ID A0A7E6DB15_9CHIR Unreviewed; 3066 AA.
AC A0A7E6DB15;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 10-JUN-2026, entry version 24.
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|RefSeq:XP_035876146.1};
OS Phyllostomus discolor (pale spear-nosed bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Phyllostomidae;
OC Phyllostominae; Phyllostomus.
OX NCBI_TaxID=89673 {ECO:0000313|Proteomes:UP000504628, ECO:0000313|RefSeq:XP_035876146.1};
RN [1] {ECO:0000313|RefSeq:XP_035876146.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_035876146.1};
RG RefSeq;
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 RefSeq; XP_035876146.1; XM_036020253.1.
DR GeneID; 114499441; -.
DR CTD; 7204; -.
DR Proteomes; UP000504628; Chromosome 3.
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-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: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 CDD; cd14113; STKc_Trio_C; 1.
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; 2.30.29.30:FF:000091; 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; 3.30.200.20:FF:000169; 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; 2.30.29.30:FF:000040; 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; 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; 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:UP000504628};
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 65..210
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1292..1467
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1479..1591
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1656..1721
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1937..2113
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2125..2239
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2518..2583
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2652..2742
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2763..3017
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1738..1933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2255..2519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2606..2627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 757..784
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..25
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1805
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1855
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1886..1895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1922
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2261..2277
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2278..2305
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2363..2382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2422..2432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2441..2457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2497..2519
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2610..2627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3066 AA; 344381 MW; 1EE7813E7E6CDD0C CRC64;
MSGSSGGAAA PAASSSPAAT ASAAGSGCGG GAGEGAEEAA KDLADIAAFF RSGFRKNDEM
KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRIR QEDLRRLISY LACIPSEEVC
KRGFTVIVDM RGSKWDSIKP LLKILQESFP CCIHVALIIK PDNFWQKQRT NFGSSKFEFE
TNMVSLEGLT KVVDPSQLTP EFDGCLEYNH EEWIEIRVAF EDYISNATHM LSRLEELQDI
