GRP2A_XENLA
ID GRP2A_XENLA Reviewed; 594 AA.
AC Q32N25; Q7ZTN0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=RAS guanyl-releasing protein 2-A;
GN Name=rasgrp2-a;
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, and Lung;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) 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; BC044323; AAH44323.1; -; mRNA.
DR EMBL; BC108872; AAI08873.1; -; mRNA.
DR RefSeq; NP_001079563.1; NM_001086094.1.
DR AlphaFoldDB; Q32N25; -.
DR SMR; Q32N25; -.
DR DNASU; 379250; -.
DR GeneID; 379250; -.
DR KEGG; xla:379250; -.
DR CTD; 379250; -.
DR Xenbase; XB-GENE-6256357; rasgrp2.S.
DR OrthoDB; 355412at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 379250; Expressed in spleen and 14 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; 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; 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; 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; 3.
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; 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-A"
FT /id="PRO_0000315611"
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 447..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..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..594
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"
FT CONFLICT 558
FT /note="R -> H (in Ref. 1; AAH44323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 68118 MW; 6033C98F9563A504 CRC64;
MDSSDLDKGL TIDDIVVKCI QSFDKDGKLS DPEFVQMFLM MHPWYIPSGD LAKKLSALSE
SGDNVERERI CQLVRFWISE FPAEFDLNPE LGEQIRDLKR ALENKGNRRE SNLIDIESVP
SYGWKRQVTQ RGPSGGRVRK TSLLFDHLDP AELAEHLTHL EFHSFSKILF QDYHSFVLHG
CTVGNPVLER FIALFNGVSQ WIQLMVLSKH TPQQRAAVIK QFVQVAEKLL QLQNFNTLMS
VVGGLSHSSI SRLKDTQSHI SPETTKVFDS LLELLTSSDN YARYRRRFAT CEGFHFPALG
VHLKDLMALH VALPDWADKA KTIINISKMR QVYKVVHELT EAQRLEPPVK ANPDLLNLLT
VSLDQYRSEE EIYQLSLQRE PRARTTQTNA KSPPSPSPPL EEWASLKAKP DQALLCQHIE
KMVESVFRLF DEDGDGHISQ EEFQSVRSNF PYLCAFNEID QNHDGKISKQ EMTSYFQRAS
SVLDCKMGFI HNFAERTFLR PVSCQHCGNL ILGIYKKGLK CRACGITCHK HCKDHLSIEC
KKRSKSVSER GESMEKGRHF SFTLPRSFRR STLYPDLREE EPQLEEDGVF DDRL
