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Database: UniProt
Entry: A0A1S3RQW0_SALSA
LinkDB: A0A1S3RQW0_SALSA
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ID   A0A1S3RQW0_SALSA        Unreviewed;      1652 AA.
AC   A0A1S3RQW0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 38.
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_014054716.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014054716.1};
RN   [1] {ECO:0000313|RefSeq:XP_014054716.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014054716.1};
RG   RefSeq;
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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the RAPGEF2 family.
CC       {ECO:0000256|ARBA:ARBA00010829}.
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DR   RefSeq; XP_014054716.1; XM_014199241.1.
DR   OrthoDB; 5473909at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa05.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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:SF2; CYCLIC NUCLEOTIDE RAS GEF; 1.
DR   PANTHER; PTHR45161; CYTOSKELETON-ASSOCIATED PROTEIN 4; 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:UP000087266}.
FT   DOMAIN          37..84
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          296..361
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          428..541
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50212"
FT   DOMAIN          546..616
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          780..866
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          891..1118
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   REGION          201..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1178..1215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1252..1355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1390..1409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1464..1652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..257
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1195..1213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1266..1287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1298..1319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1480..1494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1496..1510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1574..1606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1652 AA;  184126 MW;  6C6A605A2B3A6527 CRC64;
     MASYVDNSFR QAVMMNPAER TQQDLEIVYS YLHGMEALSN LREHQLRIMC ETVRYERHEA
     NEVLYYPDDV GSCWYILLSG SVFIKESMFL PRSSFGKRSA GSLRRGCECI VLEPSEMIVV
     DYMEENEEYF QRQASHRQSR RRFRKINQKG ERQTIIDTVD PYPTGKPPIV RGYHTECIKA
     QLPADFSRLH LADGLHPQVT HVSSSHSGCS ITSDSGSSSL SDIYQATENE PGDMDLSGLP
     ETAVDSEEDD DEEDIERSSD PLMSRDIVRD CLEKDPMDRT DDDIEQLLEF MHQLPAFANM
     TMSVRRELCA VMVFAVVERA GTIVLNDGEE LDSWSVILNG SVEVTYPEGR PEILCMGNSF
     GVSPTIEKEY MKGVMKTKVD DCQFVCIAQQ DYCCILNQVE KNMQKVEEEG EIVMVKEHRE
     LDRTGTRKGH IVIKGTKERL TMHLVEEHSV VDPTYIEDFL LTYRTFLSSP MVVGNKLLEW
     FHDPSLRDKV TRVVLLWVNN HFNDFEGDPA MTNFLEEFEN NLEREKMYGH LRLLNIACAA
     KAKLRLVTLT KPSREAPLAF TLLGGSEKGF RIFIDSVEPG SKAAEAGLKR GDQILEVNGQ
     NFENVQLTKA NEILRNNTHL SISVKTNLLV FKELLARPEH DHEAEGEETP EVDRKNGAPA
     HLPKIGDIKK GSRYSIPDLA VDVEQVMGLE KASKKAKANT VGGRNKLKKI FDKTLTSILP
     PKPYNDVGVG QSQDDSIVGL KQSKQIPAAL PVSGSLSSSN PDLLQSHHRI LDFNNPPDMS
     DQVLRVFKAD QQSRYIMIGK DTTAKEVVAQ AIREFALTAA PEAYSLCEVS ITPEGVIKQR
     RLPEQLSKLA DRIQLSGRYY LKSNMETETL CSDEDAQDLL REGQISLLQL STMEVATQLS
     MRAFELFCAI EPTEYIDDLF KLKSKTGSFC LKRFEEIINQ ETFWVASEVT REPNQLKRMK
     TVKHFIKIAL HCRECKNFNS MFSIISGLNL APVSRLRGTW EKLPSKYEKL FGDLQDLFDP
     SRNMAKYRNV LNNQNLQPPI IPLFPVIKKD LTFLHEGNDS KVDGLVNFEK LRMIAKEIRH
     VGRMASVNMD PALMFRTRKK KWRSLGSLSQ GSANAAVLDV TQTGGHKKRV RRSSFLNAKK
     LYEDAQMARR VKQFLSNLSL ETNEEALQTL SLQCEPSINT LPKNAGGSKR PDTSPVVSRA
     ASQQRSHLQK GNQALQVPAV ALYPSRKKVP VKDLPPFGTS SPQSLKKILS LSEEASERHK
     RQTEDTVSNT TSQLSSPPTS PQSSPKKGYP RTGDAYSDSG HSEISSRSSL VSNSSFDMAQ
     EERRGLRHSG GVGDPHAGGV RLERRATTDP DQYSLGSYSS MQDCRGLYTC ATVLSPSSEE
     LTQDQGDRVS LDAADSGRGS WTSCSSGSHD NIQTMQQGRS WETLAFGPGG VVSMGVHPPG
     GPEAFIGVPS GLWASQARGS WASASSSSSS AAYWGEDSEG DTGTIKRRGG KDVNADPETS
     SITSMGSDEA KQHGRPSPIT AGNKGLITRK ESRYREPPPT PPGYTALTIS DFSEGQTQSP
     PPPTAPSHSG RRPPDYSTAL QRSRMVTQSP DSQHHHQSQQ HPGSGTTKRH GLHRTRSPDE
     DEEPEEEEGE SLSPKLVALR KTVAHTPETT RP
//
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