LAKKELPQDL DGARNMIEEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSD SFPKKNSGSG
NADLQSLLPK VSAMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE KMFDWITHNK
GLFLNSYTEI GTSHPHAMEL QTQHNHFAMN CMNVYVNINR IMSVANRLVE SGHYASQQIK
QIANQLEQEW KAFAAALDER STLLDMSSVF HQKAEKYMSN VDSWCKACGE VDLPSELQDL
EDAIHHHQGI YEHITLAYSE VSQDGKSLLD KLQRPLTPGS SDSLTASANY SKAVHHVLDV
IHEVLHHQRQ LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL
HRARALQKRH EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH QLEDRIQDFV
RRVEQRKILL DMSVSFHTHV KELWTWLEEL QKELLDDVYA ESVEAVQDLI KRFGQQQQTT
LQVTVNVIKE GEDLIQQLRD SAISSNKTPH NSSISHIETV LQQLDEAQAQ MEELFQERKI
KLELFLQLRI FERDAIDIIS DLESWNDELS QQMNDFDTED LTIAEQRLQH HADKALTMNN
LTFDVIHQGQ DLLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQQ ELDLAAEQHR
KHLEQCVQLR HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH EQFQHAIEKT
HQSALQVQQK AEAMLQANHY DMDMIRDCAE KVASHWQQLM LKMEDRLKLV NASVAFYKTS
EQVCSVLESL EQEYKREEDW CGGADKLGPN SETDHVTPMI SKHLEQKEAF LKACTLARRN
ADVFLKYLHR NSVNMPGMVT HVKAPEQQVK NILNELFQRE NRVLHYWTMR KRRLDQCQQY
VVFERSAKQA LEWIHDNGEF YLSTHTSTGS SIQHTQELLK EHEEFQITAK QTKERVKLLI
QLADGFCEKG HAHAAEIKKC VTAVDKRYRD FSLRMEKYRT SLEKALGISS DSNKSSKSLQ
LDIIPASIPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL IQTEKAYVRD LRECMDTYLW
EMTSGVEEIP PGIVNKELII FGNMQEIYEF HNNIFLKELE KYEQLPEDVG HCFVTWADKF
QMYVTYCKNK PDSTQLILEH AGSYFDEIQQ RHGLANSISS YLIKPVQRIT KYQLLLKELL
TCCEEGKGEI KDGLEVMLSV PKRANDAMHL SMLEGFDENI ESQGELILQE SFQVWDPKTL
IRKGRERHLF LFEMSLVFSK EVKDSSGRSK YLYKSKLFTS ELGVTEHVEG DPCKFALWVG
RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTIHLKGA LKEPIHIPKT APATRQKGRR
DGEDLDSQGD GSSQPDTISI ASRTSQNTLD SDKLSGGCEL TVVIHDFTAC NSTELTIRRG
QTVEVLERPH DKPDWCLVRT TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS
SNDASPPASV ASLQPHMMGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHVKKLAHKH
KKSREVRKSA DAGSQKDSDD SAATPQDETV EERGRNEGLS SGTLSKSSSS GMQSCGEEEG
EEGADAVPLP PPMAIQQHSL LQPDSQDDKA LEDRPSSLLV DQGDSSSPSF NPSDNSLLSS
SSPIDEMEER KSSSLKRRHY VLQELVETER DYVRDLGYVV EGYMALMKED GVPDDMKGKD
KIVFGNIHQI YDWHRDFFLG ELEKCLEDPE KLGSLFVKHE RRLHMYIVYC QNKPKSEHIV
SEYIDTFFED LKQRLGHRLQ LTDLLIKPVQ RIMKYQLLLK DFLKYSKKAS LDTSELERAV
EVMCIVPKRC NDMMNVGRLQ GFDGKIVAQG KLLLQDTFLV TDQDAGLLPR CRERRVFLFE
QIVIFSEPLD KKKGFSMPGF LFKNSIKVSC LCLEENVEND PCKFALTSRT GDVVETFVLH
SSSPSVRQTW IHEINQILEN QRNFLNALTS PIEYQRNHSG GSAGGGSAGA TPGGGSSGSN
HSSGPSSCSG LPSSSRSRPS RIPQPVRHHS PVLVSSAASS QAEADKMSGM STPGPSLPPP
SSSLTLEAGP SQHGRHPPGS HSEGPEKEAE QIPKMKMIDS PRKSTGNAAG ASQDGNAKED
GRSRSGLGSL PLGKPRPGAI SPLNSPLSTT FPSPLGKEPF SPSSPLQKGG SFWSSIPASP
ASRPGSFTFP GDSDSLQRQA HRHAAPSKDT DRMSTCSSAS EQSVQSAQSN GSESSSSSNI
STMLVTHDYT AVKEDEINVY QGEVVQILAS NQQNMFLVFR AATDQCPAAE GWIPGFVLGH
TSTVIMENPD GTLKKSTSWH TALRLRKKSE KKDKDGKREG KLENGYRKSR EGLSNKVSVK
LLNPNYIYDV PPEFVIPLSE VTCETGETVV LRCRVCGRPK ASITWKGPEH NTLNNDGHYS
ISYSDLGEAA LKIVGVTTED DGIYTCIAVN DMGSASCSAS LRVLGPGSDG IMVTWKDNFD
SFYSEVAELG RGRFSVVKKC DQKGTKRAVA TKFVNKKLMK RDQVTHELGV LQNVQHPLLV
GLLDTFETPT SYVLVLEMAD QGRLLDCVVR WGNLTEGKIR AYLGEVLEAV RYLHNCRIAH
LDLKPENILV DQSSAKPTIK LADFGDAVQL NTTYYIHQLL GSPEFAAPEI ILGNPVSLTS
DTWSVGVLTY VLLSGVSPFL DDSVEETCLN ICRLDFSFPD DYFKGVSQKA KDFVCFLLQE
DPAKRPSAAL ALQEQWLQAG QGDGKGAGVL DTSRLTSFIE RRKHQNDVRP IRSIKNFLQS
RLLPRV
//
