ID A0A2K6US42_SAIBB Unreviewed; 1485 AA.
AC A0A2K6US42;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN Name=RAPGEF2 {ECO:0000313|Ensembl:ENSSBOP00000034723.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000034723.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000034723.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC -!- SIMILARITY: Belongs to the RAPGEF2 family.
CC {ECO:0000256|ARBA:ARBA00010829}.
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DR Ensembl; ENSSBOT00000051648.1; ENSSBOP00000034723.1; ENSSBOG00000033382.1.
DR GeneTree; ENSGT00940000156418; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; 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; cd01785; RA_PDZ-GEF1; 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 InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45161; CYTOSKELETON-ASSOCIATED PROTEIN 4; 1.
DR PANTHER; PTHR45161:SF2; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 2; 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:UP000233220};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 122..222
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 254..367
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 372..442
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 593..679
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 704..931
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 24..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 165914 MW; 8693387E4EA6F940 CRC64;
GERDKNSLPA DFTKLHLTDS LHPQVTHVSS SHSGCSITSD SGSSSLSDIY QATESEAGDM
DLSGLPETAV DSEDDDDEED IERASDPLMS RDIVRDCLEK DPIDRTDDDI EQLLEFMHQL
PAFANMTMSV RRELCAVMVF AVVERAGTIV LNDGEELDSW SVILNGSVEV TYPDGKAEIL
CMGNSFGVSP TMDKEYMKGV MRTKVDDCQF VCIAQQDYCR ILNQVEKNMQ KVEEEGEIVM
VKEHRELDRT GTRKGHIVIK GTSERLTMHL VEEHSVVDPT FIEDFLLTYR TFLSSPMEVG
KKLLEWFNDP SLRDKVTRVV LLWVNNHFND FEGDPAMTRF LEEFENNLER EKMGGHLRLL
NIACAAKAKR RLMTLTKPSR EAPLPFILLG GSEKGFGIFV DSVDSGSKAT EAGLKRGDQI
LEVNGQNFEN IQLSKAMEIL RNNTHLSITV KTNLFVFKEL LTRLSEEKRN GAPHLPKIGD
IKKASRYSIP DLAVDVEQVI GLEKVNKKSK ANTVGGRNKL KKILDKTRIS ILPQKPYNDI
GIGQSQDDSI VGLRQTKHIP TALPVSGTLS SSNPDLLQSH HRILDFSTTP DLPDQVLRVF
KADQQSRYIM ISKDTTAKEV VIQAIREFAV TATPDQYSLC EVSVTPEGVI KQRRLPDQLS
KLADRIQLSG RYYLKNNMET ETLCSDEDAQ ELLRESQISL LQLSTVEVAT QLSMRNFELF
RNIEPTEYID DLFKLRSKTS CANLKRFEEV INQETFWVAS EILRETNQLK RMKIIKHFIK
IALHCRECKN FNSMFAIISG LNLAPVARLR TTWEKLPNKY EKLFQDLQDL FDPSRNMAKY
RNVLNSQNLQ PPIIPLFPVI KKDLTFLHEG NDSKVDGLVN FEKLRMIAKE IRHVGRMASV
NMDPALMFRT RKKKWRSLGS LSQGSTNATV LDVAQTGGHK KRVRRSSFLN AKKLYEDAQM
ARKVKQYLSN LELEMDEESL QTLSLQCEPA TNTLPKNPGD KKPVKSETSP VAPRAGLQQK
AQSLPQPQQQ PPPPHKINQG LQVPAVSLYP SRKKVPVKDL PPFGINSPQA LKKILSLSEE
GSLERHKKQA EDTVSNASSQ LSSPPTSPQS SPRKGYPLAP SGTVDNFSDS GHSEISSRSS
IVSNSSFDSV PVSLHDERRQ RHSVSIVETS LGVGRMERRT MMEPDQYSLG SYAPMSEGRG
LYATATVISS PSTEELSQDQ GDRASLDAAD SGRGSWTSCS SGSHDNIQTI QHQRSWETLP
FGHTHFDYSG DPTGLWASSS HMDQIMFSDH STKYNRQNQS RESLDQAQSR ASWASSTGYW
GEDSEGDTGT IKRRGGKDVS IEAESSSITS VTTEESKPVP MPAHIAVASS TAKGLIARKE
GRYREPPPTP PGYIGIPITD FPEGHSHPAR KPPDYNVALQ RSRMVARSSD TAGPSSVQQP
HGHPTSSRPV NKPQWHKPNE SDPRLAPYQS QGFSTEEDDE QVSAV
//
