WKAFAAALDE RSTLLEMSAG FHQKCDQYMS NVDSWCKACG EVDLPSELQD
LEDAIHHHQG LYEHITAAYS EVSQDGKALL DKLQRPLTPG SADSLTATAN YSKAVHHVLD
IIHEVLHHQR QLENIWQHRK VRLHQRLQLC VFQQDVQQVL DWIENHGEAF LSKHTGVGKS
LHRARALQKR HEDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYQAA HQLEDRIQDF
VRRVEQRKVL LDMSVAFHTH VKELWTWLEE LQKELLDDVY AESVEAVQDL IKRFGQQQQT
TLQVTVNVIK EGEDLIQQLR DSAISSNKTP HNSSINHIES VLQQLDEAQA QMEELFQERK
IKLELFLQLR IFERDAIDII SDLESWNEEL TGQMNDFDTE DLTLAEQRLQ HHADKALTMN
NLTFDVIHQG QELLQYVNEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ QELDLAAEQH
RRHLEQCVQL RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQRE HEQFQHAIEK
THQSALQVQQ KAEALLQANH YDMDMIRDCA ESVASHWQQL MLKMEDRLKL VNASVAFYKT
SEQVCSVLES LEQEYKREED WCGGADKLGP NCETDHVTPM ISKHLEQKEA FLKACTLARR
NADVFLKYMH RNSVNMPGML SHVKAPEQQV KNILNELLQR ENRVLHFWTM KKRRLDQCQQ
YVVFERSAKQ ALEWIHDTGE FYLSTHTSTG SSIHHTQELL KEHEEFHITA KQTKERVKLL
IQLADGFCEK GHSHAGEIKK WVTAVDKRYR DFSLRMDKYR CSLEKALGIS SDSNKASKDL
QLDIIPATAP GSEVKLRDAA AHELNEEKRK SARRKEFIMA ELIQTEKAYV RDLRECMDTY
LWEMTSGVEE IPPGILNKEH IIFGNMQDLY EFHHNIFLKE LEKYEQLPED VGHCFVTWAD
KFQMYVNYCK NKPDSTQLIL EHAGNYFDEI QQRHRLANSI SSYLIKPVQR ITKYQLLLKE
LLTCCEEGKG EIKDGLEVML SVPKKANDAM HLSMLEGFDE NIESQGELIL QDSFQVWDPK
TLIRKGRERH LFLFEMSLVF SKEVKDSNGR SKYIYKSKLF TSELGVTEHV EGDPCKFALW
VGRTPTSDNK IVLKVKHSSS SLLFYLTVYC TIYTRREEKL HLLLIVCAPI RDGEDLDSQG
EGSSQPDTIS LASRTSQNTL DSDKLSGGCE LTVVIHDFMA SNSNELTVRR GQTVEVLERC
HDKPDWCLVR TTDRSPAQEG LVPCSMLCIA HSRSSMEMEG IFNHKDTLSV CSNDSIMPGS
SATLQPGHGI GSHTSPGPKR PGNTLRKWLT SPVRRLSSGK ADGHVKKLAH KHKKSREVRK
SGEMTIGSQK DSDDSAATPQ DETLEERVRN EGLSSGTLSK SSSSGMQSCG EEEGEEGADS
VPLPPPMAIQ QHSLLQPDSQ DDKTSSRLSV RPSSSETPSA AELVSAIEEL VKSKMALEDR
PSSLSVEQGD SSSPSFNPSD NSLLSSSSPM EEMDERRASI LKKRHFILLE LVETERDYVR
DLGLVVEGYM SRMKEEGVPD DMKGKDKIVF GNIHQIYDWH KDFFLRELEK CLEDPDRLGP
LFLKQERRLN MYVVYCQNKP KSEHIVSEYI DTYFEDLKQR LGHRLQITDL LIKPVQRIMK
YQLLLKDFLK HSKKAGLESP DLEKAVEVMC IVPKRCNDMM NVGRLQGFDG KIVAQGRLLL
QDTFMVSDPD GGLLGRMKER RVFLFEQLVI FSEPLDKKKG FSLPGFLYKN SIKISCLGLE
ENVEGDPCKF ILTSRSASGA VESFVLHSSH PGVREVWTLQ ISQILESQRN FLNGRLLHTH
THTHTQRGLI APGGGGGSSQ SSSIPSGPQG GSRRPSRIPQ PSRLPQPLRH HPGADPDGSN
KMSGLSPRPV PPPLLPVGGS PQGKRPIHTT EDQAYTPIPR ATVGPLPSTP TSKPRPGAVS
PMASPMATPA FGKDTLPPPP PSPGQNQKSG SGFWSSMPGS PASRPGSFTF PGEAGETPVR
QSSNQSQTHR HSTHSKEADR MSTCSSASEQ SIQSTQSNGS ESSSSSSVST MLVTQDYTAV
KEDEISVIQG EVVQILASNQ QNMFLVFRAA TEQGPAAEGW IPGFVLGHTS TIVPDCPEGS
IKKSSSWHTS LRIRKKSEKK EKEAKKETKL ENGYRKSRDG LANKVSVKLL NPNYIYDVPP
EFLVPLSDVT CDNGESVTLR CKVCGRPRAT VSWKGPNQSN LTNNGHFMHV CFSDTGEATL
RIIGVASEDD GVYTCVATNE LGSVTSSASL RVLGDWKDNF ESHYTEVVEL GRGRFSVVKR
CDHRGTKRTV AVKHVNKKLM RRDRVTQELN LLQRLQHPHI VTLIDTYETP SSYALVLEMA
DQGRLLDYIV SWGNLTEEKV ACYLRNVLEA LHYLHNCRIA HLDIKPENLL VSHTASGQPI
VKLTDFGDAV QLNSAHYVHP LLGSPEFASP ELVLGEPVSL TSDLWSLGVV TYVLLSGASP
FLDESAEETC LNICRLDFSF PRDYFQGVSQ AARDFVCLLL KTDPGRRPPA GLCLQEPWLQ
AGQGDGRAEG CLDTSRLISF IDRRKHQTDA RPIGGVRSFI HGRLHQSEP
//
