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Database: UniProt
Entry: W5MW49_LEPOC
LinkDB: W5MW49_LEPOC
Original site: W5MW49_LEPOC 
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
//
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