PKHG6_MOUSE
ID PKHG6_MOUSE Reviewed; 787 AA.
AC Q8R0J1; E9QJZ0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Pleckstrin homology domain-containing family G member 6;
DE Short=PH domain-containing family G member 6;
GN Name=Plekhg6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Guanine nucleotide exchange factor activating the small
CC GTPase RHOA, which, in turn, induces myosin filament formation. Also
CC activates RHOG. Does not activate RAC1, or to a much lower extent than
CC RHOA and RHOG. Part of a functional unit, involving PLEKHG6, MYH10 and
CC RHOA, at the cleavage furrow to advance furrow ingression during
CC cytokinesis. In epithelial cells, required for the formation of
CC microvilli and membrane ruffles on the apical pole. Along with EZR,
CC required for normal macropinocytosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MYH10. Interacts with ELMO1 and EZR (in an open
CC conformation). Interacts with CSPP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus
CC {ECO:0000250|UniProtKB:Q3KR16}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q3KR16}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q3KR16}. Note=During mitosis, localizes to the
CC spindle pole, central spindle and cleavage furrow. In epithelial cells,
CC recruited to the apical membrane by EZR where it participates in
CC macropinocytosis. {ECO:0000250|UniProtKB:Q3KR16}.
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DR EMBL; AC140324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026778; AAH26778.1; -; mRNA.
DR CCDS; CCDS39642.1; -.
DR RefSeq; NP_941006.2; NM_198604.2.
DR RefSeq; XP_006505930.1; XM_006505867.2.
DR AlphaFoldDB; Q8R0J1; -.
DR SMR; Q8R0J1; -.
DR BioGRID; 229446; 10.
DR STRING; 10090.ENSMUSP00000037004; -.
DR iPTMnet; Q8R0J1; -.
DR PhosphoSitePlus; Q8R0J1; -.
DR PaxDb; Q8R0J1; -.
DR PRIDE; Q8R0J1; -.
DR ProteomicsDB; 289747; -.
DR Antibodypedia; 49879; 141 antibodies from 21 providers.
DR DNASU; 213522; -.
DR Ensembl; ENSMUST00000042647; ENSMUSP00000037004; ENSMUSG00000038167.
DR GeneID; 213522; -.
DR KEGG; mmu:213522; -.
DR UCSC; uc009dum.1; mouse.
DR CTD; 55200; -.
DR MGI; MGI:2682298; Plekhg6.
DR VEuPathDB; HostDB:ENSMUSG00000038167; -.
DR eggNOG; KOG3521; Eukaryota.
DR GeneTree; ENSGT00940000161250; -.
DR HOGENOM; CLU_021968_1_0_1; -.
DR InParanoid; Q8R0J1; -.
DR OMA; SPWESSE; -.
DR OrthoDB; 556467at2759; -.
DR PhylomeDB; Q8R0J1; -.
DR TreeFam; TF316755; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 213522; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Plekhg6; mouse.
DR PRO; PR:Q8R0J1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8R0J1; protein.
DR Bgee; ENSMUSG00000038167; Expressed in small intestine Peyer's patch and 91 other tissues.
DR Genevisible; Q8R0J1; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR042918; PLEKHG6.
DR PANTHER; PTHR47671; PTHR47671; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Cytoskeleton; GTPase activation;
KW Reference proteome.
FT CHAIN 1..787
FT /note="Pleckstrin homology domain-containing family G
FT member 6"
FT /id="PRO_0000307913"
FT DOMAIN 161..353
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 409..509
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 533..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 137
FT /note="S -> G (in Ref. 2; AAH26778)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="R -> Q (in Ref. 2; AAH26778)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="V -> I (in Ref. 2; AAH26778)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="G -> S (in Ref. 2; AAH26778)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="P -> S (in Ref. 2; AAH26778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 787 AA; 89148 MW; 0126CC8C6EAF4EC6 CRC64;
MQAFGPPNEG PLQGLVASRI ETYGGRHQTS AHSTAGNLFP RGGPGVDPSR RRLQHYVPFA
KGSGQTRGMS PLVLREPDPE KRHGSYFGVG PPHSPKLKEV TRAHELEIRL HTFSMFGMPR
LPPEDRRHWE IGEGGDSALT MEKSWKELVL EHKEMNRQLC HQQEALWELL TTELIYLRKL
KIMTDLLAAG LLNLQRVGLL TEVSAETLFG NVPNLIRAHR RFWEEVLQPI LEDTRTSGQP
LDPVSLQNGF LTFGQRFQPY VQYCLRVKQT MAYAREQQDT NPLFHTFVQW CEKHKRSGRQ
TLGDLLIKPH QRITKYPLLL QAVRKRSPEP RAQEALNAMI EAVESFLRHI NGQVRQGEEQ
ESLMAVAQRI GPYEVLEPSS EEVEKNLRPF STLDLMTPVL GVAPEYTRQL LLEGPVRVKE
GREGKMDVYL FLFSDVLLVT KPQRKADRAK VIRPPLMLEK LVCRPLRDPN SFLLIHLTEF
QCVSSALTVH CPSSTERARW LEKTQHAQTT LQKLKGEQYI QQKRELLALY RNQGTESPST
RPSTPSPSPE DSQSSAEGRT LEFAIIPRLV VTEDTDEDTP SMPDDASDSG YGTLIPSSPK
DSHSPLNRLR SKALRRDPRL TFSTLELRDV PLRPQPPDPQ APQRRSAPEL PEGILRGGSL
PRRAPPIWSE EEDETLASGN VVVETLHRAQ RRSPLPHSPT HTDSAGESPW ESSDEDEGLL
SPELRPRSLR EDMLREIREE LANQRIDGAS EPEPGNGKPR RLTLAQLQRM RVPHIIQLDT
PLSTSEV
