ID A0A1L8FCB6_XENLA Unreviewed; 1593 AA.
AC A0A1L8FCB6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Rho guanine nucleotide exchange factor 11 isoform X6 {ECO:0000313|RefSeq:XP_018086924.1};
GN Name=arhgef11.L {ECO:0000313|RefSeq:XP_018086924.1,
GN ECO:0000313|Xenbase:XB-GENE-6486859};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018086924.1};
RN [1] {ECO:0000313|RefSeq:XP_018086924.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018086924.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018086924.1};
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_018086924.1; XM_018231435.2.
DR STRING; 8355.A0A1L8FCB6; -.
DR PaxDb; 8355-A0A1L8FCB6; -.
DR GeneID; 108699391; -.
DR AGR; Xenbase:XB-GENE-6486859; -.
DR CTD; 108699391; -.
DR Xenbase; XB-GENE-6486859; arhgef11.L.
DR OMA; FICGERQ; -.
DR OrthoDB; 2875542at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 108699391; Expressed in stomach and 19 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: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; 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; 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.
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:UP000186698}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1436..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1593 AA; 178588 MW; 6266B91C8A748F55 CRC64;
MSISSAQTSI DRLSNLSSAS DGAAERRSPG HQRQPCESNE STGLVQRCVI VQRDQNGFGF
TVSGDRIVLV QSVRQGGAAM RAGVQEGDRI VKVNGTLVAN SSHIEVVKLI KSGAYVALTL
LGSPPPSMGM SGYQQDLSSS VSPRNIFLSP MPPPPPPPLP QSHHITGPKP LQDPDFQKHA
TEILWNMLKQ EEADLQNLCD VYNRSPNPSL QEQIERARKR VHQLQHKIRQ EIPSTGDLLR
SYSDCSSAGY KVKEGRLSVD SQDADSGLDS GTERISSLSE YSMNRNSVMS DLGMDSSHTS
PIISTKLFHH HHRRHGSDTT FIGTSEQVSD HTRPTIIGPE EDCDHGYYMT EQSDGLFQDL
EKLKTRPAHM GVFLRYIFSQ ADPNPLLFYL SAEACQHLSP VDAFPLRKEV WNIFLDKSAS
LRVKIPEQLL NEIESRLRNS EDIRGLFSEA QEAMLPEIQE QIQDYRTKRT MGLGSLYGEN
DLFELEIDPQ RERQVAAKQI AQLEDILSKY EKEISLPMAF ALSMYVKYAG IHTQDIRPAS
TSEKTQIIPD RDKWLPFFPK NKKSSNAKKD KESAEDKKRN PILKYINKPK STSQSTFHVP
LSPGEVKPGN VRNIIQHFEN NQQYDVPEHN LQRLSTGSFP GDLLDSDGSR SEVKLGRSES
LKGREELKKS RKVDNVPRSR SDVDMDAAAE ATRLHQSASS SASSLSARSL DNPTPPYTPK
LCRRSIESPS LGFTGELLLS NLQEDDLGHL SDLDPEPDAQ NWQHTVGRDV ALHLPPKERA
RQEVIHELFV TEASHLRVLR VLDLIFYQRM RKENLLTPDE LWLVFPNLPE LIEIHNSLAE
SMKRMREEGP VIKEIGDLML LRFDGASGEE VRMEAARFCS YQTSALELIK AKKRKETRFS
LFMQEAESNP QCRRLQLKDL IVSEMQRLTK YPLLLENVLK HTDSGTQEHE KLYRCRDRCR
DILKYVNESV KQAENEHRLA EYQKRLDASH LERSNNPLAA EFKNLDLTTR RMIHEGPLTW
RVTKDKTIDL HVLLLEDLLV LLQKQDEKLV LKCHSKTTMV STDTKQTFSP VIKLNSVLVR
SVATDKRALF IICTSDLGPQ IYELVAMTSS EKNTWKDLLE EATKGTMRNP PSATKRKSQD
INRPTSASML LQRTHMPKLP AEGVLQHNSE DLQSGDESAG EFSGHQKPDV VVEEPEREDD
EEDEARTPTL LPIPSKEEDA GGGILGLDSS NRIPYHWPAV TEGLAESALD DVHNLRQLIL
KNMLHHGHSE YDSGSAPVAE PEEDLTPTPS VIGGHGHPWD TMTDAVLENL DGDQTTEEKE
TSIPPSISGS ESSRSVLNFP HGERPGSRDG EETAWSLVER NPQGSSVHQN QSEQLHSEDH
SNRSYRVVRK AEVVGNYDVI PLPDSSQSQS VLQEAGAGAI VDGNFFYVTA SAVSAKEDNE
VSESPTNSDR LASPSFLESR ESNHTPTYQS GFATPPSRST ESDPLDLLPP KLVIQDVDII
FRTIEQLTAK LHRLKEVESA HQELLRSLGR SATDDHFHER EHAAEKDKQA QKHQGSSLNS
ASLFFVKNSR SVSLHRDGNT DPQEDAINLA MGM
//
