ID G3NT97_GASAC Unreviewed; 3132 AA.
AC G3NT97;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 27-NOV-2024, sequence version 2.
DT 10-JUN-2026, entry version 94.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Gasterosteus aculeatus aculeatus (three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=481459 {ECO:0000313|Ensembl:ENSGACP00000008565.2, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000008565.2, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Benthic {ECO:0000313|Ensembl:ENSGACP00000008565.2,
RC ECO:0000313|Proteomes:UP000007635};
RX PubMed=33598708;
RA Nath S., Shaw D.E., White M.A.;
RT "Improved contiguity of the threespine stickleback genome using long-read
RT sequencing.";
RL G3 (Bethesda) 11:0-0(2021).
RN [2] {ECO:0000313|Ensembl:ENSGACP00000008565.2}
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}.
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DR RefSeq; XP_040022377.1; XM_040166443.1.
DR STRING; 69293.ENSGACP00000008565; -.
DR Ensembl; ENSGACT00000008584.2; ENSGACP00000008565.2; ENSGACG00000006462.2.
DR CTD; 368847; -.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG4240; Eukaryota.
DR GeneTree; ENSGT00940000154766; -.
DR InParanoid; G3NT97; -.
DR OMA; CMTTIAQ; -.
DR Proteomes; UP000007635; Chromosome XX.
DR Bgee; ENSGACG00000006462; Expressed in telencephalon and 2 other cell types or tissues.
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; 5.
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; 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; 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; 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; 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:UP000007635};
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 49..180
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1283..1458
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1470..1582
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1646..1714
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1959..2135
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2565..2630
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2700..2792
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2811..3066
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 259..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1914..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2278..2421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2462..2566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 748..775
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1619..1639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1793
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1827..1845
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1882..1891
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1926..1944
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2295..2311
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2312..2326
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2327..2351
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2371..2384
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2408..2418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2509..2521
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2541..2552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2553..2566
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2840
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3132 AA; 352480 MW; 1DC05AB31AAC32E2 CRC64;
