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   24-JAN-2024, entry version 164.
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; 28.
DR   IntAct; Q80YF9; 12.
DR   STRING; 10090.ENSMUSP00000146602; -.
DR   iPTMnet; Q80YF9; -.
DR   PhosphoSitePlus; Q80YF9; -.
DR   EPD; Q80YF9; -.
DR   MaxQB; Q80YF9; -.
DR   PaxDb; 10090-ENSMUSP00000038412; -.
DR   ProteomicsDB; 254967; -.
DR   Antibodypedia; 29527; 137 antibodies from 26 providers.
DR   DNASU; 233071; -.
DR   Ensembl; ENSMUST00000044338.5; ENSMUSP00000038412.5; ENSMUSG00000036882.8.
DR   Ensembl; ENSMUST00000207860.2; ENSMUSP00000146602.2; ENSMUSG00000036882.8.
DR   Ensembl; ENSMUST00000208538.2; ENSMUSP00000146767.2; ENSMUSG00000036882.8.
DR   GeneID; 233071; -.
DR   KEGG; mmu:233071; -.
DR   UCSC; uc009geq.2; mouse.
DR   AGR; MGI:2673998; -.
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; SYGIREQ; -.
DR   OrthoDB; 2913909at2759; -.
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 78 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 145 other cell types or tissues.
DR   ExpressionAtlas; Q80YF9; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR   GO; GO:0001650; C:fibrillar center; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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; ISO:MGI.
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   CDD; cd04384; RhoGAP_CdGAP; 1.
DR   CDD; cd11835; SH3_ARHGAP32_33; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
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; CDC42 GTPASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR15729:SF11; RHO GTPASE-ACTIVATING PROTEIN 33; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q80YF9; MM.
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
//