RHG26_CHICK
ID RHG26_CHICK Reviewed; 760 AA.
AC Q5ZMW5; Q98935;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Rho GTPase-activating protein 26;
DE AltName: Full=GTPase regulator associated with focal adhesion kinase;
DE AltName: Full=Rho-type GTPase-activating protein 26;
GN Name=ARHGAP26; Synonyms=GRAF;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 177-760, FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH PTK2/FAK1, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=8649427; DOI=10.1128/mcb.16.6.3169;
RA Hildebrand J.D., Taylor J.M., Parsons J.T.;
RT "An SH3 domain-containing GTPase-activating protein for Rho and Cdc42
RT associates with focal adhesion kinase.";
RL Mol. Cell. Biol. 16:3169-3178(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 161-391, AND FUNCTION.
RX PubMed=10982819; DOI=10.1074/jbc.m007574200;
RA Longenecker K.L., Zhang B., Derewenda U., Sheffield P.J., Dauter Z.,
RA Parsons J.T., Zheng Y., Derewenda Z.S.;
RT "Structure of the BH domain from Graf and its implications for Rho GTPase
RT recognition.";
RL J. Biol. Chem. 275:38605-38610(2000).
CC -!- FUNCTION: GTPase-activating protein for RHOA and CDC42.
CC {ECO:0000269|PubMed:10982819, ECO:0000269|PubMed:8649427}.
CC -!- SUBUNIT: Binds to the C-terminus of PTK2/FAK1.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:8649427}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8649427}. Note=Colocalizes with actin stress fibers
CC and cortical actin structures.
CC -!- TISSUE SPECIFICITY: Detected in embryonic brain and liver, and at low
CC levels in embryonic eye, heart, lung, intestine and skeletal muscle.
CC {ECO:0000269|PubMed:8649427}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB07998.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ719269; CAG30928.1; -; mRNA.
DR EMBL; U36309; AAB07998.1; ALT_INIT; mRNA.
DR RefSeq; NP_990525.2; NM_205194.2.
DR PDB; 1F7C; X-ray; 2.40 A; A=353-583.
DR PDBsum; 1F7C; -.
DR AlphaFoldDB; Q5ZMW5; -.
DR SMR; Q5ZMW5; -.
DR STRING; 9031.ENSGALP00000011921; -.
DR iPTMnet; Q5ZMW5; -.
DR PaxDb; Q5ZMW5; -.
DR Ensembl; ENSGALT00000070058; ENSGALP00000046116; ENSGALG00000033938.
DR GeneID; 396113; -.
DR KEGG; gga:396113; -.
DR CTD; 23092; -.
DR VEuPathDB; HostDB:geneid_396113; -.
DR eggNOG; KOG1451; Eukaryota.
DR GeneTree; ENSGT00940000157254; -.
DR HOGENOM; CLU_011532_2_0_1; -.
DR InParanoid; Q5ZMW5; -.
DR OMA; LAXIFNT; -.
DR OrthoDB; 693048at2759; -.
DR PhylomeDB; Q5ZMW5; -.
DR Reactome; R-GGA-8980692; RHOA GTPase cycle.
DR Reactome; R-GGA-9013026; RHOB GTPase cycle.
DR Reactome; R-GGA-9013106; RHOC GTPase cycle.
DR Reactome; R-GGA-9013148; CDC42 GTPase cycle.
DR Reactome; R-GGA-9013149; RAC1 GTPase cycle.
DR Reactome; R-GGA-9013404; RAC2 GTPase cycle.
DR Reactome; R-GGA-9013405; RHOD GTPase cycle.
DR Reactome; R-GGA-9013406; RHOQ GTPase cycle.
DR Reactome; R-GGA-9013409; RHOJ GTPase cycle.
DR Reactome; R-GGA-9013423; RAC3 GTPase cycle.
DR EvolutionaryTrace; Q5ZMW5; -.
DR PRO; PR:Q5ZMW5; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000033938; Expressed in granulocyte and 14 other tissues.
DR ExpressionAtlas; Q5ZMW5; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
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; 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; 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 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cytoplasm; Cytoskeleton; GTPase activation;
KW Reference proteome; SH3 domain.
FT CHAIN 1..760
FT /note="Rho GTPase-activating protein 26"
FT /id="PRO_0000355552"
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 702..760
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 571..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 196
FT /note="F -> S (in Ref. 1; CAG30928)"
FT /evidence="ECO:0000305"
FT HELIX 387..403
FT /evidence="ECO:0007829|PDB:1F7C"
FT TURN 408..412
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 446..458
FT /evidence="ECO:0007829|PDB:1F7C"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 467..477
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 482..493
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 498..516
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 525..536
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 550..562
FT /evidence="ECO:0007829|PDB:1F7C"
FT HELIX 564..569
FT /evidence="ECO:0007829|PDB:1F7C"
SQ SEQUENCE 760 AA; 86524 MW; DE3E2F3D4ED56667 CRC64;
MGLPALEFSE CCLDSPQFRE RLRSHEAELE KTNKFIKELI KDGKSLIAAL KNLSSAKRKF
ADSLNEFKFR CIGDAETDDE ICIAKSLQEF ATVLRNLEDE RMRMIENASE VLITPLEKFR
KEQIGAAKDA KKKYDKETEK YCGVLEKHLN LSSKKKESQL QEADSQVDLV RQHFYEVSLE
YVFKVQEVQE RKMFEFVEPL LAFLQGLFTF YHHGYELAKD FSDFKTELTI SIQNTRNRFE
GTRSEVESLM KKMKENPHEH KNISPYTMEG YLYVQEKRHF GTSWVKHYCT YQRESKRITM
VPFDQKSGGK GGEDEAVILK SCTRRKTDSI EKRFCFDVEA VDRPGVITMQ ALSEEDRRLW
MEAMDGREPV YNSNKDNQSE GTAQLDSIGF SIIKKCIHAV ETRGINEQGL YRIVGVNSRV
QKLLSILMDP KTATETETEI CAEWEIKTIT SALKTYLRML PGPLMMYQFQ RSFIKAAKLE
NQESRVSEIH SLVHRLPEKN RQMLHLLMNH LAKVADNHKQ NLMTVANLGV VFGPTLLRPQ
EETVAAIMDI KFQNIVIEIL IENHEKIFNT VPETPPSNSQ LLLSRKKSTD SKPPSCSERP
LTLFHTAQPN EKQESRNSII NSSLESVISS NANSFLNSNS APQSNLNSSD LELEVIKPNR
PNSLPQNPSP TSPLSPSWPM FSAPSSPMPT SSTSSDSSPI SSPLRKARAL YACKAEHDSE
LSFTAGTVFD NVHPSQEPGW LEGTLNGKTG LIPENYVEFL
