ID F7CDS5_HORSE Unreviewed; 3056 AA.
AC F7CDS5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 3.
DT 27-MAR-2024, entry version 81.
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:ENSECAP00000017858.3,
GN ECO:0000313|VGNC:VGNC:24528};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000017858.3, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000017858.3, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000017858.3,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000017858.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000017858.3};
RG Ensembl;
RL Submitted (NOV-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: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC 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; 9796.ENSECAP00000017858; -.
DR PaxDb; 9796-ENSECAP00000017858; -.
DR Ensembl; ENSECAT00000021668.3; ENSECAP00000017858.3; ENSECAG00000019952.3.
DR VGNC; VGNC:24528; TRIO.
DR GeneTree; ENSGT00940000154766; -.
DR HOGENOM; CLU_000373_1_0_1; -.
DR InParanoid; F7CDS5; -.
DR OMA; IRYLHNC; -.
DR OrthoDB; 2906033at2759; -.
DR Proteomes; UP000002281; Chromosome 21.
DR Bgee; ENSECAG00000019952; Expressed in cerebellum and 23 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:UP000002281};
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 14..159
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1241..1416
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1428..1540
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1605..1670
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1918..2094
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2106..2220
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2508..2573
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2642..2732
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2753..3007
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1554..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1687..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2236..2509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2597..2617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 706..733
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1577..1599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1827..1856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2236..2285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2344..2361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2437..2465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2480..2509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3056 AA; 344243 MW; EC447C68390AE92E CRC64;
MRFRKNDEMK AMDVLPILKE KVAYLSGGRD KRGGPILTFP ARSNHDRIRQ EDLRRLISYL
ACIPSEEVCK RGFTVIVDMR GSKWDSIKPL LKILQESFPC CIHVALIIKP DNFWQKQRTN
FGSSKFEFET NMVSLEGLTK VVDPSQLTPE FDGCLEYNHE EWIEIRVAFE DYISNATHML
SRLEELQDIL AKKELPQDLE GARNMIEEHS QLKKKVIKAP IEDLDLEGQK LLQRIQSSDS
FPKKNSGSGN ADLQSLLPKV SAMLDRLHST RQHLHQMWHV RKLKLDQCFQ LRLFEQDAEK
MFDWITHNKG LFLNSYTEIG TSHPHAMELQ TQHNHFAMNC MNVYVNINRI MSVANRLVES
