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GDT1_DICDI
ID   GDT1_DICDI              Reviewed;        1661 AA.
AC   Q54XS3; Q9GRX5; Q9U987;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable inactive serine/threonine-protein kinase gdt1;
DE   AltName: Full=Growth-differentiation transition protein 1;
DE   Flags: Precursor;
GN   Name=gdt1; ORFNames=DDB_G0278723;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 102-1661, FUNCTION, DEVELOPMENTAL
RP   STAGE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=AX2;
RX   PubMed=10793140; DOI=10.1091/mbc.11.5.1631;
RA   Zeng C., Anjard C., Riemann K., Konzok A., Nellen W.;
RT   "gdt1, a new signal transduction component for negative regulation of the
RT   growth-differentiation transition.";
RL   Mol. Biol. Cell 11:1631-1643(2000).
RN   [3]
RP   IDENTIFICATION, AND NOMENCLATURE.
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).
CC   -!- FUNCTION: Regulates the transition between growth and differentiation.
CC       {ECO:0000269|PubMed:10793140}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in vegetative cells only (at protein
CC       level). {ECO:0000269|PubMed:10793140}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- DISRUPTION PHENOTYPE: Cells overexpress discoidin and initiate
CC       multicellular development prematurely. {ECO:0000269|PubMed:10793140}.
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; AAFI02000024; EAL67963.2; -; Genomic_DNA.
DR   EMBL; AJ000992; CAB51908.1; -; Genomic_DNA.
DR   EMBL; AJ279060; CAC09932.1; -; Genomic_DNA.
DR   RefSeq; XP_641957.2; XM_636865.2.
DR   AlphaFoldDB; Q54XS3; -.
DR   SMR; Q54XS3; -.
DR   STRING; 44689.DDB0215003; -.
DR   PaxDb; Q54XS3; -.
DR   PRIDE; Q54XS3; -.
DR   EnsemblProtists; EAL67963; EAL67963; DDB_G0278723.
DR   GeneID; 8621689; -.
DR   KEGG; ddi:DDB_G0278723; -.
DR   dictyBase; DDB_G0278723; gdt1.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_251247_0_0_1; -.
DR   InParanoid; Q54XS3; -.
DR   PhylomeDB; Q54XS3; -.
DR   PRO; PR:Q54XS3; -.
DR   Proteomes; UP000002195; Chromosome 3.
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:0004672; F:protein kinase activity; IEA:InterPro.
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   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR026237; STKINASEGDT.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR02079; STKINASEGDT.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Developmental protein; Membrane; Nucleotide-binding;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1661
FT                   /note="Probable inactive serine/threonine-protein kinase
FT                   gdt1"
FT                   /id="PRO_0000323579"
FT   TOPO_DOM        21..1007
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1008..1028
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1029..1661
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1372..1661
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          802..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1089..1175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1547..1584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1378..1386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1399
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        121
FT                   /note="I -> V (in Ref. 2; CAB51908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        720
FT                   /note="F -> S (in Ref. 2; CAB51908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1243..1251
FT                   /note="ALSDFKDFS -> RHYQILKIFP (in Ref. 2; CAB51908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1591
FT                   /note="I -> N (in Ref. 2; CAB51908)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1661 AA;  186642 MW;  B6A5F41CD9018B83 CRC64;
     MKKILLSIFF VVFLLIGSEC ELIDTPPGYY NLKKIDKFQQ FSKIQIERNN KTIYSSSFHD
     LFYPDICEGT IQNIPGSLYF GRSSFPGAQE SSNLMITRGT KMKYRVGNGG IPIYKINVLC
     IEGTLEIPEG ISFFNVGALF ILPGGVLNSK SSIRFTDLDP YNSKMDPFNF FPGMMVLGGS
     LSLIGEKKRI FQATRIDDYQ LQIEDFKKIG SLTNNIYLGS KVTIYSQQIS EGQTCSFSFG
     ASNDKINLTS SSSSSLRGTN CLPISKNDKN IIVHFNCKYL LGGSSESFID STSTVGSSIY
     ITGDSQVQIE NFTLDSIGKT TNKLYNDTKL IFSNDKPNQV IDIIKGENQR FRNSLYIEFS
     NSVVIKGCAI IDRVKESRAP LIFVSSNVSL SESLIVSKSG SNLIAQYGTE FIKSKLNHYF
     LIPPLPQPFG LNSPINFPSP FSMDYGFEGN GIYSLSPNVQ SINDTFISQL IALNFNFIGN
     RSIITGFDND CYSPCTNTSI LFSNLIQYPV DFKINNSTYF YKLNNNNNDN NNNTNNFNLL
     NINNENNNND DNNNNNNSQN HYLLNINNNG NSPGRFFTIK DLVASDTVSA YLPNSALVFN
     NLNATENFSF NGTVSRLDFI NSSFNTNLTS TQKFFDETTT TVTNFQNTYI YGSPETTEPP
     EKVFGSSITP IYYFSKSVLD SLKVETVYPN EPHKMFFNSS VSLSVKLNNM GLKTPIICIF
     SSNGMESKEV QYNPISTKCS FLYVSEKLGN HNIRVTIKNE YSKDSSYYFI IDFPIITVYG
     QSLFNAGWQM IDPTSTTIIP TPTPTSTSTS TSTSTPTTTN NNQLVNDNNN KINELDGLKF
     QGGCIKTLGC QLSSNAKYVG GLPNVTASST LNSLFSWGIT SDVQYDPVII DLFINKSIAT
     LQVQLFFTFY KPIDQYSSPL SVSIQKNPVL VMEPFAGDQP FSKNLTFVYN NTQSLDFLNI
     SFTSRGDIYL TSLAIFSVSD SLPQIIDPIT PTLLPIESVK ASKPAILAIV LSIVLGSLAL
     SIITILIVKH RKRLSQFLSK SNKDIEYAQN NEIEIKVLPK ITSHSSYPSI SILDTISSDS
     IFNNQIPKNN NRYKFKNQSL NNNNYFNNNN NNNNSNNNNS NNIIYSNCNS NYSNSNSNNN
     NNNNNSNSNN NSNSNSNINI NSNSNSNSNS NSNGNNNYQI YSNKLESFKI DEISNDTIPI
     INSTFPDEFQ TLEFQKLAFE ILKREKRLDF SFRTTNDILT CCALSDFKDF SNFPLRFNQS
     IITFGLINGK AKLGETYYDT LSITNDSTIR FTAFLILPMD NHSATFTSDH SSFDLGPGET
     FSIKFSITLH CTTRFFENFS IQINSNNIKE MYTLLKIKVE SESSTRLDFN DIHFQELIEK
     YSWEILYRGT VGDKNALLKL IKLKTKNCEE AYRELNIISR LKHQNILPLI GCVISKDYLC
     LAFEYPPLGS LDYIISKKKL KMSITQKIRI LIDVAKGCKF LQQSSIIQKT LRARNIFLYD
     TNENAEVCAK VLDLTSSKTI KGLACNNYIE RVDTPINLTR EISIIRDPKQ NNDFNNSNNS
     NNNNNNNNNN NNNNNNNSNN SNNSSSLKYN IHSFAVLSYE LLIDEILVGD TRKFGQEKPS
     IGLDKIDPNI KNFIHKCWNP IDGFTFNEIL KTLKDFIESL N
 
 
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