ID A0A087RA38_APTFO Unreviewed; 1118 AA.
AC A0A087RA38;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Rho guanine nucleotide exchange factor 11 {ECO:0000313|EMBL:KFM10342.1};
DE Flags: Fragment;
GN ORFNames=AS27_10656 {ECO:0000313|EMBL:KFM10342.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM10342.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM10342.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM10342.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; KL226235; KFM10342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087RA38; -.
DR STRING; 9233.A0A087RA38; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
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.
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:UP000053286}.
FT DOMAIN 39..103
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 757..946
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 988..1101
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM10342.1"
FT NON_TER 1118
FT /evidence="ECO:0000313|EMBL:KFM10342.1"
SQ SEQUENCE 1118 AA; 125733 MW; CE1EEA556CE9E467 CRC64;
LRRLSSLSSL GDSSSERRSP GHHRQPSDSS ETTGLVQRCV IIQKDQHGFG FTVSGDRVVL
VQSVRPGGAA MRAGVQEGDR IVKVNGTMVT NSSHLEVVKL IKSGAYVALT LLGSPPPSVG
LSSSQQDVSM AGPPPPPPPL PPPQRITDPK PLQDPEVQKH ATQILRNMLR QEEAELQRFY
EVYSRNPATT VEEQIEGARR RVSQLQLKIL QETGGSMDSG RLCGDSGLAG FRVMEGRLSL
DSQDGDSGLE SGTERFPSVS EISLNRNSVL SDHGLDSPRT SPVITARLFQ HHRRQGSDTP
FAPPAEQGLD RTGRPLIIGP EEDYDPGYFN NECDSLFQDL GKLKSRPAHL GVFLRYIFSQ
ADPSPLLFYL CTDVCQQTAT KDSRVLGKDI WNIFLDRNAP LRVKVSEQLL AEIETRLRNG
DDVRAALFEA QEMVMPEIQE QIQDYRTKRT MGLGSLYGEN DLLDLDGDPQ KERQVAEKQL
AQLGDILSKY EEDRSSPMAF ALSTYMNHTG IRSREPRVAG TSEKAQSLPD RDKWLPFFPK
TKKSSSTKKD KDAMEDKKRN PILKYIGKPK ISSQSTFHVP LSPVEAVKPG NVRNIIQHFE
NNQHYESQEP GTQRLSTGSL PEAPLSRAEV KLGRSESLKG REEMKKSRKA ENVPRSRSDV
DMDAAAEATR LHQSASSSAS SLSTRSLENP TPPYTPKMGR RSIESPNLGF GVDPFLPHLL
EDEQGQLSDL EPELDSQNWQ HTVSRELVAN LPQKEIDRQE VINELFATEG SHLRILRVLD
LLFYQRMKKE SLLSREELAL LFPNLPDLIE IHNSLSESMK KLREEGPIIK EIGDLMLSRF
DGLAKEEIQQ VAADFCSYQS IALELIKTKQ RKETRFQIFM QEAESNPQCR RLQLKDLIIS
EMQRLTKYPL LLENIIKHTE AGTSEHDKLC RARDQCRDIL KYVNEAVKRA ENRHRLESYQ
KRLDATSLER TSNPLAAEFK NLDLTSRRMI HEGPLTWRIS KDKTVDLHVL LLEDLLVLLQ
KQDEKLVLKC HSKTALGSSD NKQTFSPVLK LNSVLIRSVA TDKRALFIIC TSELGPQIYE
LVALTSSEKN TWMELLEEAV QSATRNATFP PKRRTLEP
//