GHYASQQIKQ IANQLEQEWK AFAAALDERS TLLDMSSIFH QKAEKYMSNV DSWCKACGEV
DLPSELPDLE DAIHHHQGIY EHITLAYSEV SQDGKSLLDK LQRPLTPGSS DSLTASANYS
KAVHHVLDVI HEVLHHQRQL ENIWQHRKVR LHQRLQLCVF QQDVQQVLDW IENHGEAFLS
KHTGVGKSLH RARALQKRHE DFEEVAQNTY TNADKLLEAA EQLAQTGECD PEEIYQAAHQ
LEDRIQDFVR RVEQRKILLD MSVSFHTHVK ELWTWLEELQ KELLDDVYAE SVEAVQDLIK
RFGQQQQTTL QVTVNVIKEG EDLIQQLRDS AISSNKTPHN SSISHIETVL QQLDEAQAQM
EELFQERKIK LELFLQLRIF ERDAIDIISD LESWNDELSQ QMNDFDTEDL TIAEQRLQHH
ADKALTMNNL TFDVIHQGQD LLQYVNEVQA SGVELLCDRD VDMATRVQDL LEFLHEKQQE
LDLAAEQHRK HLEQCVQLRH LQAEVKQVLG WIRNGESMLN AGLITASSLQ EAEQLQREHE
QFQHAIEKTH QSALQVQQKA EAMLQANHYD MDMIRDCAEK VASHWQQLML KMEDRLKLVN
ASVAFYKTSE QVCSVLESLE QEYKREEDWC GGADKLGPNS ETDHVTPMIS KHLEQKEAFL
KACTLARRNA DVFLKYLHRN SVNMPGMVTH IKAPEQQVKN ILNELFQREN RVLHYWTMRK
RRLDQCQQYV VFERSAKQAL EWIHDNGDFY LSTHTSTGSS IQHTQELLKE HEEFQITAKQ
TKERVKLLIQ LADGFCEKGH AHAAEIKKCV TAVDKRYRDF SLRMEKYRTS LEKALGISSD
SNKSSKSLQL DIIPASIPGS EVKLRDAAHE LNEEKRKSAR RKEFIMAELI QTEKAYVRDL
RECMDTYLWE MTSGVEEIPP GIVNKELIIF GNMQEIYEFH NNIFLKELEK YEQLPEDVGH
CFVTWADKFQ MYVTYCKNKP DSTQLILEHA GSYFDEIQQR HGLANSISSY LIKPVQRITK
YQLLLKELLT CCEEGKGEIK DGLEVMLSVP KRANDAMHLS MLEGFDENIE SQGELILQES
FQVWDPKTLI RKGRERHLFL FEMSLVFSKE VKDSSGRSKY LYKSKLFTSE LGVTEHVEGD
PCKFALWVGR TPTSDNKIVL KASSIENKQD WIKHIREVIQ DRTIHLKGAL KEPIHIPKTA
PATRQKGKRD GEDLDSQGDG SSQPDTISIA SRTSQNTLDS DKLSGGCELT VVIHDFTACN
STELTIRRGQ TVEVLERPHD KPDWCLVRTT DRSPAAEGLV PCGSLCIAHS RSSMEMEGIF
NHKDSLSVSS NDASPPASVA SLQPHMMGAQ SSPGPKRPGN TLRKWLTSPV RRLSSGKADG
HVKKLAHKHK KSREVRKSAD AGSQKDSDDS AATPQDETVE ERGRNEGLSS GTLSKSSSSG
MQSCGEEEGE EGADAVPLPP PMAIQQHSLL QPDSQEDKAS SRLIVRPTSS ETPSAAELVS
AIEELVKSKM ALEDRPSSLL VDQGDSSSPS FNPSDNSLLS SSSPIDEMEE RKSSSLKRRH
YVLQELVETE RDYVRDLGCV VEGYMALMKE DGVPDDMKGK DKIVFGNIHQ IYDWHRDFFL
GELEKCLEDP EKLGSLFVKH ERRLHMYIVY CQNKPKSEHI VSEYIDTFFE DLKQRLGHRL
QLTDLLIKPV QRIMKYQLLL KDFLKYSRKA SLDTSELERA VEVMCIVPKR CNDMMNVGRL
QGFDGKIVAQ GKLLLQDTFL VTDQDTGLLP RCKERRVFLF EQIVIFSEPL DKKKGFSLPG
FLFKNSIKVS CLCLEENVEN DPCKFALTSR TGDVVETFIL HSSSPSVRQT WIHEINQILE
NQRNFLNALT SPIEYQRNHS GGGGSGGSGG GSASGGAPSS GPSNHSGGPS SCSGLPSSSR
SRPSRIPQPV RHHSPVLVSS AACSQAEADR MSGMSTLGPS LPPPSSGPAL EAGPGQCGRH
PPSGESEGPE REAEQIPKMK VIESPRKSAG NAAGASPEGN AKEARANPED SRSRSGLGSL
PLGKPRPGAI SPLNSPLSTA FPSPFGKEPF PPSSPLQKGG SFWSSIPASP ASRPGSFTFP
GDSDSLQRQA HRHAAPSKDT DRMSTCSSAS EQSVQSTQSN GSESSSSSNI STMLVTHDYT
AVKEDEINVY QGEVVQILAS NQQNMFLVFR AATDQCPAAE GWIPGFVLGH TSAVIMENPD
GTLKKSTSWH TALRLRKKSE KKEKDGKREG KLENGYRKSR EGLSNKVSVK LLNPNYIYDV
PPEFVIPLSE VTCETGETVV LRCRVCGRPK ASITWKGPEH NTLNNDGHYS ISYSDLGEAA
LKIVGATTED DGLYTCIAVN DMGSASCAAS LRVLGPGSDG IMVTWKDNFD SFYSEVAELG
RGRFSVVKRC DQKGTKRTVA TKFVNKKLMK RDQVTRELGI LQNLQHPLLV GLLDTFETPT
SYVLVLEMAD QGRLLDCVVR WGNLTEGKIR AYLGEVLEAV RYLHNCRIAH LDLKPENILV
DQSVAKPTIK LADFGDAVQL NTTYYIHPLL GNPEFAAPEI ILGNPVSLTS DSWSVGVLTY
VLLSGVSPFL DDSVEETCLN ICRLDFSFPD DYFKGVSQKA KDFVCFLLQE DPAKRPSAAL
ALQEQWLQAG HGHGKGAGVL DTSRLTSFIE RRKHQNDVRP IRSIKNFLQS RLLPRV
//
