ID A0A2K6NT71_RHIRO Unreviewed; 1561 AA.
AC A0A2K6NT71;
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 11 {ECO:0000313|Ensembl:ENSRROP00000007469.1};
GN Name=ARHGEF11 {ECO:0000313|Ensembl:ENSRROP00000007469.1};
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:ENSRROP00000007469.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000007469.1}
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_010379574.1; XM_010381272.1.
DR STRING; 61622.ENSRROP00000007469; -.
DR Ensembl; ENSRROT00000030915.1; ENSRROP00000007458.1; ENSRROG00000027550.1.
DR Ensembl; ENSRROT00000030936.1; ENSRROP00000007469.1; ENSRROG00000027550.1.
DR GeneID; 104676436; -.
DR CTD; 9826; -.
DR GeneTree; ENSGT00940000158350; -.
DR OrthoDB; 2875542at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProt.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd13391; PH_PRG; 1.
DR CDD; cd08753; RGS_PDZRhoGEF; 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; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR037889; PDZRhoGEF_RGS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037803; PRG_PH.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR45872:SF1; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 11; 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; SM00315; RGS; 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; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50132; RGS; 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 47..111
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 353..459
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 774..963
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1005..1119
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1561 AA; 171995 MW; 1ECD892F0E942EE3 CRC64;
MSVRLPQSID RLSSLSSLGD SAPERKSPSH HRQASDASET TGLVQRCVII QKDQHGFGFT
VSGDRIVLVQ SVRPGGAAMK AGVKEGDRII KVNGTMVTNS SHLEVVKLIK SGAYVALTLL
GSSPSSVGIS GLQQDPFPAG APRITPVIPQ PPPPPPLPPP QRITGPKPLQ DPEVQKHATQ
ILRNMLRQEE KELQRICEVY SRNPASLLEE QIEGARRRVT QLQLKIQQET GGSVDVLPLY
GDTSQRPSEG RLSLDSQEGD SGLDSGTERF PSLSESLMNR NSILSDPGLD SPRTSPVIMA
RVAQHHRRQG SDAAVPSTGD QGVDQSPKPL IIGPEEDYDP GYFNNESDII FQDLEKLKSR
PAHLGVFLRY IFSQADPSPL LFYLCAEVYQ QTSPKDSRNL GKDIWNIFLE KNAPLRVKIP
EMLQAEIDSH LRNSEDARGV LCEAQEAAMP EIQEQIHDYR TKRTLGLGSL YGENDLLDLD
GDPLRERQVA EKQLAALGDI LSKYEEDRSA PMDFALNTYM SHAGIRLREA RPSNTAEKAQ
SAPDKDKWLP FFPKTKKSSN SKKEKDALED KKRNPILKYI GKPKSSSQST FHIPLSPVEV
KPGNVRNIIQ HFENNQQYDA PEPGTQRLST GSFPEDLLES DSSRSEIRLG RSESLKGREE
MKRSRKAENV PRSRSDVDMD AAAEATRLHQ SASSSASSLS TRSLENPTPP FTPKMGRRSI
ESPSLGFCTD ALLPHLLEDD LGQLSDLEPE PDAQNWQHTV GKDVVAGLTQ REIDRQEVIN
ELFVTEASHL RTLRVLDLIF YQRMKKENLM PREELARLFP NLPELIEIHN SWCEAMKKLR
EEGPIIKEIS DLMLARFDGP AREELQQVAA QFCSYQSIAL ELIKTKQRKE SRFQLFMQEA
ESHPQCRRLQ LRDLIISEMQ RLTKYPLLLE SIIKHTEGGT SEHEKLCRAR DQCREILKYV
NEAVKQTENR HRLEGYQKRL DATALERASN PLAAEFKSLD LTTRKMIHEG PLTWRISKDK
TLDLHVLLLE DLLVLLQKQD EKLLLKCHSK TAVGSSDSKQ TFSPVLKLNA VLIRSVATDK
RAFFIICTSK LGPPQIYELV ALTSSDKNTW MELLEEAVRN ATRHPGAAPM PIHPPPPGSQ
EPAHQGLTPS RVELDDSDVF HGEPEPEELP GGTGPQQRVQ GKHPVLLEDP EQEGSVEEEL
GVLPCPSTSL DGENRGIRTR NPIHLAFPGP LFMEGLADSA LEDVENLRHL ILWSLLPGHT
METQAAREPE DDLTPTPSVI SVTSHPWDPG SPGQAPPGDQ GDNTQLAGPE GERPEQEDVG
LCSLEHLPPR TRNSGIWESP ELDRNLAEEA ASTEAAGGYK VVRKAEVAGS KVVPALPESG
QSEPGPPEVE GGTKATGNCF YVSMPAGPLD SSTDHSGVPT SPPQPDSVPA GQAEPQPQLQ
GGNGDPRCLS RSPPSLALRD VGMIFRTIEQ LTLKLNRLKD MELAHRELLK SLGGESSGGT
TPVGSFHTEA ARWTDGSLSP PTKEPLASDS RNSHELGPCP EDGSDAPLED SAADAAASPG
P
//
