ID A0A3Q0GI61_ALLSI Unreviewed; 1653 AA.
AC A0A3Q0GI61;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_025059361.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025059361.1};
RN [1] {ECO:0000313|RefSeq:XP_025059361.1}
RP IDENTIFICATION.
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_025059361.1; XM_025203576.1.
DR Proteomes; UP000189705; 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; 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:UP000189705};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 15..62
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 274..374
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 406..519
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 524..594
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 745..831
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 856..1083
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..235
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1653 AA; 185105 MW; 14C8052909E82BAD CRC64;
MDLEIVYSYL HGMEALSNLR EHQFRLMCET VRYERHEANE VLYYPDDIGT CWYILLSGSV
FIKESMFLPR SSFGKRSAGS LRRGCECIVL EPSEMIVVDY MDENEEYFQR QASHRQSRRR
FRKINQKGER QTIIDTVDPY PVGKPPLPRG YHTECTKPQL PADFTKLHLT DSLHPQVTHV
SSSHSGCSIT SDSGSSSLSD IYQATESEAG DMDLSGLPET AVDSEDDDDE EDIERASDPL
MSRDIVRDCL EKDPIDRTDD DIEQLLEFMH QLPAFANMTM SVRRELCAVM VFAVVERAGT
IVLNDGEELD SWSVILNGSV EVTYPDGRME ILCMGNSFGV SPTLDKEYMK GVMRTKVDDC
QFVCIAQQDY CRILNQVEKN MQKVEEEGEI VMVKEHRELD RTGTRKGHIV IKGTAERLTM
HLVEEHSVVD PTFIEDFLLT YRTFLSSPMD VGKKLLEWFS DPSLRDKVTR VVLLWVNNHF
NDFEGDPAMT QFLEEFENNL EREKMGGHLR LLNIACAAKA KRRLITLTKP SREAPLPFIL
LGGSEKGFGI FVDSVDFGSK ATEAGLKRGD QILEVNGQNF ENIQLSKALE ILRNNTHLSI
TVKTNLFVFK ELLTRLSEEK RNGAPHLPKI GDIKKASRYS IPDLAVDVEQ VIGLEKVNKK
SKANTVGGRN KLKKILDKTR ISILPQKPYN DIGIGQSQDD SIVGLRQTKH IPPALPVSGT
LSSSNPDLLQ SHHRILDFNT TPDLPDQVLR VFKADQQSRY IMISKDTTAK EVVIQAIREF
ALTATPDAYS LCEVSVTPEG VIKQRRLPDQ LSKLADRIQL SGRYYLKNNM ETETLCSDED
AQELLRESQI SLLQLSTVEV ATQLSMRNFE LFRNIEPTEY IDDLFKLKSK SGCTNLKKFE
EVINQETFWV ASEILRETNQ LKRMKIIKHF IKIALHCREC KNFNSMFAII SGLNLAPVAR
LRTTWEKLPS KYEKLFQDLQ DLFDPSRNMA KYRNVLNSQN LQPPIIPLFP VIKKDLTFLH
EGNDSKVEGL VNFEKLRMIA KEIRHVGRMA SVNMDPALMF RTRKKKWRSL GSLSQGSTNA
AVLDVAQTGG HKKRVRRSSF LNAKKLYEDA QMARKVKQYL SNLDLEMDEE SLQTLSLQCE
PATNTLPKNP GDKRSGKSET SPVAPRAGTQ QKTQQQHKVN QALQVPAVSL YPSRKKVPVK
DLPPFGINSP QALKKILSLS EEGSLERHKK QAEDTISNAS SQMSSPPTSP QSSPRKGGSG
NQLRSYGSRL SDLTSSSSSL GSYTLAPSGT VDNFSDSGHS EISSRSSIVS NSSFDSMPIS
LHDERRQRHS VSIVETNLGV GRIDRRTMIE PDQYSLGSYA PLSENRGLYA GATVLSSPST
EELSQDQGDR ASLDAADSGR GSWTSCSSGS HDNIQTIQHQ RSWETLPFGH AHFDNAGDGA
GLWASGSHMD QMMFPDHGPK YGRQSQGREG LDQAQSRASW ASSTGYWGED SEGDTGTIKR
RGGKDVSIEA ETSSITSVTA EETKPASMPA HIAVSSSSAK GLIARKEGRY REPPPTPPGY
VGIPIADFAE SISHPARKPP DYNIALQRSR MMARTCESHG SSTSQQQSHG HSASRPVNKP
QWHKPNESDP RLAHYQSQGF STEEDEDEQV SAV
//
