GenomeNet

Database: UniProt
Entry: Q6NTL4
LinkDB: Q6NTL4
Original site: Q6NTL4 
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   01-OCT-2014, entry version 82.
DE   RecName: Full=RAS guanyl-releasing protein 1;
GN   Name=rasgrp1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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
CC       of bound GDP for GTP. {ECO:0000250}.
CC   -!- ENZYME REGULATION: Regulated by F-actin polymerization and
CC       probably by calcium. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Golgi apparatus membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Note=Found both in the cytosol and associated with membranes.
CC       {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
CC       functional activation through DAG-binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RASGRP family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 EF-hand domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00448}.
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00135}.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00226}.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00168}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC068947; AAH68947.1; -; mRNA.
DR   RefSeq; NP_001084532.2; NM_001091063.1.
DR   UniGene; Xl.46699; -.
DR   ProteinModelPortal; Q6NTL4; -.
DR   GeneID; 414479; -.
DR   KEGG; xla:414479; -.
DR   CTD; 10125; -.
DR   Xenbase; XB-GENE-489815; rasgrp1.
DR   HOVERGEN; HBG007513; -.
DR   KO; K04350; -.
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:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.238.10; -; 1.
DR   Gene3D; 1.10.840.10; -; 1.
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; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR023578; Ras_GEF_dom.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF13405; EF-hand_6; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF48366; SSF48366; 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; Repeat;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    791       RAS guanyl-releasing protein 1.
FT                                /FTId=PRO_0000316981.
FT   DOMAIN       49    172       N-terminal Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00135}.
FT   DOMAIN      201    432       Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00168}.
FT   DOMAIN      466    501       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      493    528       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND     479    490       1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND     506    517       2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   ZN_FING     537    587       Phorbol-ester/DAG-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00226}.
FT   REGION       53    106       Ras exchanger motif region; required for
FT                                transforming activity. {ECO:0000250}.
FT   COILED      728    783       {ECO:0000255}.
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
//
DBGET integrated database retrieval system