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Database: UniProt
Entry: A0A3Q3MXB8_9TELE
LinkDB: A0A3Q3MXB8_9TELE
Original site: A0A3Q3MXB8_9TELE 
ID   A0A3Q3MXB8_9TELE        Unreviewed;      1637 AA.
AC   A0A3Q3MXB8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
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|Ensembl:ENSMAMP00000024874.2};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000024874.2, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000024874.2}
RP   IDENTIFICATION.
RG   Ensembl;
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   Ensembl; ENSMAMT00000025516.2; ENSMAMP00000024874.2; ENSMAMG00000016541.2.
DR   GeneTree; ENSGT00940000156418; -.
DR   Proteomes; UP000261640; 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:UP000261640};
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..355
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          422..536
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          771..857
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          882..1109
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   REGION          195..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1169..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1242..1329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1365..1402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1452..1637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..251
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1186..1201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1256..1279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1287..1307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1386..1402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1469..1483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1485..1510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1532..1583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1637 AA;  182166 MW;  CA14AC3AC25EAB47 CRC64;
     MASYVDNSFR QAVMMNPAER TQQDLEIVYS YLHGMEALSN LREHQLRMMC ETVRYERHEA
     NEVLYYPDDI GSCWYILLSG SVFIKESMFL PRSSFGKRSA GSLRRGCECI VLEPSEMIVV
     DYMDENEEYF QRQASHRQSR RRFRKINQKG ERQTIIDTVD PYPTGKPPIA RGYHTLPADF
     SRLHLADGLH PQVTHVSSSH SGCSITSDSG SSSLSDIYQA TENEPGDMDL SGLPETAVDS
     EEDDDEEDIE RASDPLMSRD IVRDCLEKDP MDRTDDDIEQ LLEFMHQLPA FANMTMSVRR
     ELCAVMVFAV VERAGTIVLN DGEELDSWSV ILNGSVEVTY PDSRTEILCM GNSFGVSPTM
     EKEYMKGVMK TKVDDCQFVC IAQQDYCCIL NQVEKNMQKV EEEGEIVMVK EHRELDRTGT
     RKGHIVIKGT PERLTMHLVE EHSVVDPTYI EDFLLTYRTF LSSPMVVGKK LLEWFHDPSL
     RDKVTRVVLL WVNNHFNDFE GDPAMTHFLE EFENNLEKEK MCGHLRLLNI ACAAKAKPRQ
     VTLTKPSRDS PLAFSLLGGQ EKGFRIFIDA VDPGSKAAEA GLKRGDQILE VNGQNFENVQ
     LSKANEILKN NTHLSITVKT NLLVFKELLT RPEQDHDLDG EDEHDRKNGA PHLPKIGDIK
     KASRYSIPDL AVDVEQVMGL EKVSKKAKTN TVGGRNKLKK IFDKTLTSIL PPKPYNDVCV
     GQSQDDSIVG MKQSKQIPPA LPVSGNLSSS NPDLLQSHHR ILDFNNQPDM SDQVLRVFKA
     DQQSRYIMIG KDTTAKEVVA QAIREFALTA APEAYSLCEV SVTPEGVIKQ RRLPDQLSKL
     ADRIQLSGRY YLKSNMETET LCSDEDAQDL LREGQISLLQ LSTVEVATQL SMRAFELFCA
     IEPTEYIDDL FKLRSKTGSA SLKRFEEAIN HETFWVATEV TREPNQLKRM KTIKHFIKIA
     LHCRECKNFN SMFAIISGLN LAPVSRLRGT WEKLPSKYEK LFGDLQDLFD PSRNMAKYRN
     VLNNQNLQPP IIPLFPVIKK DLTFLHEGND SKVDGLVNFE KLRMIAKEIR HVGRMASVNM
     DPALMFRTRK KKWRSLGSLS QGSANAAVLD VTQTGGHKKR VRRSSFLNAK KLYEDAQMAR
     KVKQYLSNLS LETNEESLQT LSLQCEPSIS TLPKNAGGKR PDTSPVVSRA ANQQRGQLAK
     GNQALQVPAV ALYPSRKKVP VKDLPPFGTS SPQSLKKILS LSEEGSDRHR RQPEDTVSNA
     SSQLFSPPTS PQSSPKKGYR MGDTYSDSGH SEISSRSSLV SNSSFDMAQE ERRLRHSGGI
     GEAHIGGARL ERRATTDPDQ YSLGSYSSMQ DCRGIYVGCP TVLSSPSSEE LTQDQGDRVS
     LDAADSGRGS WTSCSSGSHD NIQTMQQGRS WETLAFGVGG GGIGGLPPGG PEALLGGPAA
     LWAAQARGSW ASASSSSSSA AYWGEDSEGD TGTIKRRGGK DVSADPETSS ITSTGSEEAK
     QHSRPSPSPI TTGARKEGRY REPPPTPPGY TALSISDLSE GQHPVPSVPT STVTHSGRRP
     PDYTTALQRS RMVTQSPDSH QAHQVAKQRV GGLHRTRSPA EEQGPEEEEE GESLSSKVIA
     LKKPKPLAQH TPETPRQ
//
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