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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
 
 
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