SHKD_DICDI
ID SHKD_DICDI Reviewed; 744 AA.
AC Q54U31;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Dual specificity protein kinase shkD;
DE EC=2.7.11.1;
DE AltName: Full=SH2 domain-containing protein 4;
DE AltName: Full=SH2 domain-containing protein D;
GN Name=shkD; ORFNames=DDB_G0281343;
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; AAFI02000040; EAL66757.1; -; Genomic_DNA.
DR RefSeq; XP_640734.1; XM_635642.1.
DR AlphaFoldDB; Q54U31; -.
DR SMR; Q54U31; -.
DR STRING; 44689.DDB0230122; -.
DR PaxDb; Q54U31; -.
DR EnsemblProtists; EAL66757; EAL66757; DDB_G0281343.
DR GeneID; 8623010; -.
DR KEGG; ddi:DDB_G0281343; -.
DR dictyBase; DDB_G0281343; shkD.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_373607_0_0_1; -.
DR InParanoid; Q54U31; -.
DR OMA; TREMEMS; -.
DR PhylomeDB; Q54U31; -.
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:Q54U31; -.
DR Proteomes; UP000002195; Chromosome 3.
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 SMART; SM00252; SH2; 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..744
FT /note="Dual specificity protein kinase shkD"
FT /id="PRO_0000327811"
FT DOMAIN 277..534
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 641..734
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 283..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 744 AA; 83535 MW; D58B4ABB88741D89 CRC64;
MKRFFSNLFK RKQDQNSHIK QINGPTTSTP TTTPTTPTTP TTTQTPTPQN NNTNNNTNNN
NNTNSNNSNQ QKKEQAQASP STNQTQTPSN NTISTSPTVT TQPSFTPGVI STSKLTTSPP
ESPRPPTSTT NTTQPSTTTT TATNSTNTNT ASAPTKTASP SSPSATASPN NNSNNTTTTA
ATTTTTTTTT TTTNANQTAS VNHTSSDQSL NAQNVTQTNN NNNNNNNNNN NNNANNTKPI
NPNDYIPLDF VDSTPKVDNN QPKRKASGPP EILPEEIDRT DFLGQGSFGS VYKGKCRGQE
VAVKIPRKQK LSLYELTSFR HEVKIMSKIF HPNVVLFLGA CTQSGKMQIV TELCQTDLEK
LLHNDRTKKE FSLFRRMQMA KDAALGMNWL HGITRIVHND LKTANLLVDI NLRVKVTDFG
FSQIKEGEEF QDKAAKGTPL WMAPEVMMGN PYNEKADVYS FGIILWEILT KEAPYSHHKD
YDIFFNAICN EKERPPIPAD TLPSLRHLIQ TCWDHNPQNR PSFSEILFRL NEILIDCAID
FDDGRKYWKE HFLVPKQELQ EEVEWSDFEK TLKATHKQLN LDYAPLKELL VQQSHQTVQK
TKQVVTMERF DKVSKWFGSF FEPNTGIETI DNINKLSAKI WFHGDIVREQ ATSRLSKAAE
GAFLIRLSST EPKTCPFTLS MKNNQHRRIQ LIDENNFTGF KIQGKTAVYN SLIELVEKCN
DYPLLVPCPK FTQETFNPYD PYTN
