RHG42_MOUSE
ID RHG42_MOUSE Reviewed; 841 AA.
AC B2RQE8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Rho GTPase-activating protein 42 {ECO:0000312|MGI:MGI:1918794};
DE AltName: Full=Rho-type GTPase-activating protein 42 {ECO:0000312|MGI:MGI:1918794};
GN Name=Arhgap42 {ECO:0000312|MGI:MGI:1918794};
GN Synonyms=Graf3 {ECO:0000303|PubMed:24335996};
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] {ECO:0000312|EMBL:AAI37892.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649 AND SER-707, 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-342; SER-720 AND SER-723, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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, AND FUNCTION.
RX PubMed=24335996; DOI=10.1038/ncomms3910;
RA Bai X., Lenhart K.C., Bird K.E., Suen A.A., Rojas M., Kakoki M., Li F.,
RA Smithies O., Mack C.P., Taylor J.M.;
RT "The smooth muscle-selective RhoGAP GRAF3 is a critical regulator of
RT vascular tone and hypertension.";
RL Nat. Commun. 4:2910-2910(2013).
CC -!- FUNCTION: May influence blood pressure by functioning as a GTPase-
CC activating protein for RHOA in vascular smooth muscle.
CC {ECO:0000269|PubMed:24335996}.
CC -!- TISSUE SPECIFICITY: Highly and selectively expressed in smooth muscle
CC cells. {ECO:0000269|PubMed:24335996}.
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DR EMBL; BC137891; AAI37892.1; -; mRNA.
DR EMBL; BC137892; AAI37893.1; -; mRNA.
DR CCDS; CCDS52720.1; -.
DR RefSeq; NP_082099.1; NM_027823.1.
DR AlphaFoldDB; B2RQE8; -.
DR SMR; B2RQE8; -.
DR BioGRID; 214772; 36.
DR STRING; 10090.ENSMUSP00000091419; -.
DR iPTMnet; B2RQE8; -.
DR PhosphoSitePlus; B2RQE8; -.
DR MaxQB; B2RQE8; -.
DR PaxDb; B2RQE8; -.
DR PRIDE; B2RQE8; -.
DR ProteomicsDB; 255267; -.
DR Antibodypedia; 51394; 53 antibodies from 13 providers.
DR Ensembl; ENSMUST00000093893; ENSMUSP00000091419; ENSMUSG00000050730.
DR GeneID; 71544; -.
DR KEGG; mmu:71544; -.
DR UCSC; uc009odp.2; mouse.
DR CTD; 143872; -.
DR MGI; MGI:1918794; Arhgap42.
DR VEuPathDB; HostDB:ENSMUSG00000050730; -.
DR eggNOG; KOG1451; Eukaryota.
DR GeneTree; ENSGT00940000155492; -.
DR HOGENOM; CLU_011532_1_0_1; -.
DR InParanoid; B2RQE8; -.
DR OMA; KASGKMN; -.
DR OrthoDB; 693048at2759; -.
DR PhylomeDB; B2RQE8; -.
DR TreeFam; TF316851; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 71544; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Arhgap42; mouse.
DR PRO; PR:B2RQE8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; B2RQE8; protein.
DR Bgee; ENSMUSG00000050730; Expressed in animal zygote and 200 other tissues.
DR ExpressionAtlas; B2RQE8; baseline and differential.
DR Genevisible; B2RQE8; MM.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:MGI.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IGI:MGI.
DR GO; GO:1904694; P:negative regulation of vascular associated smooth muscle contraction; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
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 Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; GTPase activation; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..841
FT /note="Rho GTPase-activating protein 42"
FT /id="PRO_0000399498"
FT DOMAIN 7..228
FT /note="BAR"
FT /evidence="ECO:0000255"
FT DOMAIN 231..340
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 342..538
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 783..841
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 541..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..227
FT /evidence="ECO:0000255"
FT COMPBIAS 550..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 342
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NI28"
FT MOD_RES 837
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A6NI28"
SQ SEQUENCE 841 AA; 94636 MW; C69170FCA44EDB95 CRC64;
MGLPTLEFSD SYLDSPDFRE RLQCHEIELE RTNKFIKELL KDGSLLIGAL RNLSMAVQKF
SQSLQDFQFE CIGDAETDDE ISIAQSLKEF ARLLIAVEEE RRRLIQNAND VLIAPLEKFR
KEQIGAAKAD SQIGREHQNF YEASLEYVFK IQEVQEKKKF EFVEPLLSFL QGLFTFYHEG
YELAQEFAPY KQQLQFNLQN TRNNFESTRQ EVERLMQRMK SANQDYRPPS QWTMEGYLYV
QEKRPLGFTW TKHYCTYDKG SKMFTMSVSD VKASGKMNGL VTGSPEMFKL KSCIRRKTDS
IDKRFCFDIE VVERHGIITL QAFSEANRKL WLEAMDGKEP IYTLPAIISK KEEMYLNEAG
FNFVRKCIQA VEMRGITILG LYRIGGVNSK VQKLMNTTFS PKSPPDMDID IELWDNKTIT
SGLKNYLRCL AEPLMTYKLH KDFIIAVKSD DQNYRVEAVH ALVHKLPEKN REMLDILIKH
LLKVSLHSQQ NLMTISNLGV IFGPTLMRAQ EETVAAMMNI KFQNIVVEIL IEHYEKIFHT
APDPNIPLPQ PQSRSGSRRT RAICLSTGSR KPRGRYTPCL AEPDSDSYSS SPDSTPMGSI
ESLSSHSSEQ NSTTKSTACQ PREKSGGIPW ITTPSSSNGQ KSQGLWTTSP ESSSREDATK
TDVESDCQSV ASITIPGNVS PPIDLVKKGP YGLSGLKRSS ASSSLRSISA AEGNKSYSGS
IQSLTSIGSK ESPKAIPNPE LPPKMCRRLR LDTASSNGYQ RPGSVVAAKA QLFENAGSPK
PVSSGRQAQA MYSCKAEHSH ELSFPQGAIF SNVHPSVEPG WLKATYEGRT GLVPENYVVF
L
