ID A0A3B3TN19_9TELE Unreviewed; 1056 AA.
AC A0A3B3TN19;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Rap guanine nucleotide exchange factor 6-like {ECO:0000313|Ensembl:ENSPLAP00000001696.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000001696.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000001696.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
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DR AlphaFoldDB; A0A3B3TN19; -.
DR Ensembl; ENSPLAT00000014311.1; ENSPLAP00000001696.1; ENSPLAG00000002855.1.
DR GeneTree; ENSGT00940000158124; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45161; CYTOSKELETON-ASSOCIATED PROTEIN 4; 1.
DR PANTHER; PTHR45161:SF4; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 6; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 147..176
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 244..358
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 360..431
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 580..647
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 618..838
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 118359 MW; 616A911089B6D82D CRC64;
KMHLTDHAHQ QVMHMAPSQS GCSITSDSGS SSLSDIYQAT ESDLGDVDLS GLPEAPVDSE
EEEEEDEDLE RASDGLLGRD LVRECLEKDP ADRNDDDIQL LEFLHQLPAF ANMTMSVRRD
LCSVMVFEVV EQSGTVILHN KQELQLDHWY VILNGAVEIS HAESRTETLC MGNSFGISPS
LDKQYMNGEV RTKGDDCQQF VCIAQEDYWR ILNHVEKNTH KVEEEGEIVM VKEHRELDRS
GTRKGHIVIK GTPERLIMHL VEEPSVVDPT YIEDFLLTYR TFLSSPMDVG RKLLDWFQVD
CYRDTVTRIV LLWVNNHFND FEGDSAMTLF LEEFEKHLEK MKGHLRLLNI ACAAKAKWRQ
ITLQKASRES QLHFSVQGGS ERGFGVFVES VEEGSKAAET GLKRGDQQIM EVNGQNFENI
GLSKAVDILR NNTHLSLTVK TNIFFKELLS RIMHEKKNGG PHIPKIQEKK GNRFSIADFS
GDIEFPTDSK STRKMKANTV SGGRNKIRKM LEKTRFSILP PKPFDGGLGQ SQDDSIVGTK
QCRHSVAIMP IPGNLSSSSP DLLQPATSVL DFSNPSGEEK DMTAKDVVTH TVNEFSLPAP
PDTYSLCEVS VSPEGVIKQR RLPDQLSKLA DRIQLNGVED LFKLDSSAGC TNLKQFEEVI
NQETFWVATE ILKEPNTLKR MKTIKHFIKI ALHCRECKNF NSMFAIIGLN LAPVARLRSS
WEKLPSKYEK LFEDLQDVFD PSRNMAKYRN VLSSQSMQPP IIPLFPVVKK DLTFLHENDS
NVDGLVNFEK LRMIAKEIRH VVRMTSANMD PALMFRQKKR WKSLSLSQGS TNSNILDVQG
GAHKKRVRRS SLLNAKKLYE DAQMARKVKQ YLSNLTVETD EDKHQIMSLQ CEPSYNTGKN
LSERRANKSD MSPVSLRATL PSGKTQNRVS QVLQVQVPLN PLRKKSTAKD ECPPSSGCPL
LPSAKSDNLS DSSHSEISSR SSICSVDSYC VTSPTKDERY RAPPPTPPGY QGLALGDLGV
ADGVGGGPGS PAPRPPHLRP PDYSVALQRS KLLQSP
//
