ID RHG12_MACFA Reviewed; 847 AA.
AC Q9BE31;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE RecName: Full=Rho GTPase-activating protein 12;
DE AltName: Full=Rho-type GTPase-activating protein 12;
GN Name=ARHGAP12; ORFNames=QflA-11329;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
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DR EMBL; AB060206; BAB41146.1; -; mRNA.
DR RefSeq; NP_001306290.1; NM_001319361.1.
DR AlphaFoldDB; Q9BE31; -.
DR SMR; Q9BE31; -.
DR STRING; 9541.ENSMFAP00000034105; -.
DR eggNOG; KOG1450; Eukaryota.
DR OrthoDB; 5395569at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
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 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 2: Evidence at transcript level;
KW GTPase activation; Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..847
FT /note="Rho GTPase-activating protein 12"
FT /id="PRO_0000056714"
FT DOMAIN 12..74
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 265..298
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 358..391
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 463..575
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 657..845
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 110..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 243
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWW6"
SQ SEQUENCE 847 AA; 96275 MW; C089AC2E03793762 CRC64;
MKMADRSGKI IPGQAYIEVE YDYEYEAKDR KIVIKQGERY ILVKKTNDDW WQVKPDENSK
AFYVPAQYVK EVTRKALMPP VKQVAGLPNN STKIMQSLHL QRSTENVNKL PELSSFGKPS
SSVQGTGLTR DANQNFGPSY NPGHTVNLSL DLTHNNGKFN NDSHSPKVSS QNRTRLFGHF
PGPEFLDVEK TSFSQEQSCD SAGEGSERIH QDSESGDELS SSSTEQIRAT TPPNQGRPDS
PVYANLQELK ISQSALPPLP GSPAIQINGE WETHKDSSGR CYYYDRGTQE RTWKPPRWTR
DASISKGDFQ SPGDQELLSS EENYYSTSYS QSDSQCGSPP RGWSEELDER GHTLYTSDYT
NEKWLKHIDD QGRQYYYSAD GSRSEWELPK YNASSQQQRE IIKSRSLDRR LQEPIVLTKW
RHSTIVLDTN DKESPTASKP CFPENESSPS SPKHQDTASS PKDQEKYGLL NVTKIAENGK
KVRKNWLSSW AVLQGSSLLF TKTQGSSTSW FGSNQSKPEF TVDLKGATIE MASKDKSSKK
NVFELKTRQG TELLIQSDND TVINDWFKVL SSTINNQAVD TDEGIEEEIL PDSPGIEKHD
KEKEQKDPKK LRSFKVSSID SSEQKKTKKN LKKFLTRRPT LQAVREKGYI KDQVFGSNLA
NLCQRENGTV PKFVKLCIEH VEEYGLDVDG IYRVSGNLAV IQKLRFAVNH DEKLDLNDSK
WEDIHVITGA LKMFFRELPE PLFTFNHFND FVNAIKQEPR QRVAAVKDLI RQLPKPNQDT
MQILFRHLKR VVENGEKNRM TYQSIAIVFG PTLLKPEKET GNIAVHTVYQ NQIVELILLE
LSSIFGR
//
