ID A0A2U4ALU9_TURTR Unreviewed; 1638 AA.
AC A0A2U4ALU9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 27.
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|RefSeq:XP_019781938.2};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019781938.2};
RN [1] {ECO:0000313|RefSeq:XP_019781938.2}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019781938.2};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_019781938.2; XM_019926379.2.
DR Proteomes; UP000245320; Chromosome 5.
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; 2.
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; 2.
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; 2.
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; 2.
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; 2.
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:UP000245320};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 37..84
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 290..390
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 422..535
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 540..610
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 761..847
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 872..1099
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 195..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1638 AA; 183194 MW; A5EA351BAB93EEA5 CRC64;
MASYVDNSFR QAVMKNPAER TPQDLEIVYS YLHGMEALSN LREHQLRLMC ETVRYERHEA
NEVLYYPDDI GTCWYILLSG SVFIKESMFL PRSSFGKRSA GSFRRGCECI VLEPSEMIVV
DYMDENEEYF QRQASHRQSR RRFRKINQKG ERQTIIDTVD PYPVGKPPLP RGYHTLPADF
TKLHLTDSLH PQVTHVSSSH SGCSITSDSG SSSLSDIYQA TESEAGEMDL SGLPETAVDS
EDDDDEEDIE RASDPLMSRD IVRDCLEKDP IDRTDDDIEQ LLEFMHQLPA FANMTMSVRR
ELCAVMVFAV VERAGTIVLN NGEELDSWSV ILNGSVEVTY PDGKAEILCM GNSFGVSPTM
DKEYMKGVMR TKVDDCQFVC IAQQDYCRIL NQVEKNMQKV EEEGEIVMVK EHRELDRTGT
RKGHIVIKGT SERLTMHLVE EHSVVDPTFI EDFLLTYRTF LCSPMEVGKK LLEWFNDPSL
RDKVTRVVLL WVNNHFNDFE GDPAMTRFLE EFENNLEREK MGGHLRLLNI ACAAKAKRRL
MTLTKPSREA PLPFILLGGS EKGFGIFVDS VDSGSKATEA GLKRGDQILE VNGQNFENIQ
LSKAMEILRN NTHLSITVKT NLFVFKELLT RLSEEKRNGA PHLPKIGDIK KASRYSIPDL
AVDVEQVIGL EKVNKKSKAN TVGGRNKLKK ILDKTRISIL PQKPYNDIGI GQSQDDSIVG
LRQTKHIPTA LPVSGTLSSS NPDLLQSHHR ILDFSATPDL PDQVLRVFKA DQQSRYIMIS
KDTTAKEVVI QAIREFAVTT TPDQYSLCEV SVTPEGVIKQ RRLPDQLSKL ADRIQLSGRY
YLKNNMETET LCSDEDAQEL LRESQISLLQ LSTVEVATQL SMRNFELFRN IEPTEYIDDL
FKLRSKTSCA NLKKFEEVIN QETFWVASEI LRETNQLKRM KTIKHFIKIA LHCRECKNFN
SMFAIISGLN LAPVARLRTT WEKLPNKYEK LFQDLQDLFD PSRNMAKYRN VLNSQNLQPP
IIPLFPVIKK DLTFLHEGND SKVDGLVNFE KLRMIAKEIR HVGRMASVNM DPALMFRTRK
KKWRSLGSLS QGSTNATVLD VAQTGGHKKR VRRSSFLNAK KLYEDAQMAR KVKQYLSNLE
LEMDEESLQT LSLQCEPATN TLPKNPGDRK PVKADTSPVA PRAGLQPKPP PQAPQPSQRP
SPGLQLPAVP LYPSRKKVPL RDLPPFGINS PQALKKILAL SEEGSLERHK RPAEDTVSDA
SSRFSSPPTS PQSSPRKGYT LAPSGTVDNF SDSGHSEISS RSSIVSNSSF DSLPVSLPDE
RRQRPSVGTV ETSLAAGRPE RRPAGEPDQC SLGSCAPLSE SRGLYAAATV ISSPSTEELS
QDQGDRASLD AADSGRGSWT SCSSGSHDNI QTIQQQRSWE TLPFGHTHFD YSGDAAGLWA
SSSHVDQIMF SDHSTKYNRQ SQSRESLDQA QSRASWASST GYWGEDSEGD TGTIKRRGGK
DVSLEAESSS MMSASAEEAK PVAMAAHVAV PPSATKGLIA RKEGRYREPP PTPPGYVGIP
ITDFPDAHPH PARKPPDYTV ALQRSRMLAR PAETPAPGGA RPTPRPQWHR PGDDPRPGPC
APPGLATEED EDEQVSAV
//
