GRP1_XENLA
ID GRP1_XENLA Reviewed; 791 AA.
AC Q6NTL4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=RAS guanyl-releasing protein 1;
GN Name=rasgrp1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) 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; BC068947; AAH68947.1; -; mRNA.
DR RefSeq; NP_001084532.2; NM_001091063.1.
DR AlphaFoldDB; Q6NTL4; -.
DR SMR; Q6NTL4; -.
DR PRIDE; Q6NTL4; -.
DR DNASU; 414479; -.
DR GeneID; 414479; -.
DR CTD; 414479; -.
DR Xenbase; XB-GENE-489815; rasgrp1.L.
DR OrthoDB; 355412at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 414479; Expressed in spleen and 18 other tissues.
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; 3.
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_0000316981"
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 671..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 728..783
FT /evidence="ECO:0000255"
FT COMPBIAS 671..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; 90172 MW; CA0A023D63B8469E CRC64;
MGTVGKKKDR PAHGCSTIPK LALELKQIIH STTHPKVPAV TPLRVMMPLG KLSKGASLDE
LIQMCIQAFD LDGNMGQNNE LLQIMLTMHG FLIPSTELLI KLRTLYQDAM QNRSFSFCLR
ICYFIRYWIT ELWVMFKMDA KLTQTMEEFQ ELVRSHGEEL HWRLIDTAQI NSRDWSRKLT
QRIQSNCSKK RKVSLLFDHL EPQELAEHLT YLEFKAFRRI SFSDYQNYIV NGCVKDNPTM
ERSIALCNGI SQWVQLMVLS RPTPQLRAEV LTKFIHVAQK LHQLQNFNTL MAVIGGLCHS
SISRLKDTSS HVSHDVTKVL NEMTELLSSC RNYDNYRRAY NECTNFKIPI LGVHLKDLIA
LHEAMPDFLE ESKINVPKLH SLYNHINELI QLQNIAPPLE ANMDLVHLLT LSLDLYYTED
EMYELSYARE PRNYRAPPVT PSKPPVVADW ASGVSPKPDP KTISKHVQRM VDSVFKNYDL
DQDGYISQEE FEKIAASFPF SFCVMDKDRE GLISRQEITA YFMRASSICS KLGLGFLHNF
QETTYLRPTF CDNCAGFLWG VIKQGYRCKD CGMNCHKQCK ELVVFECKKR SKCSMGENNT
LSDAGQLEVI PAGGKGLTND CLGADEGPYS YPNGDGDIHT EVSKDRTIML MGSSAQKISV
RLQPAVKHRA TQTENETQSL CLQVPSPPRS RTPDLTSHLP ISPMPSPCPS PVPTRKKAYA
KWENKDSIRK ARAELRGGKA GIQELEKEKV FLKEENTALK IQLKDAHRRV ETLRAELRKY
VLDSDTHQKG S
