GRP4_RAT
ID GRP4_RAT Reviewed; 678 AA.
AC Q8R5I4; Q8R5I3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=RAS guanyl-releasing protein 4;
GN Name=Rasgrp4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=12217396; DOI=10.1016/s0161-5890(02)00076-7;
RA Li L., Yang Y., Stevens R.L.;
RT "Cloning of rat Ras guanine nucleotide releasing protein 4, and evaluation
RT of its expression in rat mast cells and their bone marrow progenitors.";
RL Mol. Immunol. 38:1283-1288(2002).
RN [2]
RP FUNCTION.
RX PubMed=12493770; DOI=10.1074/jbc.c200635200;
RA Li L., Yang Y., Stevens R.L.;
RT "RasGRP4 regulates the expression of prostaglandin D2 in human and rat mast
RT cell lines.";
RL J. Biol. Chem. 278:4725-4729(2003).
CC -!- FUNCTION: Functions as a cation- and diacylglycerol (DAG)-regulated
CC nucleotide exchange factor activating Ras through the exchange of bound
CC GDP for GTP. May function in mast cells differentiation.
CC {ECO:0000269|PubMed:12493770}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Recruited to membranes upon activation by DAG.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by mast cells and their progenitors (at
CC protein level). {ECO:0000269|PubMed:12217396}.
CC -!- DOMAIN: The phorbol-ester/DAG-type zinc finger mediates the binding and
CC the functional activation by DAG. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RASGRP family. {ECO:0000305}.
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DR EMBL; AF465263; AAL76250.1; -; mRNA.
DR EMBL; AF465264; AAL76251.1; -; mRNA.
DR RefSeq; NP_570837.2; NM_130824.2.
DR AlphaFoldDB; Q8R5I4; -.
DR SMR; Q8R5I4; -.
DR STRING; 10116.ENSRNOP00000046440; -.
DR PaxDb; Q8R5I4; -.
DR PRIDE; Q8R5I4; -.
DR GeneID; 170668; -.
DR KEGG; rno:170668; -.
DR UCSC; RGD:620476; rat.
DR CTD; 115727; -.
DR RGD; 620476; Rasgrp4.
DR eggNOG; KOG3417; Eukaryota.
DR InParanoid; Q8R5I4; -.
DR OrthoDB; 355412at2759; -.
DR PhylomeDB; Q8R5I4; -.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR PRO; PR:Q8R5I4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0009991; P:response to extracellular stimulus; ISS:UniProtKB.
DR CDD; cd00029; C1; 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; 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; PF00617; RasGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cytoplasm; Differentiation;
KW Guanine-nucleotide releasing factor; Membrane; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..678
FT /note="RAS guanyl-releasing protein 4"
FT /id="PRO_0000315215"
FT DOMAIN 49..175
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 201..432
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 466..501
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT ZN_FING 540..595
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 472
FT /note="E -> EK (in Ref. 1; AAL76251)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 678 AA; 75405 MW; 2E700F20953558DB CRC64;
MNRKDIKRKS HQECSGKAGG HGRPRQARRH KTCPTPREIS KVMASLNLGV LSESSCSVDE
LLEECIRCFD SAGSLHRGDH ILKMVLTMHS WVLPSSDLAA RLLTSYQKAA KDARELRQLQ
ICYLVRYWLT HHPEVVHQEP QLEAIINRFW TTVAQEGNMA QRSLGDASNL LSPGGPGPPP
LMSSPGLGKK RKVSLLFDHL ETEELAQHLT YLEFRSFQAI TPQDLRGYVL QGSVRGCPAL
EGSVGLSNSV SRWVQVMVLS RPGPAQRAQV LDKFIRVAQR LRQMQNFNTL MAVTGGLCHS
AISRLKDSHV HLSPDSTKAL LELTELLSSH NNYAYYRRTW ASCTDFRLPV LGVHLKDLVS
LYEAHPDRLP DGRLHLPKLN SLYLRLQELA ALQRQHPPCS ANEDLLHLLT LSLDLFYTED
EIYELSYARE PRCPKSLPLS PFKAPVVVEW AHGVTPKPDS ATLGQHVEQL VESVFKNYDP
EGHGSISLED FEKLSANFPF ACHGLHPPPR HGSGSFSREE LTKYLLHASA ICSKLGLAFL
HAFQEVTFRK PTFCHSCNGF VSTGPLWGVT KRGYRCQDCG LCCHRHCRDQ VRVECKKRPE
TKGDPGPPGA PGPATPLPPT GCGSEEGLSY TLSPHLESGC HLHHAWTQTE SSHSSWEPEM
VPCPAPVLPS KASSKSSV