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 01-MAY-2013, entry version 74.
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 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Cell
CC membrane; Peripheral membrane protein (By similarity). Cell
CC junction, synapse, synaptosome (By similarity). Note=Found both in
CC the cytosol and associated with membranes (By similarity).
CC -!- SIMILARITY: Belongs to the RASGRP family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC -!- SIMILARITY: Contains 1 Ras-GEF domain.
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; BC078012; AAH78012.1; -; mRNA.
DR RefSeq; NP_001087119.1; NM_001093650.1.
DR UniGene; Xl.14799; -.
DR HSSP; Q62768; 1Y8F.
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:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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-like_dom.
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; IPR008937; Ras_GEF.
DR InterPro; IPR023578; Ras_GEF_dom.
DR InterPro; IPR001895; RasGRF_CDC25.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF13202; EF_hand_3; 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; Ras_GEF; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00720; RASGEF; FALSE_NEG.
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.
FT DOMAIN 149 382 Ras-GEF.
FT DOMAIN 418 453 EF-hand 1.
FT DOMAIN 447 482 EF-hand 2.
FT CA_BIND 431 442 1 (Potential).
FT CA_BIND 460 471 2 (Potential).
FT ZN_FING 490 540 Phorbol-ester/DAG-type.
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
//
