ARHGP_RAT
ID ARHGP_RAT Reviewed; 579 AA.
AC Q6P720;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Rho guanine nucleotide exchange factor 25;
DE AltName: Full=Guanine nucleotide exchange factor GEFT;
DE AltName: Full=Rac/Cdc42/Rho exchange factor GEFT;
DE AltName: Full=RhoA/Rac/Cdc42 guanine nucleotide exchange factor GEFT;
GN Name=Arhgef25; Synonyms=Geft;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play a role in actin cytoskeleton reorganization in
CC different tissues since its activation induces formation of actin
CC stress fibers. It works as a guanine nucleotide exchange factor for Rho
CC family of small GTPases. Links specifically G alpha q/11-coupled
CC receptors to RHOA activation. May be an important regulator of
CC processes involved in axon and dendrite formation. In neurons seems to
CC be an exchange factor primarily for RAC1. Involved in skeletal
CC myogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with activated GNAQ and GNA11. Interacts with RHOA,
CC CDC42 and RAC1. Interacts (via the DH domain) with BVES (via the C-
CC terminus cytoplasmic tail) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000250}.
CC Cell membrane {ECO:0000250}. Note=Highly colocalizes with actin
CC regions. {ECO:0000250}.
CC -!- DOMAIN: The guanine nucleotide exchange activity is autoinhibited by
CC the PH domain. {ECO:0000250}.
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DR EMBL; BC061879; AAH61879.1; -; mRNA.
DR RefSeq; NP_955427.1; NM_199395.1.
DR AlphaFoldDB; Q6P720; -.
DR SMR; Q6P720; -.
DR BioGRID; 260857; 1.
DR STRING; 10116.ENSRNOP00000006800; -.
DR iPTMnet; Q6P720; -.
DR PhosphoSitePlus; Q6P720; -.
DR jPOST; Q6P720; -.
DR PaxDb; Q6P720; -.
DR PRIDE; Q6P720; -.
DR GeneID; 314904; -.
DR KEGG; rno:314904; -.
DR UCSC; RGD:735210; rat.
DR CTD; 115557; -.
DR RGD; 735210; Arhgef25.
DR VEuPathDB; HostDB:ENSRNOG00000005034; -.
DR eggNOG; KOG0689; Eukaryota.
DR HOGENOM; CLU_001356_6_0_1; -.
DR InParanoid; Q6P720; -.
DR OMA; HAVEVMC; -.
DR OrthoDB; 301115at2759; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q6P720; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000005034; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q6P720; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR030738; ARHGEF25.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR22826:SF117; PTHR22826:SF117; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW Reference proteome.
FT CHAIN 1..579
FT /note="Rho guanine nucleotide exchange factor 25"
FT /id="PRO_0000322134"
FT DOMAIN 199..375
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 380..499
FT /note="PH"
FT REGION 27..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..338
FT /note="Important for binding to Rho GTPases"
FT /evidence="ECO:0000250"
FT REGION 472..498
FT /note="Sufficient to bind activated GNAQ"
FT /evidence="ECO:0000250"
FT REGION 487..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 64160 MW; 4710EBEC3E1B84E3 CRC64;
MKPPDRPTPG RTDRILGVMG GMLRACAVPG QEGPQERDPL GPGSTKTESE CTEEDQTGER
EREVLAWAPQ PESYSIAGSE GSMSASAVSG LAALSGPSSG LSSHPCSPVP PGPVTGLRRW
LDHSKHCLSV ETEADSGQTR QCENWMLEPT LTTGQELPEL TLLTTLLEGP GVKAQPAEEE
TLSQAPKNEE EQKKTALERS MFVLSELVET ERMYVDDLGQ IVEGYMATMA TQGVPESLRG
RDRIVFGNIQ QIYEWHRDYF LQELQQCLKD PDWLAQLFIK HERRLHMYVV YCQNKPKSEH
VLSEFGDSYF EELRQQLGHR LQLSDLLIKP VQRIMKYQLL LKDFLKYYRR AGMDTEELEQ
AVEVMCFVPK RCNDMMSLGR LRGFEGKLTA QGKLLGQDTF LVTEPEAGGL LSSRGRERRV
FLFEQIVIFS EALGGGGRGG TQPGYVYKNS IKASDPAVSQ AWIKQVAQIL ESQRDFLNAL
QSPIEYQRRE SQTNSLGRSG GPGVGSPGRM AQVSMHTPIN GSLPSLLLLP RGEVPRAPLP
LDTQALSETP LTPYDPPALP TVNSPPGQAR LAKLDEDEL
