RHG33_MOUSE
ID RHG33_MOUSE Reviewed; 1305 AA.
AC Q80YF9; Q6P7W6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Rho GTPase-activating protein 33;
DE AltName: Full=Rho-type GTPase-activating protein 33;
DE AltName: Full=Sorting nexin-26;
DE AltName: Full=Tc10/CDC42 GTPase-activating protein;
GN Name=Arhgap33; Synonyms=Snx26, Tcgap;
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 [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INDUCTION, INTERACTION WITH CDC42 AND RHOQ, AND POSSIBLE FUNCTION.
RC TISSUE=Adipocyte;
RX PubMed=12773384; DOI=10.1093/emboj/cdg262;
RA Chiang S.-H., Hwang J., Legendre M., Zhang M., Kimura A., Saltiel A.R.;
RT "TCGAP, a multidomain Rho GTPase-activating protein involved in insulin-
RT stimulated glucose transport.";
RL EMBO J. 22:2679-2691(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-1305.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-660 AND SER-749, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1263, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking (By similarity). Could play an important role in the
CC regulation of glucose transport by insulin. May act as a downstream
CC effector of RHOQ/TC10 in the regulation of insulin-stimulated glucose
CC transport. {ECO:0000250}.
CC -!- SUBUNIT: Specifically interacts with CDC42 and RHOQ/TC10 through its
CC Rho-GAP domain. Interacts with NEK6 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12773384}.
CC Note=Translocates to the plasma membrane in response to insulin in
CC adipocytes.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and testis. Also
CC expressed in white adipose tissue (WAT) and muscle at a low level.
CC {ECO:0000269|PubMed:12773384}.
CC -!- INDUCTION: Dramatically induced during adipocyte differentiation.
CC {ECO:0000269|PubMed:12773384}.
CC -!- DOMAIN: The N-terminal PX domain interacts specifically with
CC phosphatidylinositol 4,5-bisphosphate.
CC -!- SIMILARITY: Belongs to the PX domain-containing GAP family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY217764; AAO89073.1; -; mRNA.
DR EMBL; BC065086; AAH65086.1; -; mRNA.
DR EMBL; BC065166; AAH65166.1; -; mRNA.
DR EMBL; BC066047; AAH66047.1; -; mRNA.
DR EMBL; BC061471; AAH61471.1; ALT_INIT; mRNA.
DR CCDS; CCDS21095.1; -.
DR RefSeq; NP_001276599.1; NM_001289670.1.
DR RefSeq; NP_001276611.1; NM_001289682.1.
DR RefSeq; NP_839983.1; NM_178252.3.
DR RefSeq; XP_006539951.1; XM_006539888.3.
DR AlphaFoldDB; Q80YF9; -.
DR SMR; Q80YF9; -.
DR BioGRID; 231366; 27.
DR IntAct; Q80YF9; 12.
DR STRING; 10090.ENSMUSP00000038412; -.
DR iPTMnet; Q80YF9; -.
DR PhosphoSitePlus; Q80YF9; -.
DR EPD; Q80YF9; -.
DR MaxQB; Q80YF9; -.
DR PaxDb; Q80YF9; -.
DR PRIDE; Q80YF9; -.
DR ProteomicsDB; 254967; -.
DR Antibodypedia; 29527; 134 antibodies from 26 providers.
DR DNASU; 233071; -.
DR Ensembl; ENSMUST00000044338; ENSMUSP00000038412; ENSMUSG00000036882.
DR Ensembl; ENSMUST00000207860; ENSMUSP00000146602; ENSMUSG00000036882.
DR Ensembl; ENSMUST00000208538; ENSMUSP00000146767; ENSMUSG00000036882.
DR GeneID; 233071; -.
DR KEGG; mmu:233071; -.
DR UCSC; uc009geq.2; mouse.
DR CTD; 115703; -.
DR MGI; MGI:2673998; Arhgap33.
DR VEuPathDB; HostDB:ENSMUSG00000036882; -.
DR eggNOG; KOG1449; Eukaryota.
DR GeneTree; ENSGT00940000155110; -.
DR HOGENOM; CLU_009183_0_0_1; -.
DR InParanoid; Q80YF9; -.
DR OMA; NTSMHIR; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q80YF9; -.
