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Database: UniProt
Entry: A0A3B5A896_9TELE
LinkDB: A0A3B5A896_9TELE
Original site: A0A3B5A896_9TELE 
ID   A0A3B5A896_9TELE        Unreviewed;      1603 AA.
AC   A0A3B5A896;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ENSSPAP00000017638.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000017638.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000017638.1}
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   STRING; 144197.ENSSPAP00000017638; -.
DR   Ensembl; ENSSPAT00000017912.1; ENSSPAP00000017638.1; ENSSPAG00000013176.1.
DR   GeneTree; ENSGT00940000156418; -.
DR   Proteomes; UP000261400; 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   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          3..50
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          262..327
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          394..508
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50212"
FT   DOMAIN          512..582
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          748..834
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          859..1086
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   REGION          167..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1218..1320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1341..1378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1390..1411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1426..1603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..223
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1164..1178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1233..1254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1266..1285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1364..1378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1428..1444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1449..1463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1465..1481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1530..1568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1588..1603
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1603 AA;  177860 MW;  3F40FF9311533ED5 CRC64;
     MEALSNLREH QLRIMCETVR YERHEANEVL YYPDDIGSCW YILLSGSVFI KESMFLPRSS
     FGKRSAGSLR RGCECIVLEP SEMIVVDYMD ENEEYFQRQA SHRQSRRRFR KINQKGERQT
     IIDTVDPYPT GKPPIARGYH TECNKPQLPA DFSRLHLADG LHPQVTHVSS SHSGCSITSD
     SGSSSLSDIY QATENEPGDM DLSGLPETAV DSEEDDDEED IERASDPLMS RDIVRDCLEK
     DPMDRTDDDI EQLLEFMHQL PAFANMTMSV RRELCAVMVF AVVERAGTIV LNDGEELDSW
     SVILNGSVEV TYPDSRTEIL CMGNSFGVSP TMEKEYMKGV MKTKVDDCQF VCIAQQDYCC
     ILNQVEKNMQ KVEEEGEIVM VKEHRELDRT GTRKGHIVIK GTPERLTMHL VEEHSVVDPT
     YIEDFLLTYR TFLSSPMVVG KKLLEWFHDP SLRDKVTRVV LLWVNNHFND FEGDPAMTHF
     LEEFENNLEK EKMCGHLRLL NIACAAKAKP RLVTLTKPSR DSPLAFSLLG GQEKGFRIFI
     DAVDPGSKAA EVGLKRGDQI LEVNGQNFEN VQLSKANEIL KNNTHLSITV KTNLLVFKEL
     LTRPEHDHDL DGEEEHDRKN GAPHLPKIGD IKKASRYSIP DLAVDVEQVM GLEKVSKKAK
     TNTVGGRNKL KKIFDKTLTS ILPPKPYNDV CVGQSQDDSI VGMKQSKQIP PALPVSGNLS
     SSNPDLLQSH HRILDFNNQP VPVTLNMSDQ VLRVFKADQQ SRYIMIGKDT TAKEVVAQAI
     REFALTAAPE AYSLCEVSVT PEGVIKQRRL PDQLSKLADR IQLSGRYYLK SNMETETLCS
     DEDAQDLLRE GQISLLQLST VEVATQLSMR AFELFCAIEP TEYIDDLFKL RSKTGSASLK
     RFEEAINHET FWVATEVTRE PNQLKRMKTV KHFIKIALHC RECKNFNSMF AIISGLNLAP
     VSRLRGTWEK LPSKYEKLFG DLQDLFDPSR NMAKYRNVLN NQNLQPPIIP LFPVIKKDLT
     FLHEGNDSKV DGLVNFEKLR MIAKEIRHVG RMASVNMDPA LMFRTRKKKW RSLGSLSQGS
     ANAAVLDVTQ TGGHKKRVRR SSFLNAKKLY EDAQMARKVK QYLSNLSLET NEESLQTLSL
     QCEPSISTLP KNAGGKRPDT SPVVPRAASQ QRGQLAKGNQ ALQVPAVALY PSRKKVPVKD
     LPPFGTSSPQ SLKKILSLSE EGSERHRRQP EDTVSNASSQ LSSPPTSPQS SPKKGYNRMG
     DAYSDSGHSE ISSRSSLVSN SSFDMAQEER RLRHSGGVGE SHIGGPRLER RATTDPDQYS
     LGSYSSMQDC RGIYAGCPTV LSSPSSEELT QDQGDRVSLD AADSGRGSWT SCSSGSHDNI
     QTMQQGRSWE TLAFGGGGGG GGIGGLPPGG PEALLGGPAA LWAAQARGSW ASASSSSSSA
     AYWGEDSEGD TGTIKRRGGK DVNADPETSS ITSTGSEEAK QLGRPSPSPI TAGGKGLISR
     KESRYREPPP TPPGYTALTI SDLAEGQHPA PSVPTSTATH SGRRPPDYTT ALQRSRMVTQ
     SPDSHQAHQG AKQRAGGLHR TRSPAEEQEP EEEEEEDEQV SAV
//
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