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Database: UniProt
Entry: Q6DCK3
LinkDB: Q6DCK3
Original site: Q6DCK3 
ID   GRP2B_XENLA             Reviewed;         594 AA.
AC   Q6DCK3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   29-OCT-2014, entry version 82.
DE   RecName: Full=RAS guanyl-releasing protein 2-B;
GN   Name=rasgrp2-b;
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=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as a calcium- and DAG-regulated nucleotide
CC       exchange factor specifically activating Rap through the exchange
CC       of bound GDP for GTP. May function in cell aggregation and
CC       adhesion. {ECO:0000250|UniProtKB:Q7LDG7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Cell junction, synapse, synaptosome {ECO:0000250}. Note=Found both
CC       in the cytosol and associated with membranes. {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}.
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DR   EMBL; BC078012; AAH78012.1; -; mRNA.
DR   RefSeq; NP_001087119.1; NM_001093650.1.
DR   UniGene; Xl.14799; -.
DR   ProteinModelPortal; Q6DCK3; -.
DR   GeneID; 447008; -.
DR   KEGG; xla:447008; -.
DR   CTD; 447008; -.
DR   Xenbase; XB-GENE-986629; rasgrp2.
DR   HOVERGEN; HBG007513; -.
DR   KO; K12361; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
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: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; -; 3.
DR   Gene3D; 1.10.840.10; -; 1.
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; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR023578; Ras_GEF_dom.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF13202; EF-hand_5; 2.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00054; EFh; 2.
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; 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 junction; Cell membrane; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Membrane; Metal-binding; Repeat;
KW   Synapse; Synaptosome; Zinc; Zinc-finger.
FT   CHAIN         1    594       RAS guanyl-releasing protein 2-B.
FT                                /FTId=PRO_0000315612.
FT   DOMAIN        3    121       N-terminal Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00135}.
FT   DOMAIN      149    382       Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00168}.
FT   DOMAIN      418    453       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      447    482       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND     431    442       1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND     460    471       2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   ZN_FING     490    540       Phorbol-ester/DAG-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00226}.
SQ   SEQUENCE   594 AA;  68338 MW;  8B6CC286623B8EBB CRC64;
     MDSSDLDKGL TIDEIIAKCI QSFDKDGKLS DPKLVQMFLM MHPWYIPSGD LAKKLFALSE
     SGDNVERERI CQFVRFWISE FPAEFDLNPE LGEQIRDLKR ALENKGNRRE SSLIDIESVP
     SYGWKRQVTQ RGPGGGRVRK TSLLFDHLDP AELAEHLTHL EFHSFSKILF QDYHSFVLHG
     CTVGNPVLER FIALFNGVSQ WIQLMVLSKH TPQQRAAVIK QFVQVAERLL QMQNFNTLMS
     VVGGLSHSSI SRLKDTQSHI SPETTKVYDS LLELLTSSDN YARYRRRFAT CKGFRFPALG
     VHLKDLMALH VALPDWADKA KTIINISKMR QVYKVVHELT EAQRLEPPVK ANPDLLNLLT
     VSLDQYRSEE EIYQLSLQRE PRARSTQTHA KSPPSPSPPL EEWASLKAKP DQALLCQHIE
     KMVESVFRLF DEDGDGHISQ EEFQSVRSNF PYLCAFNEID QNQDGKISKQ EMTSYFLRAS
     SVLDCKMGFI HNFAERTFLR PVSCQHCRNL ILGIYKKGLK CKACGITCHK HCRDHLSIEC
     KKRSKSVSER GESMEKGRHF FFTLPRSFRR STLYPDLREE EPHMEDDGVF DDHL
//
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