ID A0A2K6NT82_RHIRO Unreviewed; 1524 AA.
AC A0A2K6NT82;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Rho guanine nucleotide exchange factor 11 {ECO:0000313|Ensembl:ENSRROP00000007482.1};
GN Name=ARHGEF11 {ECO:0000313|Ensembl:ENSRROP00000007482.1};
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:ENSRROP00000007482.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000007482.1}
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 Ensembl; ENSRROT00000030955.1; ENSRROP00000007482.1; ENSRROG00000027550.1.
DR GeneTree; ENSGT00940000158350; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001664; F:G protein-coupled receptor binding; 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:0007266; P:Rho protein signal transduction; IEA:InterPro.
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; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 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; 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 343..449
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 754..943
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 985..1099
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 15..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1524 AA; 168416 MW; 09C133AB8CE3E816 CRC64;
SLTCFPYSFS RLSSLSSLGD SAPERKSPSH HRQASDASET TGLVQRCVII QKDQHGFGFT
VSGDRIVLVQ SVRPGECCIP PVNGTMVTNS 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 GKPKSSSQSI 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 EDGE
//
