GDT2_DICDI
ID GDT2_DICDI Reviewed; 1637 AA.
AC Q55CZ1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable serine/threonine-protein kinase gdt2;
DE EC=2.7.11.1;
DE AltName: Full=Growth-differentiation transition protein 2;
DE Flags: Precursor;
GN Name=gdt2; ORFNames=DDB_G0270666;
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, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15236669; DOI=10.1186/1471-213x-4-8;
RA Chibalina M.V., Anjard C., Insall R.H.;
RT "Gdt2 regulates the transition of Dictyostelium cells from growth to
RT differentiation.";
RL BMC Dev. Biol. 4:8-8(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).
CC -!- FUNCTION: Regulates the transition between growth and differentiation.
CC {ECO:0000269|PubMed:15236669}.
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:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the same level in vegetative cells
CC and throughout development, with a slight peak at the time when the
CC cells are aggregating. {ECO:0000269|PubMed:15236669}.
CC -!- DISRUPTION PHENOTYPE: Cells initiate multicellular development
CC prematurely. {ECO:0000269|PubMed:15236669}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GDT family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. TKL Ser/Thr protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72683.1; -; Genomic_DNA.
DR RefSeq; XP_646340.1; XM_641248.1.
DR AlphaFoldDB; Q55CZ1; -.
DR SMR; Q55CZ1; -.
DR STRING; 44689.DDB0220631; -.
DR PaxDb; Q55CZ1; -.
DR EnsemblProtists; EAL72683; EAL72683; DDB_G0270666.
DR GeneID; 8617295; -.
DR KEGG; ddi:DDB_G0270666; -.
DR dictyBase; DDB_G0270666; gdt2.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_251247_0_0_1; -.
DR InParanoid; Q55CZ1; -.
DR PhylomeDB; Q55CZ1; -.
DR PRO; PR:Q55CZ1; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0051093; P:negative regulation of developmental process; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0050793; P:regulation of developmental process; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR026237; STKINASEGDT.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR02079; STKINASEGDT.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Developmental protein; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1637
FT /note="Probable serine/threonine-protein kinase gdt2"
FT /id="PRO_0000323580"
FT TOPO_DOM 20..896
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 897..917
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 918..1637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1290..1547
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 977..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1408
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1296..1304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1637 AA; 184901 MW; 4DB46850A8C4C1F7 CRC64;
MNYILYILLI LIIFSINNTF SIGSFVYTPD GYYNLYRINK FENFSKIPTK ANSVNVEPHE
LYYPDICDSA LKNKNSNEFS IDNFPGSPFL KANIKITKGS NMTLDPLLSI HPSYINILCI
EGSFTAGSQQ TLTLGGIIVL PGGNFHCNNC VLQFVDLSST IIKIDPFGFL PGILSLGGSI
SLIGSQRILY SAKPIEDNVL EVNDISTLDP FNGFNVSIVS DSFPNVRTSR FTYNKNKLEM
QDLTIPTTDL NIKLFFNDSG SLKFGGISTR TKSSIYITGD TKLHIENYLL DSIGKTSNKE
YDDTKLTFSS DNPNNVTDII IGKNQRFRNS LYIEFSNSVT IKNSVIIGNT GSSRSSLVFF
QSNVNISGNL IVGTAGSSMI AQYGTEYIES SNNYFSLVLP NEFPTSPAFM DYGHEGNGIY
SLSPNIFSTN DIFNGQKILY NFNFISRENV TGFDKDCFAP CDINSIVVPS LSQEPIDFSK
NLVNPISINP VDYFLIVNSD EELKNTFFTI KDSTISSKII VNLKGSGLVL KNIIGVNNFK
LTGQVKRLDI YDSFFGSSTT PSLGDNGIKS SAVIIKNSSF YIDDFQLQNN QIYGSSIVPY
LYELLNVDEF ILVDSIFPTS QYQIPVGGKL DLIVKLVIIS PVISRITCEL ESDNETITSS
AISESVNKEC KFPLTFKNDG SVNLKVTVKL KNVGDSEIMY IINFPKITIF SNYSFYSGWS
MENSTENGII SVDGNSFKKG CSISSNDNSN NCTISNNIKY ITNLPKLNIS NDLNELFLNG
ITSINSNELV TITTRIDSET KYYQIQLFFI HQPIDDQPTP LSIYIENQPV FLLEPLESNS
APIFKNLTFN FDNINSLENI NISFATRGNT YLTSMAIYSS LVIEYPIPVE KINLLPIIVP
ICVTVLVLLS ILIVFFGARY YKHKKRRRLE IAVFGVELYS KKPSNNKSPV PSTPLIINSN
QEQSSSNHIS ITVNRNSDIQ TQSENNNLEP TTVETTTTTT TTAAGAILQT NVTLEMENLE
IKPIINNNEP FFEDYSDEYD DSSDGAELNE DDVEDYINII RGGNIKIEAE GELFVRQFER
NTFDQEFFEY KKSKIPSPHL VPSLAHGDFI ENPLNIIDIL LDPVTNEIPL EHYLKTYKNR
NGQSGKYRTN TQTHVLIADT IFQHCNDPDL PVSVSPYICD FGMNGRKSDL GEVCHDTITF
KNKLSEPLYA LFLFPEGDDS SITSSPFQSI ELKPNVETSI SLSVTLFSTT KYNEKVIVRF
ETLDVKQSWS TFVFLRLESE LTNIIDFNEI IIKNYISEGT FGIVYRGIWR SSPVAVKLLK
NEYVDHDEIE KEISLLERLR HPNILLYVGR FIFSGIHGIV TDYCSKGCLS KYIHENKYKI
TIIQKIRILI DISKACAYLH RNGITHRDLK PENILITSLN PKSLVCAKVS DFGTSKETNE
RYNLQTRRGT VAYMSNEILS QGSYTKSTDI YSFGMLCYEL FSERIPYYSE PHWRIRELVL
KNERPSLDQE IFKDTDISDI VTRCWSKNPS QRPTFDYLSK YLKHLLKKYD INNIIYDKDK
KNKKKNKNNN NNNNNNNNNN NNNNNNNNNN DDHDDNNNNI NDSDCDNNKN NNNNNNNNNN
NNNNNNNNNN NNNNNNN