ID W5MW49_LEPOC Unreviewed; 1629 AA.
AC W5MW49;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Rap guanine nucleotide exchange factor 2 {ECO:0000256|ARBA:ARBA00016709};
DE AltName: Full=Cyclic nucleotide ras GEF {ECO:0000256|ARBA:ARBA00031545};
DE AltName: Full=Neural RAP guanine nucleotide exchange protein {ECO:0000256|ARBA:ARBA00032021};
DE AltName: Full=PDZ domain-containing guanine nucleotide exchange factor 1 {ECO:0000256|ARBA:ARBA00030673};
DE AltName: Full=RA-GEF-1 {ECO:0000256|ARBA:ARBA00029925};
DE AltName: Full=Ras/Rap1-associating GEF-1 {ECO:0000256|ARBA:ARBA00031980};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012608.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000012608.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, perinuclear
CC region {ECO:0000256|ARBA:ARBA00004556}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}. Late endosome
CC {ECO:0000256|ARBA:ARBA00004603}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the RAPGEF2 family.
CC {ECO:0000256|ARBA:ARBA00010829}.
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DR EMBL; AHAT01021388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015204989.1; XM_015349503.1.
DR STRING; 7918.ENSLOCP00000012608; -.
DR Ensembl; ENSLOCT00000012632.1; ENSLOCP00000012608.1; ENSLOCG00000010294.1.
DR GeneID; 102691203; -.
DR CTD; 51735; -.
DR eggNOG; KOG3542; Eukaryota.
DR GeneTree; ENSGT00940000158124; -.
DR InParanoid; W5MW49; -.
DR OMA; GTCEYEF; -.
DR OrthoDB; 5473909at2759; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000010294; Expressed in bone element and 13 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01785; RA_PDZ-GEF1; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.8.1240; -; 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 InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45161:SF2; CYCLIC NUCLEOTIDE RAS GEF; 1.
DR PANTHER; PTHR45161; CYTOSKELETON-ASSOCIATED PROTEIN 4; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 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 SUPFAM; SSF54236; Ubiquitin-like; 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 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 261..361
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 393..506
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 511..581
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 736..822
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 847..1074
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 104..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1629 AA; 182525 MW; B023A0FA2CFEC45D CRC64;
MTDSMDTSFK RALKKHPSLR TREDLNTIYC HLYNMDILSH LREHQIRSMC TTARYEKHET
NHVLFYFGKQ SGGRRGYEYI TLEPSEMIVV EAANDSEDLV LQRDAPHRRS RRRFQNQTVN
QTGEKETVSD SQDPSGYHLD YEDNQLPADL AKMHLTDNPH QQVMHVPPSQ SGCSIASDSG
SSSLSDIYQA TESEVGDVDL SGLPEAAVDS EEEEEEDEDI DRASDPLLGR DVVRECLEKD
PVDRMDDDVE QLLEFMHQLP AFANMTMSVR RELCNVMKFE VIEHAGKVIL QDGQELDMWY
VILNGSVEVF HPDGRLEILC MGNSFGISPS LDKQFMSGLV RTKVEDCQFV CIAQEDYWRI
LNHVEKNTHK VEEEGEIVMV KEHRELDRSG TRKGHIVIKG TPERLIMHLV EEHSIVDPTY
IEDFLLTYRT FLSSPMEVGR KLLEWFKVDS LRDKVTRVVL LWVNNHFNDF EGDPAMTQFL
EEFERLLEAA KMKGHLRLLN IACAAKAKWR QVTLVKPSRE SSLFFTLLGG SERGFGIFIE
SVEPGSKAAE AGLKRGDQIM EINGQNFENI TSAKAIDILK NNTHLSITVK TNIFVFKELL
SRIVHEKKNG IPHIPKIQEK KGNRYSIPDL PGDMEQMFPT EKGNKKIKAN TVSGGRNKIR
KILDKTRFSI LPPKPFRGLF CDGGVGQSQD DSIVGTKQCR HSVAIMPIPG SLSSSSPDLL
QPATSVLDFS NPSDIPDQVI RVFKADQQSC YIIISKDTTA KDVVSHVVNE FGLTAAPDTY
SLCEVSISPE GVIKQRRLPD QLSKLADRIQ LNGRYYLKNN METETLCSDD DAQELLRESQ
ISLLQLSTVE VATQLSMRDF ELFRNLEPTE YIDDLFKLDS AASNTHLKQF EDVINQETFW
VATEILKEPN HFKRMKTIKH FIKISLHCRE CKNFNSMFAI ISGLNLAPVA RLRGTWEKLP
SKYEKLFRDL QDIFDPSRNM AKYRNLLSSQ SMQPPIIPLF PVVKKDLTFL HEGNDSSVDG
LVNFEKLRMV AKEIRHVVRM TSANMDPALM FRQRKKRWKS LGSLSQGSTN SNVLDVQVGA
HKKRVRRSSL LNAKKLYEDA QMARKVKQYL SNLQVETDEE KFQIMSLQCE PAYSTLSKNL
SERRSAKSDM SPVSSRSSLP SGKSHQQHRM SQVLQVPTVN LYPLRKKGAS KDIVSFSTSS
PQVVKKPVSS SEEVNCKRAA EDAGSTASSL HSSPPVSPQG SPRKVGSVPK SQNSSQMNLS
GSSSSLTSEA STRNSAHRSS IGIAVTAPTR SDNFSDSSHS EISSRSSLVS NCSVDSVPAS
ASEERCYLQA CSLAERAGAA DRKNGVHSAA DCIQPCTSYS MPRPPVTRAS TFTSSTSNEE
LTHDHIFLDT ADSGRGSWTS CSSNSHDNFQ SIPGQRAWEL SSFRHTQLEG PIVEVEPTGS
WVDDASKRHS KDSLELNQSR QSWASSSSLS DTYEGNYGTI KRRAPENSVV TQGAALDSPQ
RTDASYKTVT SSTEKGLIVY CVTSTQKDDR YRGPPPTPPG YQGISLVDVK EGPSRHPHLK
PPDYSVAVQR SKLVKPPCAI VCQPEAVAHS KRLVQSQMQF RQDSDPSLGS VNRQSQHDSE
EDGEQVSAV
//