RHG10_MOUSE
ID RHG10_MOUSE Reviewed; 786 AA.
AC Q6Y5D8; Q6Y5D6; Q6Y5D7; Q99MT3; Q99MT4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Rho GTPase-activating protein 10;
DE AltName: Full=PH and SH3 domain-containing rhoGAP protein;
DE Short=PS-GAP;
DE Short=PSGAP;
DE AltName: Full=Rho-type GTPase-activating protein 10;
GN Name=Arhgap10;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), FUNCTION, INTERACTION WITH
RP PTK2/FAK1 AND PTK2B/PYK2, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP MUTAGENESIS OF ARG-418.
RC STRAIN=C57BL/10J;
RX PubMed=11238453; DOI=10.1083/jcb.152.5.971;
RA Ren X.-R., Du Q.-S., Huang Y.-Z., Ao S.-Z., Mei L., Xiong W.-C.;
RT "Regulation of CDC42 GTPase by proline-rich tyrosine kinase 2 interacting
RT with PSGAP, a novel pleckstrin homology and Src homology 3 domain
RT containing rhoGAP protein.";
RL J. Cell Biol. 152:971-984(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, INTERACTION
RP WITH PAK2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Heart;
RX PubMed=15471851; DOI=10.1074/jbc.m410530200;
RA Koeppel M.A., McCarthy C.C., Moertl E., Jakobi R.;
RT "Identification and characterization of PS-GAP as a novel regulator of
RT caspase-activated PAK-2.";
RL J. Biol. Chem. 279:53653-53664(2004).
CC -!- FUNCTION: GTPase activator for the small GTPases RhoA and Cdc42 by
CC converting them to an inactive GDP-bound state. Essential for PTKB2
CC regulation of cytoskeletal organization via Rho family GTPases.
CC Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes
CC its localization from the nucleus to the perinuclear region. Stabilizes
CC PAK-2p34 thereby increasing stimulation of cell death.
CC {ECO:0000269|PubMed:11238453, ECO:0000269|PubMed:15471851}.
CC -!- SUBUNIT: Interacts with PKN3 (By similarity). Interacts with caspase-
CC activated PAK2 proteolytic fragment PAK-2p34; the interaction does not
CC affect ARHGAP10 GTPase activation activity towards RHOA and CDC42.
CC Interacts via its SH3 domain with PTK2/FAK1. Interacts with PTK2B/PYK2;
CC the interaction negatively regulates ARHGAP10 GTPase-activating
CC activity. {ECO:0000250, ECO:0000269|PubMed:11238453,
CC ECO:0000269|PubMed:15471851}.
CC -!- INTERACTION:
CC Q6Y5D8; PRO_0000304927 [Q29502]: PAK2; Xeno; NbExp=3; IntAct=EBI-4396535, EBI-4406512;
CC Q6Y5D8-1; PRO_0000304927 [Q29502]: PAK2; Xeno; NbExp=4; IntAct=EBI-4396677, EBI-4406512;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cell
CC membrane. Note=Association to cell membrane is dependent on PH domain.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=PS-GAP-a, PSGAP-m;
CC IsoId=Q6Y5D8-1; Sequence=Displayed;
CC Name=2; Synonyms=PS-GAP-b;
CC IsoId=Q6Y5D8-2; Sequence=VSP_028128;
CC Name=3; Synonyms=PS-GAP-c;
CC IsoId=Q6Y5D8-3; Sequence=VSP_028129;
CC Name=4; Synonyms=PS-GAP-s, PSGAP-s;
CC IsoId=Q6Y5D8-4; Sequence=VSP_028127;
CC -!- TISSUE SPECIFICITY: High levels of expression in brain, testes, liver,
CC heart and kidney. {ECO:0000269|PubMed:15471851}.
CC -!- PTM: Phosphorylated on tyrosine residues, probably involving
CC PTK2B/PYK2.
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DR EMBL; AF297029; AAK18174.1; -; mRNA.
DR EMBL; AF297030; AAK18175.1; -; mRNA.
DR EMBL; AY179965; AAO62072.1; -; mRNA.
DR EMBL; AY179966; AAO62073.1; -; mRNA.
DR EMBL; AY179967; AAO62074.1; -; mRNA.
DR CCDS; CCDS22425.1; -. [Q6Y5D8-1]
DR CCDS; CCDS90420.1; -. [Q6Y5D8-2]
DR CCDS; CCDS90421.1; -. [Q6Y5D8-3]
DR RefSeq; NP_084389.2; NM_030113.2. [Q6Y5D8-1]
DR RefSeq; XP_006531558.1; XM_006531495.3.
DR RefSeq; XP_006531561.1; XM_006531498.3.
DR RefSeq; XP_006531563.1; XM_006531500.2.
DR RefSeq; XP_017168506.1; XM_017313017.1.
DR AlphaFoldDB; Q6Y5D8; -.
DR SMR; Q6Y5D8; -.
DR BioGRID; 219450; 10.
DR IntAct; Q6Y5D8; 1.
DR STRING; 10090.ENSMUSP00000075658; -.
DR iPTMnet; Q6Y5D8; -.
DR PhosphoSitePlus; Q6Y5D8; -.
DR EPD; Q6Y5D8; -.
DR jPOST; Q6Y5D8; -.
DR MaxQB; Q6Y5D8; -.
DR PaxDb; Q6Y5D8; -.
DR PeptideAtlas; Q6Y5D8; -.
DR PRIDE; Q6Y5D8; -.
DR ProteomicsDB; 255259; -. [Q6Y5D8-1]
DR ProteomicsDB; 255260; -. [Q6Y5D8-2]
DR ProteomicsDB; 255261; -. [Q6Y5D8-3]
DR ProteomicsDB; 255262; -. [Q6Y5D8-4]
DR Antibodypedia; 45497; 111 antibodies from 16 providers.
