ID B1AUY2_MOUSE Unreviewed; 944 AA. AC B1AUY2; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 05-FEB-2025, entry version 125. DE SubName: Full=Rho GTPase activating protein 4 {ECO:0000313|Ensembl:ENSMUSP00000110046.2}; GN Name=Arhgap4 {ECO:0000313|Ensembl:ENSMUSP00000110046.2, GN ECO:0000313|MGI:MGI:2159577}; 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 {ECO:0000313|Ensembl:ENSMUSP00000110046.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000110046.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110046.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RG Mouse Genome Sequencing Consortium; 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] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [3] {ECO:0000313|Ensembl:ENSMUSP00000110046.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110046.2}; RX PubMed=21750661; RA Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N., RA Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D., RA Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L., RA Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J., RA Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P., RA Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G., RA Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.; RT "Modernizing reference genome assemblies."; RL PLoS Biol. 9:e1001091-e1001091(2011). RN [4] {ECO:0000313|Ensembl:ENSMUSP00000110046.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110046.2}; RG Ensembl; RL Submitted (OCT-2024) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; NP_001155895.1; NM_001162423.1. DR AlphaFoldDB; B1AUY2; -. DR SMR; B1AUY2; -. DR jPOST; B1AUY2; -. DR ProteomicsDB; 312427; -. DR Antibodypedia; 360; 149 antibodies from 30 providers. DR DNASU; 171207; -. DR Ensembl; ENSMUST00000114404.8; ENSMUSP00000110046.2; ENSMUSG00000031389.18. DR GeneID; 171207; -. DR KEGG; mmu:171207; -. DR UCSC; uc012hkj.1; mouse. DR AGR; MGI:2159577; -. DR CTD; 393; -. DR MGI; MGI:2159577; Arhgap4. DR VEuPathDB; HostDB:ENSMUSG00000031389; -. DR GeneTree; ENSGT00950000182824; -. DR BioGRID-ORCS; 171207; 2 hits in 78 CRISPR screens. DR ChiTaRS; Arhgap4; mouse. DR Proteomes; UP000000589; Chromosome X. DR Bgee; ENSMUSG00000031389; Expressed in granulocyte and 120 other cell types or tissues. DR ExpressionAtlas; B1AUY2; baseline and differential. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd07656; F-BAR_srGAP; 1. DR FunFam; 1.10.555.10:FF:000026; Rho GTPase activating protein 4; 1. DR FunFam; 2.30.30.40:FF:000404; Rho GTPase-activating protein 4; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR031160; F_BAR. DR InterPro; IPR001060; FCH_dom. 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; IPR051627; SLIT-ROBO_RhoGAP. DR PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 1. DR Pfam; PF00611; FCH; 1. DR Pfam; PF00620; RhoGAP; 1. DR Pfam; PF00018; SH3_1; 1. DR SMART; SM00055; FCH; 1. DR SMART; SM00324; RhoGAP; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51741; F_BAR; 1. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE- KW ProRule:PRU01077}; GTPase activation {ECO:0000256|ARBA:ARBA00022468}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|PeptideAtlas:B1AUY2, KW ECO:0007829|ProteomicsDB:B1AUY2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}. FT DOMAIN 19..328 FT /note="F-BAR" FT /evidence="ECO:0000259|PROSITE:PS51741" FT DOMAIN 518..695 FT /note="Rho-GAP" FT /evidence="ECO:0000259|PROSITE:PS50238" FT DOMAIN 746..805 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT REGION 181..233 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 415..447 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 476..507 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 917..944 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 144..171 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 184..197 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 224..233 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 483..497 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 928..938 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 944 AA; 105226 MW; 1121493306B678B7 CRC64; MAAHGKLRRE RGLQPEYDAQ VKEMRWQLSE QLHCLELQGE LRRDLLQELA EFMRRRAEVE LEYSRGLDKL AERFTSRSGR LGGSSQEQQS FRKEPTLLSP LHCWAVLLEH TRQQSRESAA LSEVLAGPLA QRLSHISEDV GRIVKKSKDL VQQLQAELLE VVSELQTTKK MYHVYHSESM NAETKLREAE RQEEKRSGRS ALSTTTTTSA TTTTTTTTVE TGPHRKSSLK KGGRLVEKRQ AKYLEHKLKC TKARNEYLLS LASVNAAISN YYLHDILDLM DCCDTGFHLA LEQALRSYTA AESRTQTSQM QGLGSLEEAL EALDPPGDKA KVLEVHAMAF CPPLRFEYQP HEDDEVAEVL IEMELWDEIL PRAQNIQSRL DQKTIETEEV NKTLKATLKA LLEAVASEDG DILDSLQASP STESLKSTSS DPGTRQTGRR RNQQQETETF YITKLQEYLS GRSILSKLQA KHEKLQEAIQ QGNKEKQETS RTQCTERKFH KSHPPHPRFQ YNQRLFGGDL EKFIQSSGQP VPLVVESCIR FINLNGAQAR ISEIRDAFER GEDPLEKGCT VHDLDSVAGV LKLYFRSLEP PLFPLDMFNE LLASAELEVV GERVEPVSHL LFKLPRPVLV VLRYLFTFLN HLAQYSDENM MDSYNLAVCF GPTLLPVPAG QDPVALQGRV NQLVQTLILQ PARIFPPPAM LPGPIYEKCM APPSASCLGD GQLESLIGEP ELELKTGTTA QEDDQEGVLE AVACFAYTGR TAQELTFQRG DVLRLYARAS SDWWRGEHAG VQGLIPHKYI TLCEGDEKQM AGSGLQAMGE SVSHPEGFLT LEFANRLELG TPPEALGPSR HRRPCLVPTS PEGHVEMDKA VAQNMNSVFK ELLGKTAVRQ GHGLASTASP SLGTLTPLAC SSISKNKVFS RGPGAPISPS TSHPQGPDST RKPV //