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
//