ID A0A2K6NKT3_RHIRO Unreviewed; 1525 AA.
AC A0A2K6NKT3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Rho guanine nucleotide exchange factor 12 {ECO:0000313|Ensembl:ENSRROP00000004874.1};
GN Name=ARHGEF12 {ECO:0000313|Ensembl:ENSRROP00000004874.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000004874.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000004874.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR RefSeq; XP_010355301.1; XM_010356999.1.
DR Ensembl; ENSRROT00000022391.1; ENSRROP00000004874.1; ENSRROG00000019620.1.
DR GeneTree; ENSGT00940000157662; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProt.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd13390; PH_LARG; 1.
DR CDD; cd08754; RGS_LARG; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR037801; ARHGEF12_PH.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR037884; LARG_RGS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR45872:SF3; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 12; 1.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200}.
FT DOMAIN 53..117
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 768..958
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1000..1113
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 231..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1525 AA; 171022 MW; F87A90FE12038D79 CRC64;
MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERIA SHDFDPTGLV QRCVVIQKDD
NGFGLTVSGD NPVFVQSVKE DGAAMRAGVQ TGDRIIKVNG TLVTHSNHLE VVKLIRSGSY
VALTVQGRPP GSPQIPLADS EVEPSVIGHM SPIMTSPHSP GASGNMERIT SPVLMGEENN
VVHNQKVEIL RKMLQKEQER LQLLQEDYNR TPAQRLLKEI QEAKKHIPQL QEQLSKATGS
AQDGAVVIPS RPLGDTLTVS EAETDPGDGL GRTDCSSGDA SRPSSDNADS PKSGPKERIY
LEENPEKSET IQDTDTQSLV GSPSTRIAPH IIGAEDDDFG TEHEQINGQC SCFQSIELLK
SRPAHLAVFL HHVVSQFDPA TLLCYLYSDL YKHTNSKETR RVFLEFHQFF LDRSAHLKVS
VPDEMSADLE KRRPELIPED LHRHYIQTMQ ERVHPEVQRH LEDFRQKRSM GLTLAESELT
KLDAERDKDR LTLEKERTCA EQIVAKIEEV LMTAQAVEED KSSTMQYVIL MYMKHLGVKV
KEPRNLEHKR GRIGFLPKIK QSMKKDKEGE EKGKRRGFPS ILGPPRRPSR HDNSAIGRAM
ELQKARHPKH LSTPSSVSPE PQDSAKVRQS GLANEGTDAG YLPANSMSSV ASGASFSQEG
GKENDTGSKQ VGETPAPGDT LDGTPRTLNT VFDFPPPPLD QVQEEECEVE RVTEHGTPKP
FRKFDSVAFG ESQSEDEQFE NDLETDPPNW QQLVSREVLL GLKPCEIKRQ EVINELFYTE
RAHVRTLKVL DQVFYQRVSR EGILSPSELR KIFSNLEDIL QLHIGLNEQM KAVRKRNETS
VIDQIGEDLL TWFSGPGEEK LKHAAATFCS NQPFALEMIK SRQKKDSRFQ TFVQDAESNP
LCRRLQLKDI IPTQMQRLTK YPLLLDNIGK YTEWPTEREK VKKAADHCRQ ILNYVNQAVK
EAENKQRLED YQRRLDTSSL KLSEYPNVEE LRNLDLTKRK MIHEGPLVWK VNRDKTIDLY
TLLLEDILVL LQKQDDRLVL RCHSKILAST ADSKHTFSPV IKLSTVLVRQ VATDNKALFV
ISMSDNGAQI YELVAQTVSE KTVWQDLICR MAASVKEQST KPIPLPQSTP GEGDNDEEDP
SKLKEEQHGI SVTGLQSPDR DLGLESTLIS SKPQSHSLST SGKSEVRDLF VAERQFAKEQ
HTDGTLKEVG EDYQITIPDS HLPVSEERWA LDALRNLGLL KQLLVQQLGL TEKSAQEDWR
HCPRYRTASQ GLQTDSVIQN SENIKAYHSG EGHRPFRTGT GDIATCYSPR TSTESSAPRD
SVGLAPQDSQ ASNILVMDHM MMTPEMPTME PEGGLDDSGE HFFDAREAHS DENPSEGDGA
VNKEEKDVNL RISGNYLILD GYDPVQESST DEEVASSLTL QPMTGIPAME STHQQQHSPQ
NTHSDGAVSP FTPEFLVQQR WGAMEDSCFE IQSPSSCADS QSQIMEYIHK IEADLEHLKK
VEESYTILCQ RLAGSALTDK HSDKS
//
