ID H2U4J3_TAKRU Unreviewed; 3073 AA.
AC H2U4J3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000031855.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000031855.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000031855.3}
RP IDENTIFICATION.
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: 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 Ensembl; ENSTRUT00000031978.3; ENSTRUP00000031855.3; ENSTRUG00000012584.3.
DR GeneTree; ENSGT00940000154766; -.
DR HOGENOM; CLU_000373_3_0_1; -.
DR Proteomes; UP000005226; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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 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; 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; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF206; TRIPLE FUNCTIONAL DOMAIN PROTEIN-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 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; 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; 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; 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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 53..199
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1295..1470
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1482..1594
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1659..1724
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1975..2151
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2163..2277
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2522..2587
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2657..2747
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2768..3022
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 277..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1929..1971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2294..2523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2598..2627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 757..787
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1604..1632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1827..1841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1842..1861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1936..1961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2294..2314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2332..2346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2414..2437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2438..2453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2468..2485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2495..2523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2608..2627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2797
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3073 AA; 346167 MW; 854485364BEF7BF2 CRC64;
MSSGEGAEET TTKDAGDVAA FFKTDGALPK EAKGDGSSQI AGFRRNEEMR AMEVLPILKE
KVAFLSGGRD RRGGPVLTFP SRSNHDRIRS DDLRRLIAYL AGIPSEEVCK HGFTVIVDMR
GSKWDSIKPL LKILQESFPS CIHVALIIKP DNFWQKQRTN FGSSKFEFET TMVSLEGLTK
VVDPSQLTAD FDGSLDYNHE EWIEVRVAFE EFSGHATQML TRLEEMQETV SRKDFPQDLD