MAVLDNHRWQ FAQAGKTLIR LSGFHRNEDM KAIDVLPILK EKVAFLSGGR DRRGGPVLTF
PARSNHDRIR PEDLRRLIAY LATVPSEEVA RHGFTVIVDM RGSKWDSIKP LLKILQESFP
SCIHVALIIK PDNFWQKQRT NFGSSKFEFE TVMVSLDGLS KIVDASQLTA DFEGSLDYNH
DEWIEVRLSF ETFASDSMRA LARLEELQET LSQRDLPRDL EGARRLMEEH ASLKKRATKA
SVEELDAQGR RLLQRLQFQT AGGGSSSESP YGSRGSGASG DSNDHHHGFH AHADAHNLVA
KVTGLLDKLH GTRQNLQQLW HMRKLKLDQC FQLRLFEQDA EKMFDWILHN KGLFLTSYTE
IGGNHQHAVE LQTQHNHFAM NCMNVYVNIN RIMSVGNRLL ESGHYASQQI QQISAQLEQE
WKAFAAALDE RSTLLEMSAS FHQKADQYMS KVEPWCKACG EGELPSELQD LEDTIHHHQG
LYEHITTAYS EVSQDGKSLL DKLQRPLTPG SADSLMASAN YSKAVHHVLD IIHEVLHHQR
QLENIWQHRK VRLHQRLQLC VFQQDVQQVL DWIENHGEAF LSKHTGVGKS LHRARALQKR
HEDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYQAA HQLEDRIQDF VRRVEQRKVL
LDMSVAFHTH VKELWTWLEE LQKELLDDVY AESVEAVQDL IKRFGQQQQT TLQATVNVIK
EGEDLIQQLR DSAISSNKTP HNSSMAHIES VLQQLDEAQG QMEELFQERK IKLELFLQLR
IFERDAIDII SDPESWNEEL SQQMSDFDTE DLTLAEQRLQ HHADKALTMN NLTFDVIHQG
QELLQYVTEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ QELDLAAEQH RRHLEQCVQL
RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQKE HEQFQHAIEK THQSALQVQQ
KAEALLQANH YDMDMIRDCA EKVADHWQQL MLKMEDRLKL VNASVAFYKT SEQVCSVLES
LEQEYKREED WCGGADKLGP NSDSDHVTPM ISKHLEQKEA FLKACTLARR NADVFLKYLH
RNSVNMPGML SHVKAPETQV KNILNELLQR ENRVLHFWTM RKRRLDQCQQ YVVFERSAKQ
ALEWIHDTGE FYLSTHTSTG SSIHHTQELL KEHEDFQITA KQTKERVKLL IQLADGFCDK
GHAHALEIKK WVSSVDKRYR DFSLRMDKYR TCLETALGIC SDSNKASKEL QLDIIPASAP
GSEVRLRDAA LELNEEKRKS ARRKEFIMAE LIQTEKTYVR DLRECMDTYL WEMTSGVEEI
PPGIVNKEHI IFGNMQDLYE FHHNIFLKEL EKYEQLPEDV GHCFVTWADK FQMYVNYCKN
KPDSTQLILE HAGPYFDEIQ QRHRLANSIS SYLIKPVQRI TKYQLLLKEL LTCCEEGKGE
IKDGLEVMLS VPKRANDAMH LSMLDGFDGN IDSQGELILQ DSFQVWDPKT LIRKGRERHL
FLFEMSLVFS KEVKDSNGHS KYLYKSKLFT SELGVTEHVE GDHCKFALWV GRTPTSDNKI
VLKASSIDNK QDWIKHIREV IQERTVHLRG ALKEPIHIPK ASAARHKGRR DGEELDSQGD
ASSQPDTISI ASRTSQNTLD SDKLSGGCEL TVVIHDFMAG NGGSSGELTV RRGQTVEVLE
RLHDKPDWCL VRTTDRSPAQ EGIVPCSMLC IAHSRSSMEM EGLFNHKDTL SVSSNDTLQP
GSSQTLGPHS SPGPKRPGNT LRKWLTSPVR RLSSGKADGH VKKLAHKHKK NRDGRKNMDP
MAGSQKDSDD SAATPQDETL EERMRNEGLS SGTLSKSSSS GMQSCGEEEG EEGADAVPLP
PPMAIQQHSL LQPDSQDDKS SSRLSARPNS SETPSAAELV SAIEELVKSK MSLEDRPSSL
SVEQGDSSSP SFNPSDNSLL SSSSPIDDVE ERKSGFFKRR HYVLLELVET ERDYVRDLGS
VVEGYMSRMK EEGVPDDMRG KDKIVFGNIH QIYDWHKDLF LGELEKCLED PDRLAPLFVK
QERRLHMYIV YCQNKPKSEH IVSEYIDTYF EDLKQRLGHR LQITDLLIKP VQRIMKYQLL
LKDLHKISKK AGVDTTELEK AVEVMCVVPK RCNDMMNVGR LQGFDGKIVA QGRLLLQDTF
MVSDQDGGLL SRMKERRVFL FEQIVIFSEP IDKKKGFTSP GYLFKNNIKV SWLGLEENAD
DPCKFTLTSR SSSGNLERYT LHSMSPGVSR VWVHQVSQIL ENQRNFLNAL TSPIEYQRNH
VGGGGPGAPP GSSCSNTGGV PGGSSSNNTS SMGGGGGGGG SGGSGGSSSS LFGPRSRPSR
IPQPSSRLPQ PVHHHHPPGP EGPDRSAGMW SPSHHQPLPS SSYSDTTTNR EVPASEVPKM
RMMDCPHGSN SNNSSEPSDI TEASVKLNLG SYEETQKHQT AGVPQMAVAP LNFPLKSPRV
GTVTPLISPQ SPGGGRKEAH PPSSPLWAKV AALPASPSSR PGSFSYPSEG GGGGDSLGRG
SHGTLSHHQN SSHSKEIDRM STCSSTSEQS IHSTQSNGSE SSSSSSVSTM LVTQDYVAVK
EDEISVVQGE VVQMLASNQQ NMFLVYRASN EHCPAAEGWI PGYVLGHTSS SITPELLEGT
IKKSLSWHTA LRIRKKSEKR DKEGRKMENG FRKSQDGLAT KVSVKLLNPN FSQQIHDALP
EFIIPVSDVS CEGGDSVTLR CKVCGRPRAN ITWRGPDNNS LSNNGRYSIT YSETGEAALR
ILGVSVEDSG VYTCVATNVA ASVTSSASLR VSGTPDDGSE VLWKSSFELH YTEITELGRG
RFSVTKRCDQ RRSKRTVAAK QISKKLLHRE QVLQEVRLLQ ALDHPNLIKL LDTYETANSY
ILVEEMADQG RFLDYIVSWG NLTEDKLALY LRDILEGLCY LHSWRIAHLD LKPENIVVEH
ASSQPVIKLA DFGDASQLNP PSFYIHPLVG SPEFSAPELI LGQPASLMSD LWSLGVVTYV
ILSGASPFLD ESLEETCLNI CRLDFSFPED YFQGVSTAAR DFVCLLLQGE PERRPSAASC
LREPWLLPRG VIHSDTGHGP LNHMQPPSQN HHTSHLDTSR LISFIERRKH QNDVRPIGSI
KAFLHSRLLN HI
//
