RHG18_MOUSE
ID RHG18_MOUSE Reviewed; 663 AA.
AC Q8K0Q5; Q8BP03; Q8R196;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Rho GTPase-activating protein 18;
DE AltName: Full=Rho-type GTPase-activating protein 18;
GN Name=Arhgap18 {ECO:0000312|MGI:MGI:1921160};
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 MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH30858.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH25004.1}, and
RC Liver {ECO:0000312|EMBL:AAH30858.1};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-663.
RC STRAIN=C57BL/6J; TISSUE=Muellerian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68 AND SER-260, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=21865595; DOI=10.1091/mbc.e11-04-0364;
RA Maeda M., Hasegawa H., Hyodo T., Ito S., Asano E., Yuang H., Funasaka K.,
RA Shimokata K., Hasegawa Y., Hamaguchi M., Senga T.;
RT "ARHGAP18, a GTPase-activating protein for RhoA, controls cell shape,
RT spreading, and motility.";
RL Mol. Biol. Cell 22:3840-3852(2011).
CC -!- FUNCTION: Rho GTPase activating protein that suppresses F-actin
CC polymerization by inhibiting Rho. Rho GTPase activating proteins act by
CC converting Rho-type GTPases to an inactive GDP-bound state. Plays a key
CC role in tissue tension and 3D tissue shape by regulating cortical
CC actomyosin network formation. Acts downstream of YAP1 and inhibits
CC actin polymerization, which in turn reduces nuclear localization of
CC YAP1. Regulates cell shape, spreading, and migration (By similarity).
CC {ECO:0000250|UniProtKB:Q8N392}.
CC -!- SUBUNIT: Interacts with MPHOSPH6. {ECO:0000250|UniProtKB:Q8N392}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N392}.
CC -!- TISSUE SPECIFICITY: Widely expressed: expressed in most organs, except
CC small intestine. {ECO:0000269|PubMed:21865595}.
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DR EMBL; BC025004; AAH25004.1; -; mRNA.
DR EMBL; BC030858; AAH30858.1; -; mRNA.
DR EMBL; AK078522; BAC37322.1; -; mRNA.
DR CCDS; CCDS23757.1; -.
DR RefSeq; NP_789807.1; NM_176837.2.
DR AlphaFoldDB; Q8K0Q5; -.
DR SMR; Q8K0Q5; -.
DR BioGRID; 216349; 33.
DR IntAct; Q8K0Q5; 16.
DR MINT; Q8K0Q5; -.
DR STRING; 10090.ENSMUSP00000044834; -.
DR iPTMnet; Q8K0Q5; -.
DR PhosphoSitePlus; Q8K0Q5; -.
DR CPTAC; non-CPTAC-4001; -.
DR EPD; Q8K0Q5; -.
DR jPOST; Q8K0Q5; -.
DR MaxQB; Q8K0Q5; -.
DR PaxDb; Q8K0Q5; -.
DR PeptideAtlas; Q8K0Q5; -.
DR PRIDE; Q8K0Q5; -.
DR ProteomicsDB; 254873; -.
DR Antibodypedia; 46605; 188 antibodies from 30 providers.
DR DNASU; 73910; -.
DR Ensembl; ENSMUST00000039557; ENSMUSP00000044834; ENSMUSG00000039031.
DR GeneID; 73910; -.
DR KEGG; mmu:73910; -.
DR UCSC; uc007ese.1; mouse.
DR CTD; 93663; -.
DR MGI; MGI:1921160; Arhgap18.
DR VEuPathDB; HostDB:ENSMUSG00000039031; -.
DR eggNOG; KOG2200; Eukaryota.
DR GeneTree; ENSGT00940000157142; -.
DR HOGENOM; CLU_023268_2_1_1; -.
DR InParanoid; Q8K0Q5; -.
DR OMA; QHNMESQ; -.
DR OrthoDB; 700544at2759; -.
DR PhylomeDB; Q8K0Q5; -.
DR TreeFam; TF314044; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 73910; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Arhgap18; mouse.
DR PRO; PR:Q8K0Q5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8K0Q5; protein.
DR Bgee; ENSMUSG00000039031; Expressed in cumulus cell and 214 other tissues.
DR ExpressionAtlas; Q8K0Q5; baseline and differential.
DR Genevisible; Q8K0Q5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:2000145; P:regulation of cell motility; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; ISO:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:MGI.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..663
FT /note="Rho GTPase-activating protein 18"
FT /id="PRO_0000245790"
FT DOMAIN 324..523
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 14..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N392"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N392"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N392"
FT CONFLICT 293
FT /note="I -> F (in Ref. 2; BAC37322)"
FT /evidence="ECO:0000305"
FT CONFLICT 518..519
FT /note="YQ -> FN (in Ref. 1; AAH25004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 74930 MW; BB9ED06B850FEF41 CRC64;
MNWLSSSSGV VLTAYHPSGK DQVAGDSHVK GGDEATSSRR YGQYTINQEG STKVPERPPF
DRSSSQDSLD ESMEAYWTEL ENIKRSNENR QEGQEAIVVK EPDEGELEEE WLKEAGLSNL
FGESIDDPQE SILFLSTLTR TQAAAVQKRV ETVSQTLRKK NKQHHIRDVR DIFAQQREAQ
EKPPDDSDLR SVRTNENKGQ GKDDQPSSGA VDSKEQISRV PEDTPASETD INLEVSFAEQ
AVNQKEFSKE RTQKISSNDS LPSFRLPKDK TGTTRIGDLA PQDMKKVCSL SLIELTALYD
VLGLEFKQQK AVKIKTRDSG LFGIPLTILL EQDQRKVPGT RIPLIFQKLI SRIEEGSLET
EGLLRIPGAA MRIKNLCQEL EAKFYEGTFN WESVKQHDAA SLLKLFLREL PQPLLSMEYL
KAFQAVQNLP TRKEQLQALN LLVILLPDAN RDTLKALLEF LQRVIDNKEK NKMTAGNVAM
VMAPNLFMCH TLGLKSSEQR EFEMAAGTAN VMHLLIRYQK ILWTIPKFIV IQVRKQNIEN
QKKERKAMKK LLKKMAYDRE KHEKQDKTAN GADVPQGVIR VQAPHLSKVS MAIQLTEELK
ASDVLARFLS QESGVAQTLK KGEVFLYEIG GNIGERCLDD DTHMKDLYQL NPNAEWVIKS
KPV
