ID F1A1N7_DICPU Unreviewed; 640 AA.
AC F1A1N7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=SH2 domain-containing protein {ECO:0000313|EMBL:EGC29890.1};
GN ORFNames=DICPUDRAFT_158466 {ECO:0000313|EMBL:EGC29890.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29890.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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. {ECO:0000256|ARBA:ARBA00025089}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; GL871380; EGC29890.1; -; Genomic_DNA.
DR RefSeq; XP_003293584.1; XM_003293536.1.
DR AlphaFoldDB; F1A1N7; -.
DR STRING; 5786.F1A1N7; -.
DR EnsemblProtists; EGC29890; EGC29890; DICPUDRAFT_158466.
DR GeneID; 10504904; -.
DR KEGG; dpp:DICPUDRAFT_158466; -.
DR eggNOG; KOG0192; Eukaryota.
DR InParanoid; F1A1N7; -.
DR OMA; LTKQEPY; -.
DR OrthoDB; 7122at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00173; SH2; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 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; PS50001; SH2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 163..419
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 521..595
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT COILED 4..31
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 640 AA; 72438 MW; CA46D5DA76293516 CRC64;
MDKISQYESL IAQLEKEVKE IEARQLLKEN EIRSLVDLAI SSKSPNAQIN RDQIDKLFRE
SISDLKLKAE KIQKLEEYKQ EIITSLLVEP KSPNDVSIIS VWEQLKVSSF RKVDNTNTDS
NYTYSSVILN ESENENSSPV QTKANNEEEE IIRWEIDRNE ISYNREAKLG SGAFGSVYKG
IVRGKEVAIK KLTQTVFEEN TMNEFRKEVS LMAKLRNPHL LLFMGACTTP DDLSIVTELM
PKGSVHSLLR AKEDSPDFIT FKRAILIARD TALGMTWLHA SNILHLDLKP ANLLVDQNWV
VKVADFGLSK YMKKGATQSG QAGSPLYMAP EMLLNQPYDE KVDVFSFVIL LWELLTKQEP
YNKLYSSYPQ LVEGVVNKKN RPIIPDYFPS RLKDLLNRCW DHHPARRPSF AEITKSKFLE
SILIDGLILD PSGRQFWAQY YLGKEEASWN SFIINFSLFC GYESHLHSDD IKLKFLKLLL
VPSDSDVVTI DMFGKILTWC GPLTNGKDFF EKVYSICSIK GFLGQTSSKN ANTYLAGKKP
GTYILRFSSD PGSYAISYLN KNKEIVHARV IYKPGSGYIH HGGQTHYSTL DDLIKNTFKS
LGIKEPFEGG PFHALSVAAS KGPNFNVVGS YIAVSNGKKI
//
