ID   RHG32_XENLA             Reviewed;        1940 AA.
AC   Q6GPD0;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Rho GTPase-activating protein 32;
DE   AltName: Full=Rho-type GTPase-activating protein 32;
DE   AltName: Full=Rho/Cdc42/Rac GTPase-activating protein RICS;
GN   Name=arhgap32; Synonyms=rics;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis on
CC       RHOA, CDC42 and RAC1 small GTPases. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC       Cell membrane {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal PX domain interacts specifically with
CC       phosphatidylinositides. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PX domain-containing GAP family.
CC       {ECO:0000305}.
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DR   EMBL; BC073211; AAH73211.1; -; mRNA.
DR   RefSeq; NP_001085694.1; NM_001092225.1.
DR   AlphaFoldDB; Q6GPD0; -.
DR   SMR; Q6GPD0; -.
DR   GeneID; 444120; -.
DR   KEGG; xla:444120; -.
DR   CTD; 444120; -.
DR   Xenbase; XB-GENE-1002479; arhgap32.L.
DR   OrthoDB; 1300981at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 444120; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:1901981; F:phosphatidylinositol phosphate binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07298; PX_RICS; 1.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR042139; PX_ARHGAP32.
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   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF07653; SH3_2; 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   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; GTPase activation; Membrane; Reference proteome;
KW   SH3 domain.
FT   CHAIN           1..1940
FT                   /note="Rho GTPase-activating protein 32"
FT                   /id="PRO_0000345205"
FT   DOMAIN          154..248
FT                   /note="PX; atypical"
FT   DOMAIN          262..324
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          375..570
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          646..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1219..1264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1430..1454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1675..1786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1035..1064
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1142..1163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1721..1737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1738..1752
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1940 AA;  216024 MW;  7E3BCF52E0D00D33 CRC64;
     MEGGTDAAAF AAFPSIHAVP STSGRMVTGS KLDELERIMK SSLHLEEDDF VPELPRSIHP
     RERPDWEETI SAMARGADIT VPGEIQIPAE LPLRSCGSTA SMKVKNVKKL SFTKGHFPKL
     AECAHFHYEN VDFGSIQLTL TEDQNEVNRN GCESKELVFL VQIACQGRSW IVKRSYEDFR
     VLDKHLHLCI YDRRFSQLSE LPRSDSVKDN PELVTQMLMA YLSRLSAIAG NKINCGPALT
     WMEIDNKGNH LLVHEESSIN VPAIAAAHVI KRYNAQAPDE LSFEVGDIVS VIDMPPKELT
     TWWRGKHGFQ VGFFPSECVE LINDKVPQSM TNSVPKPVSR KHGKLITFLR TFMKSRPSKQ
     KLKQRGILRE RVFGCDLGEH LLNSGQDVPQ VLRSCTEFIE KHGVVDGIYR LSGIASNIQK
     LRHEFDSEQI PDLTKDVYIQ DIHCVGSLCK LYFRELPNPL LTYQLYEKFS DAVSAASDEE
     RLVKIHDVIQ QLPPPHYRTL EFLMRHLSRL ATYCSITNMH TKNLAIVWAP NLLRSKQIES
     ACFSGTAAFM EVRIQSVVVE FILNHVEVLF SAKLSSVIRE GAGHTSLSRP KSLLVSSPST
     KLLSLEEAQA RTQAQINSPV VGDSRYIEVG EGPAALQGRF HTVIDFPSER KRPPSKMKKS
     PVGSWRSFFN IGKSSSSSSM SKRKLQRNPS EPLEMKSMAF AGGRDSSAMR SAKSEESLSS
     LHAADGESKL FRPRRPRSSS DALSASYNGD LLDSCNRCNS YDNLPRDHDS DGDEGLIHVP
     AMLSGRSPED EDLSPPDIGM ATLDFDPMSF QCSPHQLDSE GPDNFFQLDI FASNGKDKLQ
     SGTQNPGSVT GCEPLSPFQD KVISPFLSPD RSPSTDKVSK TASFAEKFVQ ALSPKMGRKA
     VRSPPLTISD PVSISLPSRV SEMIGSMPGN SAASQSIIWN RESSTNSRES ETYYGCKLVD
     ANLSSSSATA DPWSTVTPVI TCNQDGREDK AGIFTHGFPQ PLESSDLEYI ENYNLELGTT
     NVAAAYQNDD TELSRANQNK AHPPNSPQGA SASESPQELS HVSSVSIIPP PPPPKNPARM
     LALALAESAQ QASANKKPSF MQFMDLPPPP SVPEDKPLLE FSPKMSPEPL RSGPATPAAS
     PPVISRKTSP ATPPSTTSSF SVTTIHHSPV KNYNPLAGQM PTAVTPGLSP SSNQVFASVP
     DMLHSETIKM NSIIPSEAFT TGIPVTPPTE KTKESSRAPH LHQRSESFPS HPAYSTAKPT
     PPVRTMDSRL ATAMHSNFND SITANNYHSF LNTMMLPSSL EDALPRHNYS PHLKTGNIDE
     EGVNYRQTYL SHNKQDDPAD LGDLYRQPYI SPGKSENAEI GNAYRHPYPS NTESESLKEP
     LEPFLHHKPA VAPKTYRAET LLPHIPPQVY GSRCDTPSSA FYGTYINQAK HPRSRNKPDY
     MPSMSPGVRS YTEDTSSYPT IRRVQSLHVP MQTLPPPIRT VPISRTEVPP DDDPAYCPRP
     LYQYKQCPPF NSQSDYHVTQ LQPYFENGRV HYRYSPYSGG PTYFSSDSNF YDMDPYGTLR
     LRQLPLYPSR DFASYTTRLQ PKATYRSQGL PPYPRGTLRE HNFISRDVPP ALPPEHPRPL
     HISWDMEDMD RYRLQSLRRE NKARQRAKGP VMSQYDNVTP SLVEDVAGLD VIHLRSRSDP
     GKTPGLLSVA ETKDVRYPGR TEGDERTTYP PPVFGNGHQD KPSLPQKQSG SSRSRMQHDI
     STEQHSQDTL HRQPSEGRNG PPIPPVDYNA KGMPNPPDPT SYHSSANKYN LTQQEPMRLN
     HKELRLTEDI ERSHTRPADN QHRDCYREEQ AQFASVVPPP KPERSHSLRA HNPAVLERDP
     SIFYPYQTLH AKRQSTINTV SQYDNLSDYH SIPHHRTTNQ STPNAFPLPH GRTYSTALGQ
     GAFLAAELAL QRPETKIHVE