DR DNASU; 78514; -.
DR Ensembl; ENSMUST00000076316; ENSMUSP00000075658; ENSMUSG00000037148. [Q6Y5D8-1]
DR Ensembl; ENSMUST00000210519; ENSMUSP00000147493; ENSMUSG00000037148. [Q6Y5D8-2]
DR Ensembl; ENSMUST00000210922; ENSMUSP00000147485; ENSMUSG00000037148. [Q6Y5D8-3]
DR GeneID; 78514; -.
DR KEGG; mmu:78514; -.
DR UCSC; uc009mhm.1; mouse. [Q6Y5D8-1]
DR UCSC; uc009mhn.1; mouse. [Q6Y5D8-3]
DR UCSC; uc012gge.1; mouse. [Q6Y5D8-2]
DR CTD; 79658; -.
DR MGI; MGI:1925764; Arhgap10.
DR VEuPathDB; HostDB:ENSMUSG00000037148; -.
DR eggNOG; KOG1451; Eukaryota.
DR GeneTree; ENSGT00940000159559; -.
DR HOGENOM; CLU_011532_2_0_1; -.
DR InParanoid; Q6Y5D8; -.
DR OMA; WLNTQSP; -.
DR PhylomeDB; Q6Y5D8; -.
DR TreeFam; TF316851; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 78514; 4 hits in 69 CRISPR screens.
DR ChiTaRS; Arhgap10; mouse.
DR PRO; PR:Q6Y5D8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6Y5D8; protein.
DR Bgee; ENSMUSG00000037148; Expressed in interventricular septum and 129 other tissues.
DR Genevisible; Q6Y5D8; MM.
DR GO; GO:0005829; C:cytosol; IMP:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd12065; SH3_GRAF2; 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; IPR035486; GRAF2.
DR InterPro; IPR035485; GRAF2_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:SF5; PTHR12552:SF5; 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 Alternative splicing; Cell membrane; Cytoplasm; GTPase activation;
KW Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..786
FT /note="Rho GTPase-activating protein 10"
FT /id="PRO_0000304915"
FT DOMAIN 7..262
FT /note="BAR"
FT DOMAIN 265..372
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 389..574
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 728..786
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 584..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11238453"
FT /id="VSP_028127"
FT VAR_SEQ 388..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15471851"
FT /id="VSP_028128"
FT VAR_SEQ 677..727
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15471851"
FT /id="VSP_028129"
FT MUTAGEN 418
FT /note="R->Q: Inactive. Abolishes GTPase activity in vitro.
FT Greatly diminishes cytoskeletal reorganization."
FT /evidence="ECO:0000269|PubMed:11238453"
FT CONFLICT 68
FT /note="K -> E (in Ref. 1; AAK18175)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="G -> D (in Ref. 1; AAK18175)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="M -> V (in Ref. 2; AAO62072)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="K -> E (in Ref. 1; AAK18175/AAK18174)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="E -> G (in Ref. 1; AAK18175/AAK18174)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="M -> T (in Ref. 2; AAO62073)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="E -> R (in Ref. 1; AAK18175/AAK18174)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="A -> S (in Ref. 1; AAK18175/AAK18174)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="L -> S (in Ref. 1; AAK18175/AAK18174)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="F -> V (in Ref. 1; AAK18175/AAK18174)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="A -> T (in Ref. 2; AAO62074)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="A -> T (in Ref. 2; AAO62074)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="H -> R (in Ref. 2; AAO62074)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="S -> N (in Ref. 2; AAO62072/AAO62073/AAO62074)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="T -> A (in Ref. 2; AAO62073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 786 AA; 89366 MW; D55F2E694A153D90 CRC64;
MGLQPLEFSD CYLDSPWFRE RIRAHEAELE RTNKFIKELI KDGKNLISAT KSLSAAQRKF
AHSLRDFKFE FIGDAETDDE RCIDASLREF SNFLKNLEEQ REIMALSVTE TLIKPLEKFR
KEQLGAVKEE KKKFDKETEK NYSLIDKHLT LSARKKDSHL QEADLQVEQN RQHFYELSLE
YVCKLQEIQE RKKFEFVEPM LSFFQGMFTF YHQGHELSKD FNHYKMELQI NIQNTRNRFE
GTRSEVEELM NKIRQNPKDQ KRASQFTAEG YLYVQEKRPA PFGSSWVKHY CMYRKTAKKF
NMIPFEHRSG GKLGDGEAFF LKECTKRHMD STDRRFCFDI EAADRPGVPL TVQAFSEEER
KQWLEALGGK EALFHTFNRA IVPRPEGGAQ LDKMGFTILR KCISAVETRG INDQGLYRVV
GVSSKVQRLL SMLMDVKMCN ELDLENSADW EVKTVTSALK QYLRSLPEPL MTYELHRDFI
VPAKSGSPES RVNAIHFLVH KLPEKNKEML DILVKHLTNV SSHSKQNLMT VANLGVVFGP
TLMRPQEETV AAIMDLKFQN IVVEILIENH EKIFRTSPDT TFAEPTCLSA SPPNAPPRQS
KRQGQRTKRP VAVYNLCLEL EEGDSPSPLK EDPPSSSQDS LSTPSPTTSA AHGPPGLDGN
HLAADGGSCG DATATTPSQT RPSMVQWLNM QSPTTPSSNP AGTPPSPRMS PFPLSPAASI
VDKLPECVIN RKARAVYPCE AEHSSELSFE IGAIFEDVQT SREPGWLEGT LNGKRGLIPQ
NYVKLL
