SHKC_DICDI
ID SHKC_DICDI Reviewed; 506 AA.
AC Q54Y55;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Dual specificity protein kinase shkC;
DE EC=2.7.11.1;
DE AltName: Full=SH2 domain-containing protein 3;
DE AltName: Full=SH2 domain-containing protein C;
GN Name=shkC; ORFNames=DDB_G0278409;
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. TKL Ser/Thr
CC protein kinase family. SH2 domain-containing protein kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68377.1; -; Genomic_DNA.
DR RefSeq; XP_642347.1; XM_637255.1.
DR AlphaFoldDB; Q54Y55; -.
DR SMR; Q54Y55; -.
DR STRING; 44689.DDB0230123; -.
DR PaxDb; Q54Y55; -.
DR PRIDE; Q54Y55; -.
DR EnsemblProtists; EAL68377; EAL68377; DDB_G0278409.
DR GeneID; 8621552; -.
DR KEGG; ddi:DDB_G0278409; -.
DR dictyBase; DDB_G0278409; shkC.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_024030_0_0_1; -.
DR InParanoid; Q54Y55; -.
DR PhylomeDB; Q54Y55; -.
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:Q54Y55; -.
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; cd10356; SH2_ShkA_ShkC; 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; IPR035844; ShkA/ShkC_SH2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00109; TYRKINASE.
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..506
FT /note="Dual specificity protein kinase shkC"
FT /id="PRO_0000327810"
FT DOMAIN 24..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 396..488
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 506 AA; 57135 MW; 20692F4AA8C78CB9 CRC64;
MDSGLGSSYP EERSGPPEIR PEEINFEELI GTGSFGKVYK GRCRQKAVAV KLLHKQNFDA
ATLSAFRKEV HLMSKIYHPN ICLFMGACTI PGRCVIVTEL VPKGNLETLL HDQKIQLPLY
LRMRMARDAA LGINWLHESN PVFVHRDIKS SNLLVDENMR VKICDFGLSA LKQKHKMLKD
QSSAKGTPLY MAPEVMMFKE FNESSDVYSF GIVLWEILTR KEPFSHHREL EKFREAVCVK
HERPPIPNDC LDSLRRLIEK CWDKEPISRP SFKEIISALD HVIIDAAISD LNGRDFWKKS
FLTEQEVPWE AFIDALCNWS KAPARNQCDK TSIDYLNIKC LKAVLAESPK SEGTGVETVV
NIEKFGKILE FFGPVPEPAP GHSIMDTVRE ILSQKWFHGD LDTTEAASRL NGQPIGSFLI
RFSSTNAGCF TISQVVDGGS IKHQRVSRQG VKFNYQNVIY NSLIEIVSKN GGGANGDVKL
DSQLGVPNYK FMSLFCVLNK ESEVYQ
