RHG12_MOUSE
ID RHG12_MOUSE Reviewed; 838 AA.
AC Q8C0D4; Q8BVP8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Rho GTPase-activating protein 12;
DE AltName: Full=Rho-type GTPase-activating protein 12;
GN Name=Arhgap12;
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=C57BL/6J; TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238 AND TYR-241, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-238, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-211; SER-213;
RP SER-238 AND TYR-241, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
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DR EMBL; AK031648; BAC27494.1; -; mRNA.
DR EMBL; AK077063; BAC36587.1; -; mRNA.
DR CCDS; CCDS37723.1; -.
DR RefSeq; NP_001034781.1; NM_001039692.1.
DR RefSeq; NP_083553.2; NM_029277.2.
DR PDB; 6GVC; X-ray; 2.60 A; Q/R/S/T=615-838.
DR PDBsum; 6GVC; -.
DR AlphaFoldDB; Q8C0D4; -.
DR SMR; Q8C0D4; -.
DR BioGRID; 217463; 1.
DR IntAct; Q8C0D4; 1.
DR MINT; Q8C0D4; -.
DR STRING; 10090.ENSMUSP00000138585; -.
DR iPTMnet; Q8C0D4; -.
DR PhosphoSitePlus; Q8C0D4; -.
DR EPD; Q8C0D4; -.
DR jPOST; Q8C0D4; -.
DR MaxQB; Q8C0D4; -.
DR PaxDb; Q8C0D4; -.
DR PeptideAtlas; Q8C0D4; -.
DR PRIDE; Q8C0D4; -.
DR ProteomicsDB; 255263; -.
DR Antibodypedia; 26325; 63 antibodies from 20 providers.
DR DNASU; 75415; -.
DR Ensembl; ENSMUST00000182559; ENSMUSP00000138585; ENSMUSG00000041225.
DR GeneID; 75415; -.
DR KEGG; mmu:75415; -.
DR UCSC; uc008dzc.1; mouse.
DR CTD; 94134; -.
DR MGI; MGI:1922665; Arhgap12.
DR VEuPathDB; HostDB:ENSMUSG00000041225; -.
DR eggNOG; KOG1450; Eukaryota.
DR GeneTree; ENSGT00950000182860; -.
DR HOGENOM; CLU_015883_6_0_1; -.
DR InParanoid; Q8C0D4; -.
DR OMA; NDGKWED; -.
DR PhylomeDB; Q8C0D4; -.
DR TreeFam; TF329345; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 75415; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Arhgap12; mouse.
DR PRO; PR:Q8C0D4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8C0D4; protein.
DR Bgee; ENSMUSG00000041225; Expressed in animal zygote and 255 other tissues.
DR ExpressionAtlas; Q8C0D4; baseline and differential.
DR Genevisible; Q8C0D4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; ISO:MGI.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd12070; SH3_ARHGAP12; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035491; ARHGAP12_SH3.
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 InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; GTPase activation; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..838
FT /note="Rho GTPase-activating protein 12"
FT /id="PRO_0000056715"
FT DOMAIN 10..72
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 263..296
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 355..388
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 466..567
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 648..836
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 155..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17947660, ECO:0007744|PubMed:21183079"
FT MOD_RES 241
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT CONFLICT 42
FT /note="K -> N (in Ref. 1; BAC27494)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="P -> A (in Ref. 1; BAC36587)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="A -> P (in Ref. 1; BAC36587)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="S -> T (in Ref. 1; BAC36587)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="A -> T (in Ref. 1; BAC36587)"
FT /evidence="ECO:0000305"
FT HELIX 616..628
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 632..637
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 650..656
FT /evidence="ECO:0007829|PDB:6GVC"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 663..675
FT /evidence="ECO:0007829|PDB:6GVC"
FT TURN 676..678
FT /evidence="ECO:0007829|PDB:6GVC"
FT TURN 680..684
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 689..700
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 715..727
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 739..747
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 750..762
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 766..784
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 786..789
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 793..804
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 818..830
FT /evidence="ECO:0007829|PDB:6GVC"
FT HELIX 832..835
FT /evidence="ECO:0007829|PDB:6GVC"
SQ SEQUENCE 838 AA; 95352 MW; C8660927694567AB CRC64;
MAERSGKITA GQAYIEVEYD YEYDAKDRKI VIRQGERYLL VKKTNDDWWQ VRPDENSKAF
YVPAQYVKEV TRKALMPPVK QATGLPNNSM KTIQSMHLQR STENVNKMPE LSSFGKPSSS
VQGTGLIRDA NQNFGSNYNS GQTLNLSLDL THNNGKFNSD SHSPKVSSQN RTRLFGHFPG
PEFLDIEKTS FSQEQSCDSA GEGSERIQQD SESGDELSSS STEQMRATTP PNQGRPDSPV
YANLQELKIS QSALPPLPGS PAIQVNGEWE THKDSSGRCY YYNRTTQERT WKPPRWARDV
STSRDFQSPG EQEPLSSEEN YHSSCFSQSD SQCGSPPRGW SEELDERGHT LYTSDYTKEK
WLKHVDDQGR QYYYSADGSR SEWELPKYNA SSQQQREIIK SRSLDRRLQE PIVLTKWRHS
TIVLDSNDKD SPTTTKLCLP ENESPPTSSK HQDPGQEKYG LLNVTKITEN GKKVRKNWLS
SWAVLQGSSL LFTKTQGSST SWFGSNQSKP EFTVDLKGAV IEMASKDKSS KKNVFELKTR
QGTELLIQSD NDAVINDWFK VLSSTINNQV AEADEAAEEE TPDSPGVEKH DKEKDQKELK
KLRSMKGSSM DSSEQKKTKK NLKKFLTRRP TLQAVREKGY IKDQVFGSNL ANLCQRENGT
VPKFVKLCIE HVEEHGLDVD GIYRVSGNLA VIQKLRFAVN HDEKLDLNDS KWEDIHVITG
ALKMFFRELP EPLFTFNHFN DFVNAIKQEP RQRVTAVKDL IRQLPKPNQD TMQILFRHLK
RVIENGEKNR MTYQSIAIVF GPTLLKPERE TGNIAVHTVY QNQIVELILL ELSTVFGR
