ID I3K6J0_ORENI Unreviewed; 1408 AA.
AC I3K6J0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Rho guanine nucleotide exchange factor 12 {ECO:0000313|Ensembl:ENSONIP00000016735.2};
GN Name=LOC100708196 {ECO:0000313|Ensembl:ENSONIP00000016735.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000016735.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000016735.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
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 STRING; 8128.ENSONIP00000016735; -.
DR Ensembl; ENSONIT00000016750.2; ENSONIP00000016735.2; ENSONIG00000013306.2.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000157662; -.
DR HOGENOM; CLU_003962_1_0_1; -.
DR InParanoid; I3K6J0; -.
DR OMA; EIFFIAN; -.
DR TreeFam; TF106495; -.
DR Proteomes; UP000005207; Linkage group LG10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 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; IPR002466; A_deamin.
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; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR45872:SF3; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 12; 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; 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; PS50141; A_DEAMIN_EDITASE; 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:UP000005207}.
FT DOMAIN 47..124
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 666..827
FT /note="A to I editase"
FT /evidence="ECO:0000259|PROSITE:PS50141"
FT DOMAIN 691..881
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 923..1036
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1408 AA; 156894 MW; 39A333449EA4D3E8 CRC64;
MSGTQSTLAD KTPSILNREP TDWKPKNEKP SPSLKNEFDP TGLVQRCVII QRDENGFGLT
VSGDNPVFVQ LVKEDGAAMR AGVQTGDRII KVNGTLVTHS NHLEVVKLIR SGSYVALTVL
GRPPGLPQIP LEEEKEGNEE GGDTLSAPHS PALSGGEQGS FLTSSTPCSP QDNTTSSSLS
DGEGATASWN GEIEDGDGGS PLKEQTSPTP CDNGPLINNN SVHSSPLSDT VGYRGTPCQS
PDISRRDGLN ICTSPEAEDA ADTHPNTHYS GGSPPYLVNP QIIGAEDDYF ESSQEQINGE
CTCFQSIESL KSRPAHLAVF LHHVVSQFDP APLLCYLYAD MYKQTNSKES RRFFIEFHTL
FMDRTANLKV PVPETVSAEL EKRRLDLIPD SLCKQYIQTL QDALLPDLHR NLEDFRQKRS
MGLTLAEDEL CKLDSEPGRD QQALEKECSC AEHILFKIED ILLTSQNSEE EKWQTMQYVI
LTYMKHLGVK VKEHRGLEHK RARITFPRIK FPNIRPPRRP SRVDPTPVVK AVDQIKQRPP
KLPQSPLGIS EPSDPSATSP GRIRDGSDTQ FLPATTLPTH SSPTTQVSEA GGQESESNVS
PFCIQPRPGD SVQSADNHDG VSGPTGTQFD FSPTTVEQRD DDQEAFRMEV QGDIQSEDDQ
GGEAECEEDP LIWQVLVPRG VLMSLTQQEI NRQEVINELF YTERAHLRML KVLDCVFCQR
LNRDGILPPE DIKHIFINLE EIIQLHVSIT EQMTAIRKRN ETSVIGQIGD DLLGWFSGEE
EQKLKRAVAT FCSNQPSALE LIKTRQKKDQ KFNLFMQEAQ SNRLCRRLQL KDIIPVEMQR
VTKYPLLLDN IAKYTEDIEE RKKVKRAGDC CKKILNHVNQ AVKEAENKQR LEEYQRRLEF
SSLKQSENPV ILELKNLDLT KRKMVHEGPL SWKVNKEKTI ELYTLLLEDI MVLLQKQDER
LVLKFHGKNT ASVVDTKHTF SPIIKLNTVL VRPVATDNKS FFVLSMSENG AQIYELTAQT
VSDQRMWQHL ITQCADAMKA KPHRRDTPPP QSDAERDAIN IINNGMPKLS KDETPSVHSA
DMSTSDKEAA STSDIQDPPE SLNPFDGLRS EDEEEELPMA DRQEEEEQNG EVDEAELEAF
LDGQLAERLL QEGSRLGIAL ENEEEHNAFV MPCSKAEEAL KTLAMLKQAV FTHMLSREAE
EETEESKPSG ARGSQSSPSL PESPEGPSAT CDESRVSESL QKEDLQPPPE AAERNGGFVV
LDFPGSEESS TDDDVGVGSD VGIDMRKLLS SSSQMGGGGP NLSRQLMTHL RLLQADLQYL
KDIELKYNEL RQTHGDAATD SDDNNGVFLI LSVISLSSAS RSLECFVFQT LFLVFFQMGF
SDERLPALSA VRAKFHVAAC SPSSTFYH
//