SMEK_DICDI
ID SMEK_DICDI Reviewed; 1046 AA.
AC Q54I18;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Suppressor of Mek1;
DE Short=SMEK;
GN Name=smkA; ORFNames=DDB_G0289067;
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 FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND DEVELOPMENTAL STAGE.
RX PubMed=16107728; DOI=10.1128/mcb.25.17.7839-7853.2005;
RA Mendoza M.C., Du F., Iranfar N., Tang N., Ma H., Loomis W.F., Firtel R.A.;
RT "Loss of SMEK, a novel, conserved protein, suppresses MEK1 null cell
RT polarity, chemotaxis, and gene expression defects.";
RL Mol. Cell. Biol. 25:7839-7853(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPP4C.
RX PubMed=17353263; DOI=10.1128/mcb.02194-06;
RA Mendoza M.C., Booth E.O., Shaulsky G., Firtel R.A.;
RT "MEK1 and protein phosphatase 4 coordinate Dictyostelium development and
RT chemotaxis.";
RL Mol. Cell. Biol. 27:3817-3827(2007).
CC -!- FUNCTION: Suppresses MEK1 null cell polarity, chemotaxis, and gene
CC expression defects. Required for proper cytokinesis during vegetative
CC growth, timely exit from the mound stage during development, and myosin
CC II assembly. May be a regulatory subunit of serine/threonine-protein
CC phosphatase 4 (PP4) and may control localization of PP4 to the nucleus.
CC Involved in the regulation of some ppp4c functions, such as
CC developmental progression, chemotaxis, expression of stress response
CC genes and cell movement. {ECO:0000269|PubMed:16107728,
CC ECO:0000269|PubMed:17353263}.
CC -!- SUBUNIT: Interacts with ppp4c. {ECO:0000269|PubMed:17353263}.
CC -!- INTERACTION:
CC Q54I18; Q9Y0B7: ppp4c; NbExp=2; IntAct=EBI-2015890, EBI-2015876;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:16107728}. Nucleus {ECO:0000269|PubMed:16107728}.
CC Note=Localizes to the cell cortex in vegetative cells but translocates
CC to the nucleus during starvation and development (PubMed:16107728).
CC -!- DEVELOPMENTAL STAGE: Levels are constant throughout development.
CC {ECO:0000269|PubMed:16107728}.
CC -!- DOMAIN: The EVH1/WH1 domain is necessary for cortical localization.
CC {ECO:0000269|PubMed:16107728}.
CC -!- SIMILARITY: Belongs to the SMEK family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000129; EAL62912.1; -; Genomic_DNA.
DR RefSeq; XP_636416.1; XM_631324.1.
DR AlphaFoldDB; Q54I18; -.
DR SMR; Q54I18; -.
DR IntAct; Q54I18; 1.
DR STRING; 44689.DDB0232046; -.
DR PaxDb; Q54I18; -.
DR PRIDE; Q54I18; -.
DR EnsemblProtists; EAL62912; EAL62912; DDB_G0289067.
DR GeneID; 8626945; -.
DR KEGG; ddi:DDB_G0289067; -.
DR dictyBase; DDB_G0289067; smkA.
DR eggNOG; KOG2175; Eukaryota.
DR HOGENOM; CLU_004909_3_0_1; -.
DR InParanoid; Q54I18; -.
DR OMA; MMRGYML; -.
DR PhylomeDB; Q54I18; -.
DR PRO; PR:Q54I18; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IDA:dictyBase.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IGI:dictyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006887; DUF625.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF04802; SMK-1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..1046
FT /note="Suppressor of Mek1"
FT /id="PRO_0000254608"
FT DOMAIN 1..101
FT /note="WH1"
FT REGION 626..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1003..1022
FT /note="Nuclear localization signal"
FT COMPBIAS 626..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..689
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..757
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1046 AA; 119988 MW; BE7680EFA773B572 CRC64;
MEPLRKRVKV YQLDNSGKWD DKGTGHVSCI YVDALCAMGL IVRSESDNSV ILQTRLSAED
IYQKQQDSLI VWTEPDSQLD LALSFQDSLG CQDIWENILQ YQNQRTGSCD SVDLDLPPVS
INNLQTINEL LEASLPMLDK DKIINSIFKE DLVRSLLDLF DEIEKSGEGG VHLFQIFNIF
KNLILFNDTS ILEVILSEDY LVRVMGALEY DPEISENNRI KHREFLNQQV VFKQVIKFPS
KSLIGTIHQT FRIQYLKDVV LPRVLDDVTF SSLNSLIYFN NIDIVSQIQN DSDFLENLFS
EIQKSEKNSE ERKDLILFLQ DLCNLAKGLQ IQSKSTFFTV VVSLGLFKTL SAILDDENVQ
TRVSCTEIVL STLLHDPEIL RSYLCSPTSG NSKFLVQLIN LFITDKDIGV KNQIVEIIKT
LLEADSYDSS DFFRLFYDKG IDLLVSPLNE VYKGEPTIPG DPSSNLDSFV LYNIMELVIY
CIKHHCYRIK HFIVEEGIAK KILRYTNPTG SGGGGGGGGN SERYLILGSI RFFRSMVNMK
DDLYNQHIIQ ENLFEPIIEV FKSNISRYNL LNSAIIELFQ YIYKENIRDL IVYLVERYRE
LFESVTYTDV LKQLILKYEQ IKDSSFESPE TSCNNNDSSS NDIDSKPIIG NNKINHNYQR
TQREIDEEEE EAYFNRDDDS EDSDDEDELI PISINNNNNN NNNNKQICTN NENNMEKNDD
NIEKDNENTN NGNGSSHIKI VDYEDEDDED DEINKSVESD DIVEKHEIID KNEKKDEIMK
ENNDSDNDDN DNNDNDNDND NNSDIENKNH LNNNGNNENN ENNDDVQDKS NNKNNSDKIN
EDEKIEKQDE MKENLEMEEI DEKVKEKQPK DIKKENQSQP DETVFNGKSN NSNNNNNNNN
NNSNNQEIGD NRKTTPKRKL DYEKNESVVS KKIDKSNGPT SIDKDINGCD ESPNKKLNNN
NSNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNQNDENEL SSASEEEEEQ LENGKHIKKF
KRGKKDSNNS SNNSNNSSPT PSELHV
