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Database: UniProt
Entry: I3K6J0_ORENI
LinkDB: I3K6J0_ORENI
Original site: I3K6J0_ORENI 
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}.
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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
//
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