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Database: UniProt
Entry: G1PH82_MYOLU
LinkDB: G1PH82_MYOLU
Original site: G1PH82_MYOLU 
ID   G1PH82_MYOLU            Unreviewed;      1552 AA.
AC   G1PH82;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Rho guanine nucleotide exchange factor 11 {ECO:0000313|Ensembl:ENSMLUP00000010025.2};
GN   Name=ARHGEF11 {ECO:0000313|Ensembl:ENSMLUP00000010025.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000010025.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000010025.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000010025.2}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AAPE02034942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000010025; -.
DR   Ensembl; ENSMLUT00000011000.2; ENSMLUP00000010025.2; ENSMLUG00000010956.2.
DR   eggNOG; KOG3520; Eukaryota.
DR   GeneTree; ENSGT00940000158350; -.
DR   HOGENOM; CLU_003962_5_0_1; -.
DR   InParanoid; G1PH82; -.
DR   OMA; FICGERQ; -.
DR   TreeFam; TF106495; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
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:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR   CDD; cd00992; PDZ_signaling; 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; 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:UP000001074}.
FT   DOMAIN          45..109
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          351..412
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   DOMAIN          773..962
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1004..1118
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          17..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1123..1154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1199..1220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1257..1447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1507..1552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..159
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..682
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1127..1141
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1409..1423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1552 AA;  171167 MW;  6A81253A679AC3E6 CRC64;
     SLICFYYSFS RLSSLSLGDS APERKSPSHH GQPDSSETTG LVQRCVIIQK DQHGFGFTVS
     GDRIVLVQSV RPGGAAMKAG VKEGDRIIKV NGTMVANSSH LEVVKLIKSG AYVALTLLGS
     SPSTVGVSGL QQDPDPAGAP QVAPVIPPPP PPPPLPPPQR ITGPTPLQDL EFQKHATQIL
     RNMLRQEEKE LQHICEMYSR NPTSLLEEQI EAARRRVTQL QLKIQQETGG LVDILPLYSD
     ISQRSSEGRL SLDSQDGDSG LDSGTERFPS LSESLINRNS VLSDPGLDSP RTSPVIMARV
     AQHHRWQGSD APAAPTSDQG ADQSPKPLII GPEEDYDPGY FNNESDIIFQ DLEKLKSRPA
     HLGVFLRYIF SQADPSPLLF YLCAEVYQQT NSKDSRSLGK DIWNIFLEKN APLRVKVPEA
     LQAEIDLRLR SGEDLRCVLC EAQEAAMPEI QEQIQDYRSK RTLGLGSLYG ENDLLDLDGN
     PLRERQVAEK QLAALGDILF KYEEDRSAPM DFALNTYMSH AGIRLREARS SSTAEKAPLS
     APDKDKWLPF FPKTKKSSNP KKEKDALEDK KRNPILKYIG KPKSSSQSTF HIPLSPVEVK
     PGNVRNIIQH FENNQQYDAP EPGMQRLSTG SFPEDLLESD SSRSEIRLGR SESLKGREEL
     KRSRKTENVP RSRSDVDMDA AAEAARLHQS ASSSASSLST RSLENPTPPF TPKMGRRSIE
     SPSLGFCTDV LLPHLLEDDL GQLSDLELEP DTQNWQHTVG KDVVAGLTQR EIDRQEVINE
     LFVTEASHLR TLRVLDLIFY QRMKKENLMP REELARLFPN LPELIEIHNS WCEAMKKLRE
     EGPIIKEISD LMLARFDGPA REELQQVAAQ FCSYQSIALE LIKTKQRKES RFQLFMQEAE
     SHPQCRRLQL RDLIISEMQR LTKYPLLLES IIKHTEGGTS EHEKLCRARD QCREILKYVN
     EAVKQTENRH RLEGYQETDT TSLERASNPL AADLRKSLDL TTRKMIHEGP LTWRISKDKT
     LDLHVLLLED LLVLLLKQDE KLLLKCHSKT AMGSSDSKQT FSPVLKLNAV LVRSVATDKR
     AFFIICTSEL GPPQIYELVA LTSSDKNTWM ELLEEAVRNA TRHPGAAPTP VLPPPPGPQE
     SAHQSPRSSR VGLDDSEVFQ REPEPEVLPG GTGPQPGVTG KHSVLLEDLK HEGSMEATEL
     GALPHPSASL DGENRGGRTR DPIVLPLPGP LFMEGLADAA LEDVEILRHL ILRGQLPSHP
     REPQAAGEPE DDLTPTPSVV SITSHPWDPG SPGRAPTEGE GENTQLPGPE GGQPEQEDVA
     LCSLEHLPPR TRNSGIWEPP ELDRSPEEEA SSTEAAGSYK VVRKAEVAGS KAVPALPEGG
     QSEAEPPEVE GGAKATGNCF YVSMPAGPPD SSTDLSQPNG LPAWRTEPQP RGGNGEPRRP
     SCSPPSLAVK DMGIIFQTIE QLTLKLNRLK DMELAYRELL RSLGGESSGG TTPVGSFHTE
     AAKWADCSLS PPVKDPPPSA SWDSHELGPC PEDSTRSPRE DSVADAATPP GL
//
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