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 27-MAR-2024, entry version 113. 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; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; 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 exchange CC factor specifically activating Rap through the exchange of bound GDP CC for GTP. May function in cell aggregation and adhesion. CC {ECO:0000250|UniProtKB:Q7LDG7}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse, CC synaptosome {ECO:0000250}. Note=Found both in the cytosol and CC associated with membranes. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RASGRP family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC078012; AAH78012.1; -; mRNA. DR RefSeq; NP_001087119.1; NM_001093650.1. DR AlphaFoldDB; Q6DCK3; -. DR SMR; Q6DCK3; -. DR DNASU; 447008; -. DR GeneID; 447008; -. DR KEGG; xla:447008; -. DR AGR; Xenbase:XB-GENE-986629; -. DR Xenbase; XB-GENE-986629; rasgrp2.L. DR OrthoDB; 4260488at2759; -. DR Proteomes; UP000186698; Chromosome 4L. DR Bgee; 447008; Expressed in spleen and 11 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; 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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR CDD; cd00051; EFh; 1. DR CDD; cd00155; RasGEF; 1. DR CDD; cd06224; REM; 1. DR Gene3D; 3.30.60.20; -; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1. DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1. DR InterPro; IPR046349; C1-like_sf. 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; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1. DR PANTHER; PTHR23113:SF16; RAS GUANYL-RELEASING PROTEIN 2; 1. DR Pfam; PF00130; C1_1; 1. DR Pfam; PF00036; EF-hand_1; 1. DR Pfam; PF13202; EF-hand_5; 1. DR Pfam; PF00617; RasGEF; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00054; EFh; 2. DR SMART; SM00147; RasGEF; 1. DR SMART; SM00229; RasGEFN; 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF48366; Ras GEF; 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; Cytoplasm; Guanine-nucleotide releasing factor; KW Membrane; Metal-binding; Reference proteome; Repeat; Synapse; Synaptosome; KW Zinc; Zinc-finger. FT CHAIN 1..594 FT /note="RAS guanyl-releasing protein 2-B" FT /id="PRO_0000315612" FT DOMAIN 3..121 FT /note="N-terminal Ras-GEF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135" FT DOMAIN 149..382 FT /note="Ras-GEF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168" FT DOMAIN 418..453 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 455..482 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT ZN_FING 490..540 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT REGION 377..403 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 431 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 433 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 435 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 437 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 442 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 460 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 462 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 464 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 466 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 471 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 //