ID E9QAQ3_MOUSE Unreviewed; 759 AA.
AC E9QAQ3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Rho GTPase-activating protein 26 {ECO:0000256|ARBA:ARBA00020525};
DE AltName: Full=Rho-type GTPase-activating protein 26 {ECO:0000256|ARBA:ARBA00032211};
GN Name=Arhgap26 {ECO:0000313|Ensembl:ENSMUSP00000122371.2,
GN ECO:0000313|MGI:MGI:1918552};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000122371.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000122371.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122371.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000122371.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122371.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004608}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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DR RefSeq; XP_006526331.1; XM_006526268.3.
DR AlphaFoldDB; E9QAQ3; -.
DR SMR; E9QAQ3; -.
DR MaxQB; E9QAQ3; -.
DR ProteomicsDB; 349319; -.
DR Antibodypedia; 27437; 285 antibodies from 33 providers.
DR DNASU; 71302; -.
DR Ensembl; ENSMUST00000155576.8; ENSMUSP00000122371.2; ENSMUSG00000036452.19.
DR AGR; MGI:1918552; -.
DR MGI; MGI:1918552; Arhgap26.
DR VEuPathDB; HostDB:ENSMUSG00000036452; -.
DR GeneTree; ENSGT00940000157254; -.
DR HOGENOM; CLU_011532_2_0_1; -.
DR OrthoDB; 5395569at2759; -.
DR BioGRID-ORCS; 71302; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Arhgap26; mouse.
DR Proteomes; UP000000589; Chromosome 18.
DR Bgee; ENSMUSG00000036452; Expressed in interventricular septum and 210 other cell types or tissues.
DR ExpressionAtlas; E9QAQ3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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: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 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Proteomics identification {ECO:0007829|EPD:E9QAQ3,
KW ECO:0007829|MaxQB:E9QAQ3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 265..369
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 383..568
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 701..759
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 584..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..682
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 85952 MW; AC17F55C198C4728 CRC64;
MGLPALEFSD CCLDSPHFRE TLKSHEAELD KTNKFIKELI KDGKSLISAL KNLSSAKRKF
ADSLNEFKFQ CIGDAETDDE MCIARSLQEF AAVLRNLEDE RSRMIENASE VLITPLEKFR
KEQIGAAREA KKKYDKETEK YCGTLEKHLN LSSKKKESQL QEADSQVDLV RQHFYEVSLE
YVFKVQEVQE RKMFEFVEPL LAFLQGLFTF YHHGYELAKD FGDFKTQLTI SIQNTRNRFE
GTRSEVESLM KKMKENPLEH KTISPYTMEG YLYVQEKRHF GTSWVKHYCT YQRDSKQITM
VPFDQKSGGK GGEDESVTLK SCTRRKTDSI EKRFCFDVEA VDRPGVITMQ ALSEEDRRLW
MEAMDGREPV YNSNRDSQSE GTAQLDSIGF SIIRKCIHAV ETRGINEQGL YRIVGVNSRV
QKLLSVLMDP KAASETETDI CAEWEIKTVT SALKTYLRML PGPLMMYQFQ RSFIKAAKLE
NQETRVSEIH SLVHRLPEKN RQMLQLLMNH LANVANNHKQ NLMTVANLGV VFGPTLLRPQ
EETVAAIMDI KFQNIVIEIL IENHEKIFNT VPDVPLTNAQ LHLSRKKSSD SKPPSCSKRP
LTLFHAVPST EKQEQRNSII NSSLESVSSS ANSILNSSSS LQPNLNSSDS NLDVVKPSRP
SSLPPNPSPT SPLSPSWPMF SAPSSPMPTS STSSDSSPIS TPFRKAKALY ACQAEHDSEL
SFTAGTVFDN VHPSQEPGWL EGTLNGKTGL IPENYVEFL
//
