ID H2SR65_TAKRU Unreviewed; 1576 AA.
AC H2SR65;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Rap guanine nucleotide exchange factor 6 {ECO:0000313|Ensembl:ENSTRUP00000014902.3};
GN Name=rapgef6 {ECO:0000313|Ensembl:ENSTRUP00000014902.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000014902.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000014902.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000014902.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC -!- SIMILARITY: Belongs to the RAPGEF2 family.
CC {ECO:0000256|ARBA:ARBA00010829}.
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DR STRING; 31033.ENSTRUP00000065283; -.
DR Ensembl; ENSTRUT00000014970.3; ENSTRUP00000014902.3; ENSTRUG00000006132.3.
DR GeneTree; ENSGT00940000158124; -.
DR HOGENOM; CLU_002782_0_1_1; -.
DR Proteomes; UP000005226; Chromosome 15.
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; 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; 1.
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:SF4; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 6; 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; 1.
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; 1.
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 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 Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT DOMAIN 233..333
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 365..478
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 483..553
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 703..789
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 814..1042
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 175472 MW; 21710B132A10603A CRC64;
HTIYCHLYHM DVLSHLREHQ LSPDSIATCW YILLSGSVFV KEHMYLARCC FGRQLGGRRG
CECITLEPSE MIVVSWDDSF LQREGSQRRS RRRFRRINPR GERELITDGQ EPSGYTKLPG
DLNKMHLTDH AHQQVMHVPP SQSGCSIASD SGSSSLSDIY QATESELGDV DLSGLPEAVV
DSEEDEEEDE DLERASDTLL GRDLVRECLE KDPVDRNDDD IEQLLEFMHQ LPAFANMTMS
VRRELCSVMV FEVVEQAGTV ILHNKQELDL WYVILNGAVE FSYPDGRMET LCMGNSFGIS
PSLDKQYMNG EVRTKGDDCQ FVCIAQEDYW RILNHVEKNT HKVEEEGEIV MVKEHRELDR
SGTRKGHIVI KGTPDRLIMH LVEEPSVVDP TYIEDFLLTH RTFLSNPMDV GKKLFEWFQV
DTLRDTVTRI VLLWVNNHFN DFEGNPAMTR FLEDFEKLLE TTKMKGHLRL LNIACAAKAK
LRQITLQKAS RDSPLHFSVQ GGSERGFGVF VDSVEEGSKA AETGLKRGDQ IMEVNGQNFD
NISITKAVDI LRNNTHLSLT IKTNIFVFKE LLSRVMHEKK NGGPHIPKIQ EKKGNRFSIP
DLPGDMEFPS DHKSNRKLKA NTVSGGRNKI RKMLEKTRFS ILPPKPFSDG GMVQSQDDSI
VGTKQCRHSV AIMPIPGNLS SSSPDLLQPA TSVLDFSNPA DIPDQVIRVF KADQQSCYII
ISKDTTAKDV VAHTVNEFGL VAAPETYSLC EVSVSPEGVI KQRRLPDQLS KLADRIQLNG
RYYLKNNMET ETLCSDEDAQ DLLRESQISL LQLSTMEVAA QLSMRDFDLF RNIESTEYVD
DLFKLDTSIG SGNLKQFEEV INKETFWVAS EILKEPNALK RMKTIKHFIK IALHCRECKN
FNSMFAIISG LNLAPVARLR SSWEKLPSKY EKLFGDLQDV FDPSRNMAKY RNILSSQSMQ
PPIIPLFPVV KKDLTFLHEG NDSTVDGLVN FEKLRMIAKE IRHVVRLTSA NMDPALMFRQ
RSLSQGSTNS NMLDVQGGAH KKRVRRSSLL NAKKLYEDAQ MARKVKQYLS NLTVETDEEK
HQVMSLLCEP SYSTLSKYLS ERRSTKSDMS PVSLRSALPS AKTQNRVSQV LQVQVPLNHL
RKKSTAKDTD SNSPQVVKKP PVSSSEEWSS KRPSDDAVSL ISSLHSSPTV SPHGSPRKGY
AFLPASKADN LSDSSHSEIS SRSSICSVDS MPAPGPDDRC SSGNRTAAGA AMPSPAAVAD
GTAATYTHSN ADYSQPSYVP RGSTFTSSAS TEELTPDHAS LDSVADSGRS SWTSCSSNSH
DSFQSLPPSS CRPWDHGIHG HPLAWMNEDA AAKQHSRNSS SDLSNQSRQS WASSSSLSDT
YEGNYGTIKR RNTAEHPSSP TSEEGGQSTD HVYKTVTSST EKGLIVYCVT SPAKDERYRA
PPPTPPGYQG LALGDLGLGP RPPHLRPPDY SVALQRSKLL QSPGASGGLA ELKNKRHLAP
PIAKSTLCTR TTCTPNVLTP QGRRGPCKCV HSGAGATRLI FLSYLKATKQ ANGPASPSPA
GVPFRVRFVK YLKVLL
//
