PHG2_DICDI
ID PHG2_DICDI Reviewed; 1387 AA.
AC Q54QQ1; Q6H9K1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine/threonine-protein kinase phg2;
DE EC=2.7.11.1;
GN Name=phg2; ORFNames=DDB_G0283699;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DOMAIN.
RC STRAIN=AX3 / DH1;
RX PubMed=15194808; DOI=10.1091/mbc.e03-12-0908;
RA Gebbie L., Benghezal M., Cornillon S., Froquet R., Cherix N.,
RA Malbouyres M., Lefkir Y., Grangeasse C., Fache S., Dalous J., Bruckert F.,
RA Letourneur F., Cosson P.;
RT "Phg2, a kinase involved in adhesion and focal site modeling in
RT Dictyostelium.";
RL Mol. Biol. Cell 15:3915-3925(2004).
RN [2]
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 [3]
RP FUNCTION, AND DOMAIN.
RX PubMed=16325504; DOI=10.1016/j.ejcb.2005.09.014;
RA Blanc C., Charette S., Cherix N., Lefkir Y., Cosson P., Letourneur F.;
RT "A novel phosphatidylinositol 4,5-bisphosphate-binding domain targeting the
RT Phg2 kinase to the membrane in Dictyostelium cells.";
RL Eur. J. Cell Biol. 84:951-960(2005).
RN [4]
RP FUNCTION, AND INTERACTION WITH ADRM1.
RX PubMed=16987957; DOI=10.1091/mbc.e06-07-0619;
RA Cherix N., Froquet R., Charette S.J., Blanc C., Letourneur F., Cosson P.;
RT "A Phg2-Adrm1 pathway participates in the nutrient-controlled developmental
RT response in Dictyostelium.";
RL Mol. Biol. Cell 17:4982-4987(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH RAP1.
RX PubMed=16769729; DOI=10.1074/jbc.m600804200;
RA Kortholt A., Rehmann H., Kae H., Bosgraaf L., Keizer-Gunnink I., Weeks G.,
RA Wittinghofer A., Van Haastert P.J.;
RT "Characterization of the GbpD-activated Rap1 pathway regulating adhesion
RT and cell polarity in Dictyostelium discoideum.";
RL J. Biol. Chem. 281:23367-23376(2006).
RN [6]
RP FUNCTION, AND INTERACTION WITH RAP1.
RX PubMed=17371831; DOI=10.1083/jcb.200607072;
RA Jeon T.J., Lee D.-J., Merlot S., Weeks G., Firtel R.A.;
RT "Rap1 controls cell adhesion and cell motility through the regulation of
RT myosin II.";
RL J. Cell Biol. 176:1021-1033(2007).
CC -!- FUNCTION: Serine/threonine kinase regulating cell substrate adhesion,
CC phagocytosis, motility, chemotaxis, and actin cytoskeleton
CC organization. It is a downstream component of Rap1-regulated adhesion,
CC and it is a regulator of myosin II phosphorylation. It is also a
CC negative regulator of development initiation.
CC {ECO:0000269|PubMed:15194808, ECO:0000269|PubMed:16325504,
CC ECO:0000269|PubMed:16769729, ECO:0000269|PubMed:16987957,
CC ECO:0000269|PubMed:17371831}.
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 -!- SUBUNIT: Interacts with adrm1, rap1, rasG and rasS.
CC {ECO:0000269|PubMed:16769729, ECO:0000269|PubMed:16987957,
CC ECO:0000269|PubMed:17371831}.
CC -!- INTERACTION:
CC Q54QQ1; Q556N5: adrm1-2; NbExp=3; IntAct=EBI-1807983, EBI-1807967;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side.
CC -!- DOMAIN: The N-terminal domain (region 81-193 aa) interacts with
CC PI(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) and PI(4)P
CC (phosphatidylinositol 4-phosphate), and it is the responsible for the
CC recruitment of phg2 to the plasma membrane.
CC {ECO:0000269|PubMed:15194808, ECO:0000269|PubMed:16325504}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AJ585374; CAE51341.1; -; mRNA.
DR EMBL; AAFI02000056; EAL65616.1; -; Genomic_DNA.
DR RefSeq; XP_638972.1; XM_633880.1.
DR AlphaFoldDB; Q54QQ1; -.
DR SMR; Q54QQ1; -.
DR IntAct; Q54QQ1; 4.
DR STRING; 44689.DDB0229845; -.
