RHG35_XENLA
ID RHG35_XENLA Reviewed; 1477 AA.
AC Q6NU25;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Rho GTPase-activating protein 35 {ECO:0000250|UniProtKB:Q9NRY4};
DE AltName: Full=Rho GAP p190A {ECO:0000303|PubMed:28894085};
DE Short=p190-A {ECO:0000303|PubMed:28894085};
GN Name=arhgap35 {ECO:0000312|Xenbase:XB-GENE-999480};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:AAH68777.1};
RN [1] {ECO:0000312|EMBL:AAH68777.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH68777.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5U4U}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 587-762, AND DOMAIN.
RX PubMed=28894085; DOI=10.1038/s41467-017-00483-x;
RA Stiegler A.L., Boggon T.J.;
RT "p190RhoGAP proteins contain pseudoGTPase domains.";
RL Nat. Commun. 8:506-506(2017).
CC -!- FUNCTION: Rho GTPase-activating protein (GAP). Binds several acidic
CC phospholipids which inhibits the Rho GAP activity to promote the Rac
CC GAP activity. This binding is inhibited by phosphorylation by PRKCA (By
CC similarity). Involved in cell differentiation as well as cell adhesion
CC and migration (By similarity). Transduces SRC-dependent signals from
CC cell-surface adhesion molecules, such as laminin, to promote neurite
CC outgrowth. Regulates axon outgrowth, guidance and fasciculation (By
CC similarity). Modulates Rho GTPase-dependent F-actin polymerization,
CC organization and assembly, is involved in polarized cell migration and
CC in the positive regulation of ciliogenesis and cilia elongation (By
CC similarity). {ECO:0000250|UniProtKB:P81128,
CC ECO:0000250|UniProtKB:Q91YM2, ECO:0000250|UniProtKB:Q9NRY4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q91YM2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q91YM2}. Nucleus {ECO:0000250|UniProtKB:Q91YM2}.
CC Cell membrane {ECO:0000250|UniProtKB:Q91YM2}. Note=In response to
CC integrins and SDC4 and upon phosphorylation by PKC, relocalizes from
CC the cytoplasm to regions of plasma membrane ruffling where it
CC colocalizes with polymerized actin. {ECO:0000250|UniProtKB:Q91YM2}.
CC -!- DOMAIN: N-terminal part (1-266) has GTPase activity. Required for
CC proper cellular localization. {ECO:0000250|UniProtKB:Q91YM2}.
CC -!- DOMAIN: The pG1 pseudoGTPase domain does not bind GTP.
CC {ECO:0000269|PubMed:28894085}.
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 EMBL; BC068777; AAH68777.1; -; mRNA.
DR RefSeq; NP_001084674.1; NM_001091205.1.
DR PDB; 5U4U; X-ray; 1.90 A; A=587-762.
DR PDBsum; 5U4U; -.
DR AlphaFoldDB; Q6NU25; -.
DR SMR; Q6NU25; -.
DR DNASU; 414634; -.
DR GeneID; 414634; -.
DR KEGG; xla:414634; -.
DR CTD; 414634; -.
DR Xenbase; XB-GENE-999480; arhgap35.L.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 414634; Expressed in brain and 19 other tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.10.440; -; 2.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039007; pG1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR032835; RhoGAP-FF1.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR045786; RhoGAP_pG1_pG2.
DR InterPro; IPR039006; RhoGAP_pG2.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF01846; FF; 1.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16512; RhoGAP-FF1; 1.
DR Pfam; PF19518; RhoGAP_pG1_pG2; 1.
