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Database: UniProt
Entry: A0A3Q7RYW5_VULVU
LinkDB: A0A3Q7RYW5_VULVU
Original site: A0A3Q7RYW5_VULVU 
ID   A0A3Q7RYW5_VULVU        Unreviewed;      1409 AA.
AC   A0A3Q7RYW5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Rap guanine nucleotide exchange factor 6 isoform X6 {ECO:0000313|RefSeq:XP_025850754.1};
GN   Name=RAPGEF6 {ECO:0000313|RefSeq:XP_025850754.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025850754.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025850754.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025850754.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025850754.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
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DR   RefSeq; XP_025850754.1; XM_025994969.1.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0005737; C: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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 1.
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   PANTHER; PTHR45161; CYTOSKELETON-ASSOCIATED PROTEIN 4; 1.
DR   PANTHER; PTHR45161:SF4; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 6; 1.
DR   Pfam; PF00027; cNMP_binding; 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; 1.
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   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW   ECO:0000256|PROSITE-ProRule:PRU00168};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT   DOMAIN          280..380
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          412..526
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50212"
FT   DOMAIN          530..600
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          749..835
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          860..1088
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1145..1174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1193..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1263..1283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1300..1368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1145..1161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1200..1214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1230..1250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1263..1282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1409 AA;  159390 MW;  2C339034F6EC06C0 CRC64;
     MNSPVDPGAR QALKKKPPER TPEDLNTIYS YLHGMEILSN LREHQLRLMS ARARYERYSG
     NQILFCSETV ARCWYILLSG SVLMKDSMVL PPCSFGKQFG GKRGCDCLVL EPSEMIVVEN
     SKDNEDSILQ REIPARQSRR RFRKINYKGE RQTITDDVDI NSYLSLPADL TKMHITDNPH
     PQVTHVSSSQ SGCSIASDSG SSSLSDIYQA TESEVGDVDL TRLPEGPVDS EDEEEEDEEI
     DRTDPLQGRD LVRECLEKEP ADKTDDDIEQ LLEFMHQLPA FANMTMSVRR ELCSVMIFEV
     VEQAGAIILE DGQELDSWYV ILNGTVEITH PDGKVENLFM GNSFGITPTL DKQYMHGVVR
     TKVDDCQFVC IAQQDYWRIL NHVEKNTHKV EEEGEIVMVH EHRELDRSGT RKGHIVIKAT
     PERLIMHLIE EHSIVDPTYI EDFLLTYRTF LESPLDVGIK LLEWFKIDSL RDKVTRIVLL
     WVNNHFNDFE GDPAMTRFLE EFEKNLEDTK MNGHLRLLNI ACAAKAKWRQ VVLQKASRES
     PLHFSLNGGS EKGFGIFVEG VEPSSKAADA GLKRGDQIME VNGQNFENIT FVKALEILRN
     NTHLALTVKT NIFVFKELLS RTEQEKSGVP HIPKIAEKKS NRHSIQDVPG DIEHTSQEKG
     NKKIKANTVS GGRNKIRKIL DKTRFSILPP KLFSDGGLSQ SQDDSIVGTR HCRHSLAIMP
     IPGTLSSSSP DLLQPTTSML DFSNPSDIPD QVIRVFKADQ QSCYIIISKD TTAKEVVCHA
     VHEFGLTGAS DTYSLCEVSV TPEGVIKQRR LPDQFSKLAD RIQLNGRYYL KNNMETETLC
     SDEDAQELVK ESQLSMLQLS TIEVATQLSM RDFDLFRNIE PTEYIDDLFK LDSKTGNTHL
     KEFEDIVNQE TFWVASEILT ESNQLKRMKI IKHFIKIALH CRECKNFNSM FAIISGLNLA
     SVARLRGTWE KLPSKYEKHL QDLQDLFDPS RNMAKYRNIL SSQSMQPPII PLFPVVKKDM
     TFLHEGNDSK VDGLVNFEKL RMIAKEIRQV VRMTSANMDP AMMFRQRSLS QGSTNSNMLD
     VQGGAHKKRA RRSSLLNAKK LYEDAQMARK VKQYLSSLDV DTDEEKFQMM SLQWEPAYGT
     LTKNLSEKRS AKSSEMSPVP MRSAGQTAKA HLHQPHRVSQ VLQVPAVNLH PIRKKGQAKD
     PATLSTNLPQ KVLGTTEEVS GKKHPEDTIS VASSLHSSPP ASPQGSPRKV GSILSDLSIL
     LRLSGSSSSP PRESSTKISG QSCPGIGGVY LQKKILQITR STAKRTDRTE KATEENRDRT
     SCENTARKRM TSPFRRFRER TLSRERLANS KKEDADHHQA TESCEKVKDV GSNIKDEKGS
     DIFNSNSRGN CNTLNCFYTR FKSKRRKTI
//
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