SHKE_DICDI
ID SHKE_DICDI Reviewed; 710 AA.
AC Q54G43;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Dual specificity protein kinase shkE;
DE EC=2.7.11.1;
DE AltName: Full=SH2 domain-containing protein 5;
DE AltName: Full=SH2 domain-containing protein E;
GN Name=shkE; ORFNames=DDB_G0290451;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15073273; DOI=10.1074/mcp.m300131-mcp200;
RA Gao Q., Hua J., Kimura R., Headd J.J., Fu X.-Y., Chin Y.E.;
RT "Identification of the linker-SH2 domain of STAT as the origin of the SH2
RT domain using two-dimensional structural alignment.";
RL Mol. Cell. Proteomics 3:704-714(2004).
CC -!- FUNCTION: Required for proper chemotaxis and phagocytosis; proper
CC spatiotemporal control of F-actin levels in chemotaxing cells. Negative
CC regulator of the PI3K (phosphatidylinositol 3 kinase) pathway.
CC Predominantly phosphorylates serines and threonines and tyrosines at a
CC lower level (By similarity). {ECO:0000250}.
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. SH2 domain-containing protein kinase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000163; EAL62241.1; -; Genomic_DNA.
DR RefSeq; XP_635729.1; XM_630637.1.
DR AlphaFoldDB; Q54G43; -.
DR SMR; Q54G43; -.
DR STRING; 44689.DDB0230104; -.
DR PaxDb; Q54G43; -.
DR EnsemblProtists; EAL62241; EAL62241; DDB_G0290451.
DR GeneID; 8627647; -.
DR KEGG; ddi:DDB_G0290451; -.
DR dictyBase; DDB_G0290451; shkE.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_024030_0_0_1; -.
DR InParanoid; Q54G43; -.
DR OMA; NWLHGIC; -.
DR PhylomeDB; Q54G43; -.
DR Reactome; R-DDI-3295583; TRP channels.
DR Reactome; R-DDI-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-DDI-5675482; Regulation of necroptotic cell death.
DR PRO; PR:Q54G43; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP 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; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR CDD; cd10357; SH2_ShkD_ShkE; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035845; ShkD/ShkE_SH2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..710
FT /note="Dual specificity protein kinase shkE"
FT /id="PRO_0000327812"
FT DOMAIN 237..495
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 597..707
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 83..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 243..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 710 AA; 81107 MW; B6DC27CAA6622651 CRC64;
MDINLIKQYI NSSLPNDKES LIQYYGQLKQ ILNALSDKEQ QQLLNNNGKI SEQQQLSIEN
NYKVIGSIEE KMKSIEHLFN NLDVSDSNNN NSTSPVFISL DNQNTVNNNN NNNNNNNNNN
NNNNNNNNNS LAPTVILDNN DNKKTAEIIL PDHHNNTPQQ QPEQQVQQQQ VQQQQQVQQQ
QQQPEQQQQH LTEEQIQKQQ QSQASIQQAI ANMGEKKRSS SRHSGPPEIP PEEIKFDVKT
DLLGGGAYGK VYKATCRGKK VAVKVPKKQT LSESELKSFK NEVEIMKQIF HPNVVLCLGA
CTKPGKVMIV SELMQTDLEK LIHSSEVEPP PLYERMKMCL DAALGINWLH GICNIIHRDL
KLANLMISKD KTVKIGDFGF SQVIKTGTTL SDQKGPKGTA LYMAPEVMMK HEFNEKADVY
SFGLILYEMA TCEELFPEYS EIDPFYDAIC NKKLRPPIPD SFPKSLKTLI QKCWDHDPNK
RPSFNEVTQR MNEVLTDTAI SGLDAAMFWK YNFIKPESES VPWNEFVYKL SSVVNLPTQV
LSPLAQLFVS QSYEEEIGGV VTMERFDLMN KWFGNFFNSK YGPAILYEMI ELLKKRWFHF
DISRDISEKR LRGRPENTFL LRLSANDPIK TPFTISKTKG SKPTHKRVSR EDVQINEIKQ
FPMGYKFTVP LDGNELVFGS ITQMVEELHR IGNLSIPCPI TEIKVPYLTD
