ID G1SZW2_RABIT Unreviewed; 1561 AA.
AC G1SZW2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Rho guanine nucleotide exchange factor 11 {ECO:0000313|Ensembl:ENSOCUP00000009249.3};
GN Name=ARHGEF11 {ECO:0000313|Ensembl:ENSOCUP00000009249.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000009249.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000009249.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000009249.3,
RC ECO:0000313|Proteomes:UP000001811};
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:ENSOCUP00000009249.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000009249.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAGW02000386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02000387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02000388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02000389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PaxDb; 9986-ENSOCUP00000009249; -.
DR Ensembl; ENSOCUT00000010739.4; ENSOCUP00000009249.3; ENSOCUG00000010731.4.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000158350; -.
DR HOGENOM; CLU_003962_5_0_1; -.
DR OMA; FICGERQ; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000010731; Expressed in frontal cortex and 16 other cell types or tissues.
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; 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.
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:UP000001811}.
FT DOMAIN 47..111
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
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..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..271
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 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 1122..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..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 142..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 310..325
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 1154..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1561 AA; 171692 MW; 2C121CFE5FB2F2DC CRC64;
MSVRLPQSID RLSSLSSLGD SAPERKSPSH HRQPSDTSET TGLVQRCVII QKDQHGFGFT
VSGDRIVLVQ SVRPGGAAMK AGVKEGDRII KVNGTMVTNS SHLEVVKLIK SGAYVALTLL
GSSPSSVGVS GLQQDPSPAG APRVTPMIPP PPPPPPLPPP QRITGPKPLQ DPEVQKHATQ
ILRNMLRQEE KELQRICEVY SRNPASLLEE QIEGARRRVT QLQLKIQQET GGLVDILPLY
GDTSQRPSEG RLSLDSQEGD SGLDSGTERF PSLSESLMNR NSVLSDPGLD SPRTSPVIMT
RVAQHHRRQG SDATVPSTSD QGVDQSPKPL IIGPEEDYDP GYFNNESDII FQDLEKLKSR
PAHLGVFLRY IFSQADPSPL LFYLCAEVYQ QTNPKDSRSL GKDIWNIFLE KNAPLRVKIP
EMLQAEIDLR LRNSEDVRSA LSEAQGAAMP EIQEQIHDYR TKRTLGLGSL YGENDLLDLD
GDLLRERQVA EKQLAALGDI LSKYEEDRSA PMDFALNTYM SHAGIRLREA RPSSTAEKAQ
AAPDKDKWLP FFPKTKKSSN SKKEKDALED KKRNPILKYI GKPKSSSQST FHIPLSPVEV
KPGNVRNIIQ HFENSQQCDA PEPGTQRLST GSFPEDLLES DSSRSEVRLG RSESLKGREE
MKRSRKAENV PRSRSDVDMD AAAEATRLHQ SASSSASSLS TRSLENPTPP FTPKMGRRSI
ESPSLGFCTD ALLPHLLEDD LGQLSDLEPE PDAQNWQHTV GKDVVAGLAQ REIDRQEVIN
ELFVTEASHL RTLRVLDLIF YQRMKKENLL PRDELARLFP NLPELIEIHN CLCEAMKRLR
EEGPIIRGIG DLMLSRFDGA AREELQQVAA QFCSYQSIAL ELIKTKQRKE SRFQLFMQEA
ESHPQCRRLQ LRDLIISEMQ RLTKYPLLLE SVIKHTEGGT SEHEKLCRAR DQCREILKYV
NEAVKQTENR HRLEGYQKRL DASALERASN PLAAEFKSLD LTTRKMIHEG PLTWRISKDK
TLDLHVLLLE DLLVLLQKQD EKLLLKCHSK TAAGSADSKQ TFSPVLKLNA VLIRSVATDK
RAFFIICTSE LGPPQIYELV ALTSSDKNTW MELLEEAVQN ATRHPGAAPT PIHAPAPGPQ
EQAHQGPTPS RLDLDDSEVF HSEPEAEEPL EAGPGPPQRG QGMQPVLLGD PEQRGHGEEE
LGALPDPPAP LGGENSTIRT RDPFHLALPG PLFMEGLADS ALEDVENLRH LILWSLLPGH
TPETQTAREP EDDLTPTPSV ISITSHPWDP GSPGRAPAAG EGDSTQLPGP ERGQPEQDTA
LSSLEHLPPR TRNSGIWESP ELDRNPAEEA SRTEGTGNYK VVRKAEVAGG KGVPALPESG
QSEPEPPEAE GGTKAAGNCF YVSMPAGPLD SSTDLPEAPA SPCQPDGLPA WQTEPRPQLQ
GGSEDPRRPS CSAPSLALRD VGMIFQTIEQ LTLKLNRLKD MELAHRELLK SLGGESSGGT
TPVGSFHTEP ARWTDSSLSP PAKEPLDPDS GNSRELGPCP EDGPDTALEY GAADAATSPG
L
//
