RHG15_MOUSE
ID RHG15_MOUSE Reviewed; 481 AA.
AC Q811M1; Q3T9M8; Q3TCU0; Q8C0I5; Q8JZY0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Rho GTPase-activating protein 15;
DE AltName: Full=ArhGAP15;
DE AltName: Full=Rho-type GTPase-activating protein 15;
GN Name=Arhgap15;
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] (ISOFORMS 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. Has activity toward RAC1.
CC Overexpression results in an increase in actin stress fibers and cell
CC contraction (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q811M1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q811M1-2; Sequence=VSP_031051, VSP_031052;
CC Name=3;
CC IsoId=Q811M1-3; Sequence=VSP_031049, VSP_031050;
CC Name=4;
CC IsoId=Q811M1-4; Sequence=VSP_031048;
CC -!- DOMAIN: The PH domain is required for localization to the membrane.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34881.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK031022; BAC27217.1; -; mRNA.
DR EMBL; AK170537; BAE41865.1; -; mRNA.
DR EMBL; AK172407; BAE42992.1; -; mRNA.
DR EMBL; AL732320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024887; AAH24887.1; -; mRNA.
DR EMBL; BC034881; AAH34881.1; ALT_INIT; mRNA.
DR CCDS; CCDS16019.1; -. [Q811M1-1]
DR RefSeq; NP_722542.2; NM_153820.3. [Q811M1-1]
DR RefSeq; XP_006498462.1; XM_006498399.3.
DR AlphaFoldDB; Q811M1; -.
DR SMR; Q811M1; -.
DR BioGRID; 217972; 42.
DR IntAct; Q811M1; 1.
DR STRING; 10090.ENSMUSP00000056461; -.
DR iPTMnet; Q811M1; -.
DR PhosphoSitePlus; Q811M1; -.
DR EPD; Q811M1; -.
DR jPOST; Q811M1; -.
DR MaxQB; Q811M1; -.
DR PaxDb; Q811M1; -.
DR PRIDE; Q811M1; -.
DR ProteomicsDB; 255200; -. [Q811M1-1]
DR ProteomicsDB; 255201; -. [Q811M1-2]
DR ProteomicsDB; 255202; -. [Q811M1-3]
DR ProteomicsDB; 255203; -. [Q811M1-4]
DR Antibodypedia; 33613; 127 antibodies from 20 providers.
DR DNASU; 76117; -.
DR Ensembl; ENSMUST00000055776; ENSMUSP00000056461; ENSMUSG00000049744. [Q811M1-1]
DR Ensembl; ENSMUST00000112822; ENSMUSP00000108441; ENSMUSG00000049744. [Q811M1-4]
DR GeneID; 76117; -.
DR KEGG; mmu:76117; -.
DR UCSC; uc008jou.2; mouse. [Q811M1-3]
DR UCSC; uc008jov.1; mouse. [Q811M1-2]
DR UCSC; uc008jow.1; mouse. [Q811M1-1]
DR CTD; 55843; -.
DR MGI; MGI:1923367; Arhgap15.
DR VEuPathDB; HostDB:ENSMUSG00000049744; -.
DR eggNOG; KOG1449; Eukaryota.
DR eggNOG; KOG1450; Eukaryota.
DR GeneTree; ENSGT00950000182860; -.
DR HOGENOM; CLU_2196054_0_0_1; -.
DR InParanoid; Q811M1; -.
DR OMA; DHNQWED; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q811M1; -.
DR TreeFam; TF329345; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 76117; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Arhgap15; mouse.
DR PRO; PR:Q811M1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q811M1; protein.
DR Bgee; ENSMUSG00000049744; Expressed in granulocyte and 162 other tissues.
DR ExpressionAtlas; Q811M1; baseline and differential.
DR Genevisible; Q811M1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTPase activation; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..481
FT /note="Rho GTPase-activating protein 15"
FT /id="PRO_0000317575"
FT DOMAIN 87..197
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 287..476
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53QZ3"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53QZ3"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYC5"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYC5"
FT VAR_SEQ 109..481
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031048"
FT VAR_SEQ 167..186
FT /note="ITTVSGNEFLLQSDIDFLIL -> VRMPPVLNFLLFPPNLSPLR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031049"
FT VAR_SEQ 187..481
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031050"
FT VAR_SEQ 316
FT /note="L -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031051"
FT VAR_SEQ 317..481
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031052"
FT CONFLICT 46
FT /note="Q -> K (in Ref. 1; BAE41865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 55339 MW; B679FC5159BE20B2 CRC64;
MEKRTSCSVQ TSTNCDNSLE ILNSAHQATG AVQMRIKNAN SHQDRQSQTK SMILTDAGKV
TEPISRHRRN HSQHVLKDVI PPLEHPMVEK EGYLQKAKIA DGGKKLRKNW STSWIVLSGR
KIEFYKDSKQ QALPNMKTRH NVESVDLCGA HIEWAKEKSS RKSVFQITTV SGNEFLLQSD
IDFLILDWFQ AIKNAIDRLP KNPSCGSLEL FNLQRSSSSE LPSHCHIDRK EQKPEHRKSF
MFRLHHSASD TSDKNRVKSR LKKFISRRPS LKTLQEKGLI KDQIFGSHLH TVCEREHSTV
PWFVKQCIEA VEKRGLDVDG IYRVSGNLAT IQKLRFIVNQ EEKLNLDDSQ WEDIHVVTGA
LKMFFRELSE PLFPYSFFER FVEAIKKQDS NEKIETMRSL VKRLPPPNHD TMKILFRHLT
KIVAKASQNL MSTQSLGIVF GPTLLRAENE SGNVAVHMVY QNQIAEFMLT EYDKIFSSEE
D
