ID   RHG26_XENLA             Reviewed;         771 AA.
AC   Q5U4T3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Rho GTPase-activating protein 26;
DE   AltName: Full=Rho-type GTPase-activating protein 26;
GN   Name=arhgap26;
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=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase-activating protein for rhoa and cdc42. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with actin
CC       stress fibers and cortical actin structures. {ECO:0000250}.
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DR   EMBL; BC084961; AAH84961.1; -; mRNA.
DR   RefSeq; NP_001088562.1; NM_001095093.1.
DR   AlphaFoldDB; Q5U4T3; -.
DR   SMR; Q5U4T3; -.
DR   PRIDE; Q5U4T3; -.
DR   DNASU; 495439; -.
DR   GeneID; 495439; -.
DR   CTD; 495439; -.
DR   Xenbase; XB-GENE-1011983; arhgap26.L.
DR   OrthoDB; 693048at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 495439; Expressed in testis and 17 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07636; BAR_GRAF; 1.
DR   CDD; cd12064; SH3_GRAF; 1.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR030061; GRAF.
DR   InterPro; IPR035483; GRAF_BAR.
DR   InterPro; IPR035481; GRAF_SH3.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
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; PTHR12552:SF4; PTHR12552:SF4; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cytoplasm; Cytoskeleton; GTPase activation;
KW   Reference proteome; SH3 domain.
FT   CHAIN           1..771
FT                   /note="Rho GTPase-activating protein 26"
FT                   /id="PRO_0000355554"
FT   DOMAIN          265..369
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          383..568
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   DOMAIN          713..771
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          575..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..619
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..695
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  87676 MW;  C914B9AAD84D8789 CRC64;
     MGLPPLEFSD CYLDSPQFRE RLKSHETELD KTNKFIKELI KDGKSLVAAH KSLSFAKRKF
     AGSLNEFKFR CIGDAETDDE ICIARSLQEF AAVLGNLEDE RIRMIDNAGE VLITPLEKFR
     KEQISAAKEV KKKYDKETEK YCGMLEKHMN LSSKKKEVLL HEADVQLDQM RQHFYEVSLE
     YVLKVHEVQE RKMFEFVEPL LAFLQGLFTF YHHGYELAKD FSDFKTQLSI SIQNTRDRFE
     GTRSEVESLM KKMKENPHEH LALSPFTMEG YLYVQEKRHF GTSWVKHYCT YQRETKQMTM
     VPFDQKSGGK VGEEELVQLK SCIRRKTESI EKRFCFDVEG VDRPTVLTMQ ALSEEDRKLW
     MEAMDGREPV YNSNKDSQSE GTAQLDNIGF SIIRKCIQAI ETRGINEQGL YRIVGVNSRV
     QKLLNILMDP KISPETETEI PSEWEIKTIT SSLKTYLRML PGPLMTYQFQ RSFIKAAKQE
     SQESRIKEIH CLIHRLPEKN RQMLHLLMTH LANVAAHHKQ NLMTVANLGV VFGPTLLRPQ
     EETVAAIMDI KFQNIVVEII IENYEEMFST VPEMPQTNSQ LHLSRKRSTD SKPPSCSERP
     LTLFHTSHSS EKEEKRNSVN SSAESVSSSN ANSSVNSTCT QRSNMNNLNA SDPDLDVAKV
     SRPNSLLNPK NISGLLPSSL NPSPTSPPTC PMVSAPSSPM PTSSTSSDSS PVSVPRKAKA
     LYACKAEHDS ELSFSAGTVF ENVCPSQEPG WLEGTLNGKT GLIPENYVEF L