ID G3PKI0_GASAC Unreviewed; 1691 AA.
AC G3PKI0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 (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=69293 {ECO:0000313|Ensembl:ENSGACP00000018110.2, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000018110.2, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000018110.2}
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR STRING; 69293.ENSGACP00000018110; -.
DR Ensembl; ENSGACT00000018145.2; ENSGACP00000018110.2; ENSGACG00000013698.2.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR InParanoid; G3PKI0; -.
DR OMA; CGRSHHV; -.
DR TreeFam; TF313551; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000013698; Expressed in intestinal epithelial cell and 13 other cell types or tissues.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF34; SERINE_THREONINE-PROTEIN KINASE MRCK BETA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 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; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 74..339
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 340..410
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1010..1060
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1080..1199
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1225..1498
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1568..1581
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 889..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..657
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 716..797
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1612..1637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1691 AA; 190390 MW; E80AFCA14F61FC43 CRC64;
MSAQARLKRL EELLLEQKAA GCLSVEALLD LLLCFYTEVS HSPLKREKHV TDFLEWVKPF
TTTVKDMRLH RDDFEMLKVI GRGAFGEVAV VKMKHTERVY AMKILNKWEM LKRAETACFR
EERDVLVKGD SQWITTLHYA FQDDNYLYLV MDYYVGGDLL TLLSKFEDRL PEDMSKFYVA
EMVLAVHSIH QQRYIHRDIK PDNVLLDVNG HIRLADFGSC LRMMEDGTVQ SSVAVGTPDY
ISPEILQAME DGMGRYGPEC DWWSLGVCVY EMLYGETPFY AESLVETYGK IMNHENTFQF
PSHGTDVSRG RQDLTQRLPG PGELLGLNGI SDFKSHAFFS GIDWENIRSA EAPYIPDVSS
PTDTSNFDVD DDVLKNPEIS PPMSHSGFTG QHLPFVGFTY TTDSCFADRS SVRQTGLGQE
EAGAGGGGQE VEAFERRIRR LEQEKQELNR KLQGETCSTQ ALQAPPRGGT LTRDKEIKKL
NEEIERLKKK LADSDRLEHQ LEEAVTLRQD YESSASKLKS LERQVKTLRQ EKEEVHKQLA
DSLERLRSHG KELKEAHAQR KVALQEFSDL SERMVDLRSS KQRLSRQLRD KEEEMDTLLQ
KMDAMRQEIR KTEKNRKELE GQLDDAKAEA QKEKKLREHI EVHSKQLETE LQNLKAQQGR
GAVAGGADFQ QELSRMKADL DTKSLFYEEE LLRRDSSHSS EIKKLRKDLQ ESEGAQLTAN
KELLQLREKL DKAKRDRQAE MDEAVSVVKE KSEREKNLLT EENRKLTAET DKLCSFVDQL
TAQNRQLEDD LQDLSSKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAT KMTEELETLR
SSSLGPRTLV TTSVTHTHTG NMHTHTHTHT LIRAKQMVQE ELRKVKAANI NMESKLKESE
ERSREMGEQV ESLKKEMEDS RSRSDKGLKL PDFQDSIFEY FNTSPLAPDL TFRVSHLSTT
DIDSTPLKSE ATPPSPSTTS EQEEVKAASV PASPSPTYQS SALTTPKPKA HQLSIKTFSS
PTQCTHCTSL MVGLLRQGYA CEVCSFICHV SCKDHAPLVC PIPAEHTKRP QGIDVQRGIG
TAYKGYVRIP KPSGVKKGWQ RAFALVSDCK LFLYDVPEGK STQPGVGASL VLDLRDEEFS
VSSVLASDVI HATRKDIPCI FRVSSSQLIS QLSAVSLLVL AESEVEKRKW VRILEGLQGI
LTKNLLKNQQ VHILHEAYDA SLPLIKTALS AAVLDRERIA LGTEDGLFVV EVTRDVIVRA
ADSKKIHQID LIPKEKIVAL LCGRNRHVHL HHWGALEGAE SAFDLKLTDT KGCQALTTGV
LRPGGPSCLL AAVKRQVLCY EISRVKPYHK KLWEVQAPGG VQWLGMVRDR LCVGYPSGFA
LLALQGESSP ISLVNPADPS LAFLAQQSLD ALHALQVGPT ELLLCFSQLG VYVDGQGRRS
RTQELMWPAT PLACSSNSTH LTVYSENGLD VFDIHTTEWV QTISLRKIRP LNIEGTLNLL
SSEPPRLIYF SNTSSERDLT IPETSDQSRK LMVRTRSKRK FLFKVPEEER LQQRREMLRD
PELRSKMISN PTNFNHVAHM GPGDGMQVLM DLPLSVMPSS QDDPVKDKPR PLSSISRQQR
SKTHITRTAS DFGGGASSRS VSELDPDLDR EPDSDSTKHS TPSNSSNPSS PPSPNSPHRS
QLTLDGLEMD P
//
