GRP4_BOVIN
ID GRP4_BOVIN Reviewed; 673 AA.
AC Q1LZ97; Q58D14;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=RAS guanyl-releasing protein 4;
GN Name=RASGRP4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Recruited to membranes upon activation by DAG.
CC {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46630.1; Type=Frameshift; Evidence={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; BT021783; AAX46630.1; ALT_FRAME; mRNA.
DR EMBL; BC116130; AAI16131.1; -; mRNA.
DR RefSeq; NP_001030456.2; NM_001035379.2.
DR AlphaFoldDB; Q1LZ97; -.
DR SMR; Q1LZ97; -.
DR STRING; 9913.ENSBTAP00000042303; -.
DR PaxDb; Q1LZ97; -.
DR PRIDE; Q1LZ97; -.
DR GeneID; 529375; -.
DR KEGG; bta:529375; -.
DR CTD; 115727; -.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_019261_2_1_1; -.
DR InParanoid; Q1LZ97; -.
DR OrthoDB; 355412at2759; -.
DR TreeFam; TF312918; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR020454; DAG/PE-bd.
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 PRINTS; PR00008; DAGPEDOMAIN.
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; 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; Differentiation;
KW Guanine-nucleotide releasing factor; Membrane; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..673
FT /note="RAS guanyl-releasing protein 4"
FT /id="PRO_0000315212"
FT DOMAIN 49..172
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..590
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 74824 MW; DC8FF23ED85840AA CRC64;
MNRKDSKRKS HQECPVKTGG RGRPRQARRH KTCPSPREIS KVMASMALGM LNEGGCSEDE
LLEKCIQSFD SAGSLRRGDH VLNMVLAMHS WVLPSAHFAA RLLTLYQEAT GSTQELRRLQ
ICHLVRYWLT QHPETMHQDP QLEEVIGRFW ATVEQEGNSV QQSLGDFSSR LSPGGPGPPH
PMSSPGLGKK RKVSLLFDHL ETGELAEHLT YLEFRSFQAI TPQDLRDYVL QGSVRGCPTL
EGSVGLSNSV SRWVQVMVLS RPGPAQRAQV LDKFIQVAQK LLQLHNFNTL MAVTGGLCHS
AISRLKDSHA HLSPDSTKAL LELTELLAAH NNYARYRRTW AGCMDFRLPV LGVHLKDLVA
LNEAQPDRLP DGRLHLPKLN SLYLRLQELA ALQQQHPPGN ASEDLLHLLT LSLDLFYTED
EIYELSYARE PRCPKSLPPS PFKAPLVVEW APGVTPKPDT VTLGRHVEQL VESVFKNYDP
DGRGTISQED FERLSGNFPF ACHGLHPPPC QGSGSFSREE LTGYLLRASA ICSKLGLAFL
HTFQEVTFRK PTFCNSCSGF LWGVTKQGYR CRDCGLCCHR HCRDQVKVEC KKRPGAKGDA
SPPEAPVPPT PVPQASCGSE DNLSYTLSLE PETGCHVRHA WTQTESPHPS WEPETVPLPA
KASPPTESSK LNS