GARRMIEEHA TLKKKVIKAP IEELDTEGQR LLQRIQSNES FSNRNGGGSS GGSGSSSSSG
GMCNADTQGL VPRITQLLDK LHSTRQHLHQ AWHVRKLQLD QCFQLRLFEQ DAEKMFDWIM
HNKGLFLAGY TEIGNNHPHA MELQTQHNHF AMNCMNVYVN INRIMSVGNR LLESGHYASQ
QIKQISGQLE KEWKAFAAAL DERSTLLEMS ASFHQKCDQY MSNVDSWCKA CGEVDLPSEL
QDLEDGIHHH QGLYEHITAT YSEVSQDGKA LLDKLQRPLT PGSAESLTAS ANYSKAVHHV
LDIIHEVLHH QRQLENIWQH RKVRLHQRLQ LCVFQQDVQQ VLDWIENHGE AFLSKHTGVG
KSLHRARALQ KRHEDFEEVA QNTYTNADKL LEAAEQLAQT GECDPEEIYQ AAHQLEDRIQ
DFVRRVEQRK VLLDMSVAFH THVKELWTWL EELQKELLDD VYAESVEAVQ DLIKRFGQQQ
QTTLQVTVNV IKEGEDLIQQ LRDSAISSNK TPHNSSINHI ESVLQQLDEA QAQMEELFQE
RKIKLELFLQ LRIFERDAID IISDLESWNE ELTGQMNEFD TEDLTLAEQR LQHHADKALT
MNNLTFDVIH QGQELLQYVN EVQASGVELL CDRDVDMATR VQDLLEFLHE KQQELDLAAE
QHRRHLEQCV QLRHLQAEVK QVLGWIRNGE SMLNAGLITA SSLQEAEQLQ REHEQFQHAI
EKTHQSALQV QQKAEALLQA NHYDMDLIRE CAENVASHWQ QLMLKMEDRL KLVNASVAFY
KTSEQVCSVL ESLEQEYKRE EDWCGGADKL GPNCETDHVS PMISKHLEQK EAFLKACTLA
RRNADVFLKY MHRNSVNMPG MLSHVKAPEQ QVKNILNELL QRENRVLHFW TLRKRRLDQC
QQYVVFERSA KQALEWIHDT GEFYLSTHTS TGSSIHHTQE LLKEHEDFHI TAKQTKERVK
LLIQLADGFC EKGHSHAGEI KKWVTAVDKR YRDFSLRMDK YRCSLEKALG ISSDSNKASK
DLQLDIIPAT VPGSEVKLRD AAHELNEEKR KSARRKEFIM AELIQTEKAY VRDLRECMDT
YLWEMTSGVE EIPPGVINKE HIIFGNMQDL YEFHHNIFLK ELEKYEQLPE DVGHCFVTWA
DKFQMYVNYC KNKPDSTQLI LEHAGNYFDE IQQRHRLANS ISSYLIKPVQ RITKYQLLLK
ELLTCCEEGK GEIKDGLEVM LSVPKRANDA MHLSMLEGFD ENIESQGELI LQESFQVWDP
KTLIRKGRER HLFLFEMSLI FSKEVKDSNG RSKYIYKSKL FTSELGVTEH VEGDPCKFAL
WVGRTPTSDN KIVLKASSIE NKQDWIKHIR EVIQERTIHL RGALKEPIHI PKPTTSKHHK
GRGDREDLDS QGEGSSQPDT ISLASRTSQN TLDSDKLSGG CELTVVIHDF MASNSNELTV
RRGQTVEVLE RCHERPDWCL VRTTDRSPAL EGLVPCAMLC IAHSRSSMEM EGIFNHKDTL
SVCSNDSIMP GSSATLQPGH GLSSHTSPGP KRPGNTLRKW LTSPVRRLSS GKADGHVKKL
APKHKKNREV RKSGEMTMVS QKDSDDSAAT PQDETVEERV RNEGLSSGTL SKSSSSGMQS
CGEEEGEEGA DSVPLPPPMA IQQHSLLQPE SQDDKTSSRL SVRPSSSETP SAAELVSAIE
ELVKSKMALE DRPSSLSVEQ GDSSSTSFNP SDNSLLSSSS PTEEMDERRS SMLKKRHYVL
LELVETERDY VRDLSLVVEG YMSRMREQGI PDDMKGKDKT VFGNINQIYD WHRDIFLGEL
EKCLEDSDQL GPLFLKHERK LNMYVVYCQN KPKSEHIVSE YIDTYFEDMR QQLRHKLQIS
DLLIKPVQRI MKYQLLLKDF LKHSKKAGLE SVELEKAVEV MCIVPKRCND MMNVGRLQGF
DGKIVAQGRL LLQDTFMVSD PEGGHLGRMK ERRVFLFEQL VIFSEPLEKK KGFSLPGFLY
KNSIKISCLG LEENVEGDPC KFILTSRAAN ASESFVLHSS HPGVREVWTL QISQILESQR
NFLNALTSPL EYQRNHVDGS SGSRVPSTAA SAGGSSGPGV PPGVGVGNPQ GGAVPSGSQG
GSRRPSRIPQ PSRLPQPLRH HPGADPEGPS KMSGAKRPIQ SPEDQAHTHT PRAMIGPLPA
TPGTKSRQGA VPPVVPPLAT PVLSKDSLPP PPPSPGQKSG SGFWSSIPGS PASRPGSFTF
PGEAGEVPVR QNSNQIQTGS GSQTHRHSTH SKEADRMSTC SSASEQSIQS TQSNGSESSS
SSSVSTMLVT QDYMAVKEDE ISVIQGEVVQ ILASNQQNMF LVFRAATDQG PAAEGWIPGF
VLGHTSAVVP DCPEGPLNRK SSSWHTSLRI RRKSEKKEKE AKKETKLENG YRKSRDGLAN
KVSVKLLNPN YIYDVPPEFL VPLADVTCDS GESVTLRCKV CGRPRATVAW KGPDQTNLAT
NGRFSIAYSD TGEATLRIIG VASEDDGVYT CVATNELGST TSSASLRVLA VSTDGIRVSW
KDNFEYHYTE VVELGRGRFS VVKCYDQRGT KRTLAVKHVN KKLMRRDRVT QELNLHMRVQ
HPNIICLVDT YETPSSYALV LEMADQGRLL DYVVSWGNLT EEKAAYYLRD VLEALHYLHS
RRIAHLDVKP ENLLVAQRSG GQMVKLSDFG DAVQLNSSDY THPLLGSPEF ASPELVLGEP
VSLTSDMWSL GVVTYVLLSG ASPFLDESAE ETCLNICRLD FSFPRDYFQG VSQAARDFIC
LLLRTNPSQR PSAALCLQEP WLQARPADEQ TGTEGCLDTS RLISFIDRRK HQTDARAISG
IRSIIQGRLQ LQA
//
