ID   RHG15_RAT               Reviewed;         482 AA.
AC   Q6AYC5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Rho GTPase-activating protein 15;
DE   AltName: Full=ArhGAP15;
DE   AltName: Full=Rho-type GTPase-activating protein 15;
GN   Name=Arhgap15;
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=Lung;
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-208 AND SER-250, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC       to an inactive GDP-bound state. Has activity toward RAC1.
CC       Overexpression results in an increase in actin stress fibers and cell
CC       contraction (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The PH domain is required for localization to the membrane.
CC       {ECO:0000250}.
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DR   EMBL; BC079103; AAH79103.1; -; mRNA.
DR   RefSeq; NP_001013939.1; NM_001013917.1.
DR   AlphaFoldDB; Q6AYC5; -.
DR   SMR; Q6AYC5; -.
DR   STRING; 10116.ENSRNOP00000043804; -.
DR   iPTMnet; Q6AYC5; -.
DR   PhosphoSitePlus; Q6AYC5; -.
DR   PaxDb; Q6AYC5; -.
DR   PRIDE; Q6AYC5; -.
DR   Ensembl; ENSRNOT00000049884; ENSRNOP00000043804; ENSRNOG00000031168.
DR   GeneID; 295635; -.
DR   KEGG; rno:295635; -.
DR   UCSC; RGD:1359304; rat.
DR   CTD; 55843; -.
DR   RGD; 1359304; Arhgap15.
DR   eggNOG; KOG1449; Eukaryota.
DR   eggNOG; KOG1450; Eukaryota.
DR   GeneTree; ENSGT00950000182860; -.
DR   HOGENOM; CLU_015883_1_0_1; -.
DR   InParanoid; Q6AYC5; -.
DR   OMA; DHNQWED; -.
DR   OrthoDB; 1300981at2759; -.
DR   PhylomeDB; Q6AYC5; -.
DR   TreeFam; TF329345; -.
DR   Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR   Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR   PRO; PR:Q6AYC5; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000031168; Expressed in thymus and 18 other tissues.
DR   Genevisible; Q6AYC5; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR   GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR   GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
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   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; GTPase activation; Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..482
FT                   /note="Rho GTPase-activating protein 15"
FT                   /id="PRO_0000317576"
FT   DOMAIN          87..198
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          288..477
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53QZ3"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53QZ3"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         250
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   482 AA;  55014 MW;  CC8F711F5B7C58E4 CRC64;
     MEKRTSCSVQ TSTNCDNSLE TLNSAHQATG AVQMRIKNAN SHPDRQSQTK SMILTDAGKV
     TEPISRHRRN HSQHVLKDVI PPLEHPMVEK EGYLQKAKIA DGGKKLRKNW STSWIVLSGR
     KLEFYKDPKQ QALPNVKPRP NAESVDLCGA HIEWAAKDKS SKKSVFQITT ASGNEFLLQS
     DIDFLILDWF HAIKNAIDRL PKNPSFGSLE LFSFQRSSSS EQPSHCHIDR KEQKPENRKS
     FMFRLHHSVS DTSDKNRVKS RLKKFISRRP SLKTLQEKGI IKDQIFGSHL HTVCEREHST
     VPWFVKQCIE AVEKRGLEVD GIYRVSGNLA TIQKLRFIVN QEEKLNLDDS QWEDIHVVTG
     ALKMFFRELS EPLFPYSFFE RFVEAIKKQD SDAKIETMKS LVKSLPPPNH DTMKILFGHL
     TKIVAKAAQN LMSTQSLGIV FGPTLLRAEN ESGNVAVHMV YQNQVAEFML TEYDKIFSSE
     ED