ID G1T1Q8_RABIT Unreviewed; 814 AA.
AC G1T1Q8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 85.
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:ENSOCUP00000010033.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000010033.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000010033.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000010033.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000010033.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000010033.3};
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 EMBL; AAGW02027616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02027617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02027618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02027619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02027620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02027621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02027622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02027623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02027624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02027625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008253380.1; XM_008255158.2.
DR AlphaFoldDB; G1T1Q8; -.
DR SMR; G1T1Q8; -.
DR STRING; 9986.ENSOCUP00000010033; -.
DR PaxDb; 9986-ENSOCUP00000010033; -.
DR Ensembl; ENSOCUT00000011670.3; ENSOCUP00000010033.3; ENSOCUG00000011665.4.
DR eggNOG; KOG1451; Eukaryota.
DR GeneTree; ENSGT00940000157254; -.
DR HOGENOM; CLU_011532_2_0_1; -.
DR InParanoid; G1T1Q8; -.
DR OrthoDB; 5395569at2759; -.
DR TreeFam; TF316851; -.
DR Proteomes; UP000001811; Chromosome 3.
DR Bgee; ENSOCUG00000011665; Expressed in frontal cortex and 16 other cell types or tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
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 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
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 756..814
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 630..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..651
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"
SQ SEQUENCE 814 AA; 92177 MW; DC93CC160A3F56A6 CRC64;
MGLPALEFSD CCLDSPHFRE TLKSHEAELD KTNKFIKELI KDGKSLISAL KNLSTAKRKF
ADSLNEFKFQ CIGDAETDDE MCIARSLQEF ATVLRNLEDE RIRMIENASE VLITPLEKFR
KEQIGAAKEA KKKYDKETEK YCGVLEKHLN LSSKKKESQL QEADSQVDLV RQHFYEVSLE
YVFKVQEVQE RKMFEFVEPL LAFLQGLFTF YHHGYELAKD FGDFKTQLTI SIQNTRNRFE
GTRSEVESLM RKMKENPLEH KTISPYTMEG YLYVQEKRHF GTSWVKHYCT YQRDSKQISM
VPFDQKSGGK GGEDETITLK SCTRRKTDSI EKRFCFDVEA VDRPGVITMQ ALSEEDRRLW
MEAMDGREPV YNSNKDNQNE GTAQLDSIGF SIIRKCIHAV ETRGINEQGL YRIVGVNSRV
QKLLSVLMDP KTAAETETDI CAEWEIKTIT SALKTYLRML PGPLMMYQFQ RSFIKAAKLE
NQETRVSEIH SLVHRLPEKN RQMLQLLMNH LANVANNHKQ NLMTVANLGV VFGPTLLRPQ
EETVAAIMDI KFQNIVIEIL IENHEKIFNT VPDAPLTGTQ LHLSRKKSGD AKPPSCSERP
LTLFHAVQAT EKQEQRNSIL NSSLESVSSN PNSILNSSSS LQPNTNSSDL DLDVVKPARP
NSLPPNPSPT SPLSPSWPMF SAPSSPMPTS STSSDSSPAR SVAGFVWFSV AAAVLSLAWS
SLHAVFSLLV NFVPCHPNLH LLFDRPEEAV REDFSTPFRK AKALYACKAE HDSELSFAAG
TVFDNDHPSQ EPGWLEGTLN GKTGLIPENY VEFL
//