DR TreeFam; TF351451; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR BioGRID-ORCS; 233071; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Arhgap33; mouse.
DR PRO; PR:Q80YF9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80YF9; protein.
DR Bgee; ENSMUSG00000036882; Expressed in embryonic brain and 143 other tissues.
DR ExpressionAtlas; Q80YF9; baseline and differential.
DR Genevisible; Q80YF9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR035510; ARHGAP33.
DR InterPro; IPR036871; PX_dom_sf.
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 PANTHER; PTHR15729:SF11; PTHR15729:SF11; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; GTPase activation; Membrane; Methylation; Phosphoprotein;
KW Protein transport; Reference proteome; SH3 domain; Transport.
FT CHAIN 1..1305
FT /note="Rho GTPase-activating protein 33"
FT /id="PRO_0000056722"
FT DOMAIN 83..192
FT /note="PX; atypical"
FT DOMAIN 210..272
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 339..534
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1188
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1263
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 357
FT /note="R -> C (in Ref. 2; AAH61471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1305 AA; 139801 MW; AA8723BDF4A3CBB6 CRC64;
MLQAQKQSDP ILPWGASWAG RGQTLRARST DSLDGPGEGS VQPVPTTGGP GTKGKPGKRL
SAPRGPFPRL ADCAHFHYEN VDFGHIQLLL SPEREGPSLS GENELVFGVQ VTCQGRSWPV
LRSYDDFRSL DAHLHRCIFD RRFSCLPELP PPPEGTRAAQ MLVPLLLQYL ETLSGLVDSN
LNCGPVLTWM ELDNHGRRLL LSEEASLNIP AVAAAHVVKR YTAQAPDELS FEVGDIVSVI
DMPPTEDRSW WRGKRGFQVG FFPSECVELF TERPGPGLKA DADSPLCGIP APQGISSLTS
AVPRPRGKLA GLLRTFMRSR PSRQRLRQRG ILRQRVFGCD LGEHLSNSGQ DVPQVLRCCS
EFIEAHGVVD GIYRLSGVSS NIQRLRHEFD SERIPELSGP AFLQDIHSVS SLCKLYFREL
PNPLLTYQLY GKFSEAMSVP GEEERLVRVH DVIQQLPPPH YRTLEYLLRH LARMARHSAN
TSMHARNLAI VWAPNLLRSM ELESVGLGGA AAFREVRVQS VVVEFLLTHV EVLFSDTFTS
AGLDPAGRCL LPRPKSLAGS SPSTRLLTLE EAQARTQGRL GTPTEPTTPK TPASPVERRK
RERAEKQRKP GGSSWKTFFA LGRGPSIPRK KPLPWLGGSR APPQPSGSRP DTVTLRSAKS
EESLSSQASG AGLQRLHRLR RPHSSSDAFP VGPAPAGSCE SLSSSSSSSS SSSSSSSSES
SAGGLGPLSG SPSHRTSAWL DDGDDLDFSP PRCLEGLRGL DFDPLTFRCS SPTPGDPAPP
ASPAPPASAS AFPPRATPQA LSPHGPTKPA SPTALDISEP LAVSVPPAVL ELLGAGGTPA
SATPTPALSP HLIPLLLRGA EAQLSDTCQQ EISSKLAPTR GAPGQQSPGG MDSPLLPPPL
PLLRPGGAPP PPPKNPARLM ALALAERAQQ VAEQQSQQEQ GGTPPAPHSP FRRSLSLEVG
GEPVGTSGSG IHPPSLAHPG AWAPGPPPYL PRQQSDGSLV RSQRPLGTSR RSPRGPSQVS
AHLRASGAYR DAPEMAAQSP CSVPSQGSNP SFFSTPRECL PPFLGVPKQG LYSLGPPSFP
PSSPAPVWRN SLGAPSALDR GENLYYEIGV GEGTSYSGPS RSWSPFRSMP PDRHNASYGM
LGQSPPLHRS PDFLLSYPPP PSCFPPEHLT HSVSQRLARR PTRPEPLYVN LALGPRGPSP
ASSSSSSPPA HPRSRSDPGP PVPRLPQKQR APWGPHTPHR VPGPWGSPEP FLLYRPAPPS
YGRGGEVRGS LYRNGGHRGE GAGPPPPYPT PSWSLHSEGQ TRSYC
