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 27-MAR-2024, entry version 99.
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 (By similarity).
CC May be involved in the regulation of neosynthesized protein export
CC through a Rab-endososomal dependent export route (By similarity).
CC {ECO:0000250|UniProtKB:Q5ZMW5, ECO:0000250|UniProtKB:Q9UNA1}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9UNA1}. Note=Colocalizes with actin stress
CC 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 DNASU; 495439; -.
DR AGR; Xenbase:XB-GENE-1011983; -.
DR Xenbase; XB-GENE-1011983; arhgap26.L.
DR OrthoDB; 5395569at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 495439; Expressed in testis and 17 other cell types or tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01249; BAR-PH_GRAF_family; 1.
DR CDD; cd07636; BAR_GRAF; 1.
DR CDD; cd04374; RhoGAP_Graf; 1.
DR CDD; cd12064; SH3_GRAF; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035483; GRAF_BAR.
DR InterPro; IPR047234; GRAF_fam.
DR InterPro; IPR035481; GRAF_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR047225; PH_GRAF.
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; OLIGOPHRENIN 1; 1.
DR PANTHER; PTHR12552:SF4; RHO GTPASE-ACTIVATING PROTEIN 26; 1.
DR Pfam; PF16746; BAR_3; 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; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 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; Endosome; GTPase activation;
KW Membrane; Reference proteome; SH3 domain.
FT CHAIN 1..771
FT /note="Rho GTPase-activating protein 26"
FT /id="PRO_0000355554"
FT DOMAIN 7..262
FT /note="BAR"
FT /evidence="ECO:0000250|UniProtKB:A1A4S6"
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
//