DR SMART; SM00441; FF; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51676; FF; 3.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW GTP-binding; GTPase activation; Lipid-binding; Membrane;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1477
FT /note="Rho GTPase-activating protein 35"
FT /id="PRO_0000443289"
FT DOMAIN 270..327
FT /note="FF 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01013"
FT DOMAIN 428..482
FT /note="FF 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01013"
FT DOMAIN 484..549
FT /note="FF 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01013"
FT DOMAIN 587..762
FT /note="pG1 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01199"
FT DOMAIN 778..940
FT /note="pG2 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01200"
FT DOMAIN 1243..1430
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..266
FT /note="Has GTPase activity, required for proper
FT localization"
FT /evidence="ECO:0000250|UniProtKB:Q91YM2"
FT REGION 965..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1230
FT /note="Required for phospholipid binding and regulation of
FT the substrate preference"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT REGION 1441..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 33..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 95..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 201..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
FT BINDING 229..231
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRY4"
SQ SEQUENCE 1477 AA; 168766 MW; 90C150E1A7BB9F4A CRC64;
MMMARKQDVR VPTYSISVVG LSGTEKEKGQ CGVGKSCLCN RFVRPSADDF HLDHTSVLST
SDFGGRVVNN DHFLYWGESG QMPEDCVDFK VHVVEQTEFI DDQTFQPHRS TALQPYIKRA
ASCKLASAEK LMYFCTDQLG LEQDFEQKQM PEGKLLIDGF LLCIDVSRGM NRNFDDQLKF
VSNLYTQMAK TKKPMVMVLT KCDEGVERYI RDAHSFALNK KNLQVVETSA RSNVNVDLAF
TTLVQLIDKS RGKSKIIPYF EALKQQSQLI AAAKDKYEWL VSRVVKSHNE TWINVNRRMQ
SSIEYQDYVH LEGTDKAKKL FHQHVQRLKQ EHIERRRKNY LSALPRALES LVPELDEIDR
LSWVKVSNLL ESKAEFLKVF IVLEETPWEF TNHIDSIDER IPYDLLETVS AAEVYASYLE
KLRNARKKEE MKRSFKDNLI TSPFITPGKP WEEARSFIMS EEFYQWLEEP VYMEIYSRHQ
KEIIDKAKEE FQELLLEYSE LFYELELDAK PSKEKMGVIQ DVLGEEQRFK ALQKLQAERD
ALILKHIHFV YHPTKDTCPS NPSCVDTKIE HILCSRCTYP YDRLQKDPNV DRINLVILGR
DGLARELANE IRALCTNDDK YVIDGKMYEL SLRPIEGNVR LPVNSFQTST FQPHGCLCLY
NSKESLSYVV ESIEKSRESS LGRKENHLIN LPLTLILVNR RGDTSSETAH SLIQHGQQVA
SKLQCVFLDA ASTGLGYGRN INEKQISLIL RGLLESKRNL NLVGSTPSIK DLTDCELRIV
MCLMCADLFN IEDVLNALKP HTYRPSQCGL GGSVLLDLPI GSQKRRLELM MLSYHSSFNV
RKTRLVHGYM IFYAAKRRAS LAMLRAFLCE VQDIVPVQIV ALTEGPLTFL ENVAREQLQE
GEEIAQDIEG KFLILPQGQT QPKFDVFYPF FKDVLEKKVI IEASHMYDNT AEACSTTEEV
FSSPRAGSPL CNSHLPDSEE DPEPSPQHLL FREEPNISVP TKFTRELEET ENLHFIPMIN
PLESKFNNKV PPPLKPKPPI PYEISKPELS YLDTGSRDGH RKSLTSINWP PLEAFDPSDY
AEPMDSVVKP RNQEENIYSV PHDSTQGKII TIRNTNKPQS NGSGNGSDSD MDTNSLERAR
KASIVTKPVL YRTKCAKLGK FSSYRSSLSV GSDDELGPIQ RKEVETGTQG TKGDNTTNSY
EADVEDPRKR NILRSLRRTT KKVKPKPRPS LTKATWESNY FGYPLSSVVT SERPIPVFIE
KCVEYIEATG MTTEGIYRVS GNKSEMDSLQ RQFDQDHNLD LVEKDFTVNT VAGALKSFFS
ELPDPLVPYN MQTELVEAYK INDLEQKLQA MKELLKKFPK ENHEIFKYVI SHLNRVSQHH
HVNLMTSENL SICFWPTLMR PDFTTMDALT ATRTYQTIIE LFIHQCPFFF YQRLPVDLPT
PSSPSTPPLT QPSPPQSPPL TPVSPSLSLL PAEHNIL
