RHG10_BOVIN
ID RHG10_BOVIN Reviewed; 785 AA.
AC Q08DP6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Rho GTPase-activating protein 10;
DE AltName: Full=Rho-type GTPase-activating protein 10;
GN Name=ARHGAP10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PKN3. Interacts with caspase-activated PAK2
CC proteolytic fragment PAK-2p34; the interaction does not affect ARHGAP10
CC GTPase activation activity towards RHOA and CDC42. Interacts via its
CC SH3 domain with PTK2/FAK1. Interacts with PTK2B/PYK2; the interaction
CC negatively regulates ARHGAP10 GTPase-activating activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Association to
CC cell membrane is dependent on PH domain. {ECO:0000250}.
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DR EMBL; BC123631; AAI23632.1; -; mRNA.
DR RefSeq; NP_001070298.1; NM_001076830.1.
DR AlphaFoldDB; Q08DP6; -.
DR BMRB; Q08DP6; -.
DR SMR; Q08DP6; -.
DR STRING; 9913.ENSBTAP00000003283; -.
DR PaxDb; Q08DP6; -.
DR PRIDE; Q08DP6; -.
DR Ensembl; ENSBTAT00000003283; ENSBTAP00000003283; ENSBTAG00000002531.
DR GeneID; 510704; -.
DR KEGG; bta:510704; -.
DR CTD; 79658; -.
DR VEuPathDB; HostDB:ENSBTAG00000002531; -.
DR VGNC; VGNC:26074; ARHGAP10.
DR eggNOG; KOG1451; Eukaryota.
DR GeneTree; ENSGT00940000159559; -.
DR HOGENOM; CLU_011532_2_0_1; -.
DR InParanoid; Q08DP6; -.
DR OMA; WLNTQSP; -.
DR OrthoDB; 693048at2759; -.
DR TreeFam; TF316851; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000002531; Expressed in myometrium and 106 other tissues.
DR ExpressionAtlas; Q08DP6; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; GTPase activation; Membrane; Reference proteome;
KW SH3 domain.
FT CHAIN 1..785
FT /note="Rho GTPase-activating protein 10"
FT /id="PRO_0000304913"
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 727..785
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 576..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 89405 MW; 7BDC5026C05096DD CRC64;
MGLQPLEFSD CYLDSPWFRE RIRAHEAELE RTNKFIKELI KDGKNLIAAT KTLSAAQRKF
AHSLRDFKFE FIGDAETDDE RCIDASLREF SNFLKNLEEQ REIMALSVTE TLIKPLEKFR
KEQLGAVKEE KKKFDKETER NYSLIDKHLN LSAKKKDSHL QEADIQVEQN RQHFYELSLE
YVCKLQEIQE RKKFEFVEPM LSFFQGMFTF YHQGHELAKD FNHYKMELQI NIQNTRNRFE
GTRSEVEELM NKIRQNPKDH KRASQFTAEG YLYVQEKRPP PFGSSWVKHY CMYRKAAKKF
TMIPFEHRSG GKLGDGEVFF LKECIRRHTD SIDRRFCFDV EAADRPGISL TMQAFSEEER
KQWLEVLGGK EALFPSFNRA IIPRPEGSAQ LDKMGFTILR KCIRAVETRG INDQGLYRVV
GVSSKVQRLL SMLMDVKTCN EVDLENSVDW EVKTITSALK QYLRSLPEPL MTYELHGDFI
VPAKSGSPES RVNAIHFLVH KLPEKNKEML DILVKHLTNV SNHSKQNLMT VANLGVVFGP
TLMRPQEETV AAIMDLKFQN IVVEILIENH EKIFRTPPDA TLPEPGPLSA PPNAPPRQSK
RQGQRTKRPV AVYNLCLELE DGDRPSLPKE DTPPSSLDSL SSPSPTTATA LGHPGPDRNH
LLTDGGSFGD WAPTAPSQAR SSAVQWLNPQ SPTTPSCSPA VTPPSPKLPP VPLSLPATVA
DKPPESIISR KARAVYPCEA EHSSELSFEI GAIFEDVQTS REPGWLEGTL NGKRGLIPQN
YVKLL
