ID A0A3Q7TXQ6_VULVU Unreviewed; 1301 AA.
AC A0A3Q7TXQ6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Rho GTPase-activating protein 33 isoform X1 {ECO:0000313|RefSeq:XP_025865982.1};
GN Name=ARHGAP33 {ECO:0000313|RefSeq:XP_025865982.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025865982.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025865982.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025865982.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025865982.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PX domain-containing GAP family.
CC {ECO:0000256|ARBA:ARBA00008795}.
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; XP_025865982.1; XM_026010197.1.
DR KEGG; vvp:112928470; -.
DR OrthoDB; 2913909at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; PF14604; SH3_9; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 193..255
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 322..517
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..909
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1301 AA; 138916 MW; EE598AC7FA9B5ACA CRC64;
MGWRGTEPRA RSTDSLDGPG EGSVQPLPHT GGPSVKGKPG KRLSAPRGPF PRLADCAHFH
YENVDFGHIQ LLLSPEREGP SFSGENELVF GVQVTCQGRS WPVLRSYDDF RSLDAHLHRC
IFDRRFSCLP ELPPPPEGAR AAQMLVPLLL QYLETLSGLV DSNLNCGPVL TWMELDNHGR
RLLLSEEASL NIPAVAAAHV IKRYTAQAPD ELSFEVGDIV SVIDMPPTED RSWWRGKRGF
QVGFFPSECV ELFTERPGPG LKGDADGPPC GVPTPQGVSS LTSAVPRPRG KLAGLLGTFM
RSRPSRQRLR QRGILRQRVF GCDLGEHLSN SGQDVPQVLR CCSEFIEAHG VVDGIYRLSG
VSSNIQRLRH EFDSERIPEL SGPAFLQDIH SVSSLCKLYF RELPNPLLTY QLYGKFSEAM
SVPGEEERLV RVHDVIQQLP PPHYRTLEYL LRHLARMARH SANTSMHARN LAIVWAPNLL
RSMELESVGL GGAAAFREVR VQSVVVEFLL THVDVLFSDT FTSAGLDPAG RCLLPRPKSL
AGSGPSTRLL TLEEAQARTQ GRLGTPTEPT TPKAPASPVE RRKGERGEKQ RKPGGSSWKT
FFALGRGPSI PRKKPLPWLG GTRAPPQPSG GRPDTVTLRS AKSEESLSSQ ASGAGLQRLH
RLRRPHSSSD AFPVGPAPAG SCESLSSSSS SSESSSSSES SSSGSSAAGL GALSGSPSHR
TSAWLDDGDE LDFSPPRCLE GLRGLDFDPL TFRCSSPTPG DPAPPASPAP PAPASAFPPR
VTPQALSPRG TTSPASPTAL DISEPLAVSV PPAVLELLGA GGTPASVTPA PALSPSPGLR
PHLIPLLLRG AEAQLSDTCQ QEICSKLALP IPRGAQGQHG PGMDSPLLPP PLSLLRPGGA
PPPPPKNPAR LMALALAERA QQVAQRQSQQ EHGGTPSAPH SPFHRSLSLE VGGEPPGTSG
VGPAPNSLAH PGAWVPGPPP SLPRQQSDGS LVRNQRPPGT SRRGLRGPAQ VSAQLGRGGC
RGRGHEPEMA AQLPCSVPSQ APTPGFFSSA PRECLPPFLG VPKPGLYPLG SPSFQPSSPA
PVWRSPLGPP APLDRGENLY YEIEAGEGTP YSGPTRSWSP FRSMPPDRLN ASYGLLGQSP
PLHRSPDFLL SYPPPPSCFP HDHLGYSAPQ HSARRPTRPE PLYVNLALGP RGPSPASSSS
SSPPAHPRSR SDPGPPAPRL PQKQRAPWGP HTPHRVPAPW GPPEPLLLYR AAPPAYGRGG
EHHRGSLYRN GGQGREGAGP PPPYPTPSWS LHSEGQTRSY C
//