DR PaxDb; Q54QQ1; -.
DR EnsemblProtists; EAL65616; EAL65616; DDB_G0283699.
DR GeneID; 8624218; -.
DR KEGG; ddi:DDB_G0283699; -.
DR dictyBase; DDB_G0283699; phg2.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_255217_0_0_1; -.
DR InParanoid; Q54QQ1; -.
DR OMA; RIYWAND; -.
DR PRO; PR:Q54QQ1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030666; C:endocytic vesicle membrane; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:dictyBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:dictyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0031670; P:cellular response to nutrient; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:dictyBase.
DR GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1387
FT /note="Serine/threonine-protein kinase phg2"
FT /id="PRO_0000327706"
FT DOMAIN 807..1072
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..193
FT /note="Binding to PI(4,5)P2"
FT REGION 175..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..775
FT /note="Interaction with adrm1"
FT REGION 729..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 930
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 813..821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 834
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 1325..1326
FT /note="NN -> YY (in Ref. 1; CAE51341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1387 AA; 154449 MW; 824784039911F7FA CRC64;
MDDQQPLQTY NQPPPPLPKH IQLQIQQRQL QLQQQEEQER LQQQQQQQQQ QQDQQQHKLE
EGSRRRSLSD VVGGVNISNK ETPKRAFRIY WANDNHMYWT LLLDSTNTVG DVSEGLKDKV
PSSGTQCYLY KRTKANFGRW KDRRLSNEDS VWDIVDRRRK NHKSDPIFVL KRKKSTFSIS
QKKSPQNESD TSPLSSSGEF LNPYTNPTGS NNIVPSNAGH SRNTSSNSNN SANTSSNNLL
AHHQFNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNSNNSSN SNSNNSSNTT
TTTTTTTTTT TTSTSTNSIN TSNNNNNNNS GSNINPSSFI SPMSSLVSLS LSSSPASSAP
HSPTLSSQPS SPHTITPITT SPPPPQRNNS SKSLKSTMEM EPPAEYISLL SNNPPPTNGS
GSRPPSGSFI PGSIVNGSRS SASDLIGFKP PVCQQQQQQQ QQQQQQQQQQ VQQQQQQPQQ
VQQLQQLQQL QQQYQQQQPQ QQIQPLSPQQ QSQQQQQSPV KQSESIPQSP NLQSITQSSS
SNKPLSGSTG MNRSSSPSPF AKKNIGGGGG GGSLADRKNR LSVQPKDIMR LMRFYFGDSL
DGTFFTIAVQ NDTSAKDVCA SVEQKLLLPS GSTFVSLVLP IQPNGSKIER VLGEDEIIIE
VKDTWEDPSQ TFFQVTHKQQ APNNKRLSRQ IQAEPHVIPS EWRRSTDAIS LRASSDDMWK
RKSIPIFLQV TGPPNTHSHS HSPQRQLPNM SGSPHSHHHH QNNNNNNNNN NNNNNNNDLD
DDDSDDESDF DVSTLRGWVH WIPSADLEYI KRIGSGTYSK VYKGKYRDKF VAIKTMRGSN
MTTEQIESFK KECDILSTIQ SPLLISFYGS CIEESQLSMV VEYCSKGTLH KVLNNPLLDF
DWDKWFKWMT EVVEGVRYLH SMNPPMVHRD LKTLNILISS DWTAKLCDFG LTRTMTMTNV
STLGMLRGTM AYTAPEIYDG LLFNTKSDVY SLGVIMWEAI QRCISGVYLR PFHEHPISMD
IQIIILTSKN KVRPKISENC PEQLKTLITR CWDENPDKRP NCDEILEILL TMKQAHDENK
DEWESIRTKL PKQTIKAVSS SSSNNNNNNN NNNNNNNNNN NNNNNNNNNN NGTNTNSTVN
NVVVPSSSNA TIVVAPSVSS NSSNINTSMD NKSMSSLSDS PVLPSVGIVS TSSLTGNSNI
NNNNNNIHDN NNPNNNNSNN SNNTSLDVPP VGVILTRDRR NSIIAVGEVP VIVKPPETPD
GTTMVTEVFD FEVPQDSPSL EPLSSNNIIS TANILNIGYV NNENNSIIIE GNKSTLNEIG
NNNNNNNNNN NNNNNNNNSS NNNSINNNSS NNDENNCINN CINIESNESC IKSNTPEQIT
LKCVDER
