ID F7H4E1_CALJA Unreviewed; 843 AA.
AC F7H4E1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Rho GTPase activating protein 12 {ECO:0000313|Ensembl:ENSCJAP00000050138.3};
GN Name=ARHGAP12 {ECO:0000313|Ensembl:ENSCJAP00000050138.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000050138.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000050138.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000050138.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; F7H4E1; -.
DR STRING; 9483.ENSCJAP00000050138; -.
DR Ensembl; ENSCJAT00000062280.4; ENSCJAP00000050138.3; ENSCJAG00000013435.5.
DR GeneTree; ENSGT00950000182860; -.
DR HOGENOM; CLU_644892_0_0_1; -.
DR InParanoid; F7H4E1; -.
DR Proteomes; UP000008225; Chromosome 7.
DR Bgee; ENSCJAG00000013435; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13233; PH_ARHGAP9-like; 1.
DR CDD; cd04403; RhoGAP_ARHGAP27_15_12_9; 1.
DR CDD; cd12070; SH3_ARHGAP12; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035491; ARHGAP12_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 InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR23176:SF107; RHO GTPASE-ACTIVATING PROTEIN 12; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16618; SH3-WW_linker; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 12..74
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 262..295
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 361..388
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 460..572
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 653..841
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 152..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 95827 MW; 1F43168B5766A26E CRC64;
VKMADRSGKI IPGQVYIEVE YDYEYEAKDR KIVIKQGERY ILVKKTNDDW WQVKPDENSK
AFYVPAQYVK EVTRKALMPP VKQVAGLPNN STKIMQSLHL QRSTENVNKL PELSSFGKPS
SSVQGTGLIR DANQNFGPSY NPGQTLNLSL DLTHNNGKFN NDSHSPKVSS QNRTRLFPGP
EFLDIEKTSF SQEQSCDSAG EGSERIHQDS ESGDELSSSS TEQIRATTPP NQGRPDSPVY
ANLQELKISQ SALPPLPGSP AIQINGEWET HKDSSGRCYY YNRGTQERTW KPPRWTRDAS
ISKGDFQSPG DQELLSSEEN YYSTCYSQSD SQCGSPPKGW SEELDERGHT LYTSDYTNEK
WLKHVDDQGR QYYYSADGSR SEWELPKYNA SSQQQREIIK SRSLDRRLQE PIVLTKWRHS
TIVLDTNDKE SPTASKPCLP ENESSPSSPK HQDTASSPKD QEKYGLLNVT KIAENGKKVR
KNWLSSWAVL QGSSLLFTKT QGSSTSWFGS NQSKPEFTVD LKGATIEMAS KDKSSKKNVF
ELKTRQGTEL LIQSDNDTVI NDWFKVLSST INNQAVETDE GIEEEIPDSP GIEKHDKEKE
QKDPKKLRSL KVSTIDSSEQ KKTKKNLKKF LTRRPTLQAV REKGYIKDQV FGSNLANLCQ
RENGTVPKFV KLCIEHVEEH GLDVDGIYRV SGNLAVIQKL RFAVNHDEKL DLNDSKWEDI
HVITGALKMF FRELPEPLFT FNHFNDFVNA IKQEPRQRVT AVKDLIRQLP KPNQDTMQIL
FRHLRRVIEN GEKNRMTYQS IAIVFGPTLL KPEKETGNIA VHTVYQNQIV ELILLELSSI
FGR
//
