GRP1_XENTR
ID GRP1_XENTR Reviewed; 791 AA.
AC A4IJ06;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=RAS guanyl-releasing protein 1;
GN Name=rasgrp1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a diacylglycerol (DAG)-regulated nucleotide
CC exchange factor specifically activating Ras through the exchange of
CC bound GDP for GTP. {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Regulated by F-actin polymerization and probably
CC by calcium. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi
CC apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Found both in the cytosol and
CC associated with membranes. {ECO:0000250}.
CC -!- DOMAIN: The phorbol-ester/DAG-type zinc finger is the principal
CC mediator of the targeting to membranes and is required for functional
CC activation through DAG-binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RASGRP family. {ECO:0000305}.
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DR EMBL; BC136226; AAI36227.1; -; mRNA.
DR AlphaFoldDB; A4IJ06; -.
DR SMR; A4IJ06; -.
DR PaxDb; A4IJ06; -.
DR eggNOG; KOG3417; Eukaryota.
DR InParanoid; A4IJ06; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008937; Ras-like_GEF.
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 PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00617; RasGEF; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Coiled coil; Cytoplasm; Differentiation;
KW Endoplasmic reticulum; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Membrane; Metal-binding;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..791
FT /note="RAS guanyl-releasing protein 1"
FT /id="PRO_0000316982"
FT DOMAIN 49..172
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 201..432
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 466..501
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 502..528
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT ZN_FING 537..587
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 53..106
FT /note="Ras exchanger motif region; required for
FT transforming activity"
FT /evidence="ECO:0000250"
FT REGION 683..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 728..785
FT /evidence="ECO:0000255"
FT COMPBIAS 683..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 481
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 508
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 791 AA; 90109 MW; AAC516D91CB02C5E CRC64;
MGTVGKKKDR PTHGCSTIPK LALELKQIIH STTHPKVPPV TPLRVMMPLG KLSKGASLDD
LIQMCIQAFD LDGNMGQNSE LLQIMLTMHG FLLPSTELLM KLRTLYQDAL QNRSFSFCLR
ICYFIRYWVT ELWVMFKMDA KLTQAMEEFQ ELVRSKGEEL HWRLIDTAQI NSRDWSRKLT
QRIKPNCSKK RKVSLLFDHL EPQELAEHLT YLEFKAFRRI SFSDYQNYIV SGCVKENPTM
ERSIALCNGI SQWVQFMVLS RPTPQLRAEV LTKFIHVAQK LHQLQNFNTL MAVIGGLCHS
SISRLKDTSA HVSHDVNKVL NEMTELLSSC RNYDNYRRVY NECTNFKIPI LGVHLKDLIA
LHEAMPDFLE DSKINVPKLH SLYNHINELI QLQNIAPPLE ANMDLVHLLT LSLDLYYTED
EMYELSYARE PRNHRAPPVT PSKPPVVADW ASGVSPKPDP KTISKHVQRM VDSVFKNYDL
DQDGYISQEE FEKIAASFPF SFCVMDKDRE GLISRQEITA YFMRASSICS KLGLGFLHNF
QETTYLRPTF CDNCAGFLWG VIKQGYRCKD CGMNCHKQCK ELVVFECKKR SKLSVGENSS
MFDSGQLEVI PAGGKGQTND CLGAEEGPYS YPNGDGDIHT EVSKDRTIML MGSSAQKISV
RLQPAVKHRA TQTENEPQSL CLQVPSPQRS RTPGLTSHLP ISPMPSPCPS PVPTRKKAYA
KWENKDSIRK ARAELRGGKA GIQELEKEKA LLKEENTTLK IQLKDAQRRV ETLRAELRKY
VLDSDVHQTG S
