ID A0A2Y9M862_DELLE Unreviewed; 1571 AA.
AC A0A2Y9M862;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Rho guanine nucleotide exchange factor 11 isoform X4 {ECO:0000313|RefSeq:XP_022415277.1};
GN Name=ARHGEF11 {ECO:0000313|RefSeq:XP_022415277.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022415277.1};
RN [1] {ECO:0000313|RefSeq:XP_022415277.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022415277.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR RefSeq; XP_022415277.1; XM_022559569.2.
DR Proteomes; UP000248483; 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: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; IPR001331; GDS_CDC24_CS.
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; PS00741; DH_1; 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:UP000248483}.
FT DOMAIN 46..110
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 352..413
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 125..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..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 688..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1571 AA; 172862 MW; 1166163BAEAFA9AB CRC64;
MSVRLPQSID RLSSLSLGDS APERKSPSHH RQPSDTSETT GLVQRCVIIQ KDQHGFGFTV
SGDRIVLVQS VRPGGAAMKA GVKEGDRIIK VNGTMVTNSS HLEVVKLIKS GAYVALTLLG
SSPSSIGVSG PQQDPVPAGA PRVTPVIPPP PPPPPLPPPQ RITGPKPLQD PEFQKHATQI
LRNMLRQEEK ELQRICEVYS RNPGSLLEEQ IEGARRRVTQ LQLKIQQETG GLVDILPLYG
DTGQRSSEGR LSLDSQEGDG GLDSGTERFP SLGESLVNRN SVLSDPGPDS PRTSPVIMAR
VAQHHRRQGS DALVPPSGDQ GVDQSPKPLI IGPEEDYDPG YFNNESDIIF QDFEKLKSRP
AHLGVFLRYI FSQADPSPLL FYLCAEVYQQ TNPKDSRSLG KDIWNIFLEK NAPLRVKVPE
MLQAEIDLRL RNGEDVRAVL CEAQEAAMPE IQEQIHDYRT KRTLGLGSLY GENDLLDLDG
DPLRERQVAE KQLAALGDIL SKYEEDRSAP MDFALNTYMS HAGIRLREAR PSNTAEKAQS
APDKDKWLPF FPKTKKQSSN SKKEKDALED KKRNPILKYI GKPKSSSQST FHIPLSPVEV
KPGNVRNIIQ HFENSQQCDA PEPGTQRLST GSFPEDLLES DSSRSEIRLG RSESLKGREE
MKRSRKAENV PRSRSDVDMD AAAEAARLHQ SASSSASSLS TRSLENPTPP FTPKMGRRSI
ESPSLGFGTD ALLPNLLEDD LGQLSDLEPE PDAQNWQHAV GKDVVAGLSQ REVDRQEVIN
ELFVTEASHL RTLRVLDLIF YQRMKKEGLL PREELARLFP NLPELIEIHN SWCEAMRKLR
EEGPIIKEVS DLMLARFDGP AREELQQVAA QFCSYQSIAL ELIKTRQRKE SRFQLFMQEA
ESHPQCRRLQ LRDLIISEMQ RLTKYPLLLE NIIKHTEGGT SEHEKLCRAR DQCREILKYV
NEAVKQTENR HRLEGYQKRL DTTSLERASN PLAAEFKSLD LTTRKMIHEG PLTWRISKDK
TLDLHVLLLE DLLVLLQKQD EKLLLKCHSK TAVGSSDSKQ TFSPVLKLNA VLIRSVATDK
RAFFIICTSE LGPPQIYELV ALTSSDKNTW MELLEEAVRN ATRHPGAAPK PVHPPPSGPQ
EPAHQSPTPS REGLDDSEVF HSEPEPETVP GGTGPQQRVK GKHPVLLEDP KQEGSIEEEE
LGTLPHPSAS LDGENRGSRT RDPILLPLPG PLFMEGLADA ALEDVENLRH LILWSLLPAR
PTDPQTSGEP EDDLTPTPSV ISITSHPWDP GSPGRAPTGG EGDNAPLSGP ERGQQEDMAL
CSLEHLPPRT RNSGIWESPE LDRNPEEEAS STEATGSYKV VRKVSTVPGG GVGAAEVAGS
KVVPALPESG QSEPEPPEVE GGAKATGNCF YVSMPAGPLD SSTDPSGARV GPSQPDGLPA
WQPAPRPALR EGNEDQRRLG RSPPSLALRD MGVIFHTIEQ LTVKLNRLKD MELAHKELLR
SLGGESSGGT TPVGGFHTEA ARWIDSSLSP PAKEHLASDS RDSCELGPCP EDGHNAPLED
GPADSATSPG L
//
