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Database: UniProt
Entry: E1BG59_BOVIN
LinkDB: E1BG59_BOVIN
Original site: E1BG59_BOVIN 
ID   E1BG59_BOVIN            Unreviewed;       797 AA.
AC   E1BG59;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=RAS guanyl-releasing protein 1 {ECO:0000256|ARBA:ARBA00041172};
GN   Name=RASGRP1 {ECO:0000313|Ensembl:ENSBTAP00000029159.5,
GN   ECO:0000313|VGNC:VGNC:33747};
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 {ECO:0000313|Ensembl:ENSBTAP00000029159.5, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000029159.5, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000029159.5,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000029159.5}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000029159.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004395}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the RASGRP family.
CC       {ECO:0000256|ARBA:ARBA00009566}.
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DR   AlphaFoldDB; E1BG59; -.
DR   SMR; E1BG59; -.
DR   STRING; 9913.ENSBTAP00000029159; -.
DR   PaxDb; 9913-ENSBTAP00000029159; -.
DR   Ensembl; ENSBTAT00000029159.6; ENSBTAP00000029159.5; ENSBTAG00000021872.6.
DR   VEuPathDB; HostDB:ENSBTAG00000021872; -.
DR   VGNC; VGNC:33747; RASGRP1.
DR   eggNOG; KOG3417; Eukaryota.
DR   GeneTree; ENSGT00940000158910; -.
DR   HOGENOM; CLU_019261_0_0_1; -.
DR   InParanoid; E1BG59; -.
DR   OMA; CAKWENG; -.
DR   TreeFam; TF312918; -.
DR   Reactome; R-BTA-1169092; Activation of RAS in B cells.
DR   Reactome; R-BTA-354192; Integrin signaling.
DR   Reactome; R-BTA-392517; Rap1 signalling.
DR   Reactome; R-BTA-5673001; RAF/MAP kinase cascade.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000021872; Expressed in thymus and 89 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0019992; F:diacylglycerol binding; IEA:Ensembl.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0031210; F:phosphatidylcholine binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:Ensembl.
DR   GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IEA:Ensembl.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IEA:Ensembl.
DR   GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl.
DR   GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; IEA:Ensembl.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0032252; P:secretory granule localization; IEA:Ensembl.
DR   GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IEA:Ensembl.
DR   CDD; cd20860; C1_RASGRP1; 1.
DR   CDD; cd22290; cc_RasGRP1_C; 1.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 6.10.250.2730; -; 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; IPR020454; DAG/PE-bd.
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:SF174; RAS GUANYL-RELEASING PROTEIN 1; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00054; EFh; 1.
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; 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   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW   ECO:0000256|PROSITE-ProRule:PRU00168};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          53..176
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50212"
FT   DOMAIN          205..436
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   DOMAIN          470..505
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          541..591
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   COILED          748..782
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   797 AA;  90452 MW;  3857A5092AC5F56B CRC64;
     MGTLGKAREA PRKPTHGCRA VPKARLEAKP ASSPLPCHPG LAQITQFRMM VPLGHFAKGA
     SLDDLIDSCV QSFDADGNLC RSNQLLQVML TMHRILISSA ELLQKVITLY PDALAKNSPG
     LCLKICYFVR YWITEFWIMF KMDTSLASTM EEFQELVKAN GEELHCRLID TTQINARDWS
     RKLTQRIKSN TSKKRKVSLL FDHLEPEELS EHLTFLEFKS FRRISFSDYQ NYLVNSCVKE
     NPTMERSIAL CNGISQWVQL MVLSRPTPQL RAEVFIKFIQ VAQKLHQLQN FNTLMAVIGG
     LCHSSISRLK ETSSHVPHEI NKVLGEMTEL LSSCRNYDNY RRAYGECTDF KIPILGVHLK
     DLISLYEAMP DYLEEGKVNV HKLLALYNHI NELVQLQEVP PPLEANKDLV HLLTLSLDLY
     YTEDEIYELS YAREPRNHKA PPLTPSKPPV VVDWASGVSP KPDPKTISKH VQRMVDSVFK
     NYDHDQDGYI SQEEFEKIAA SFPFSFCVMD KDREGLISRD EITAYFMRAS SIYSKLGLGF
     PHNFQETTYL KPTFCDNCAG FLWGVIKQGY RCKDCGMNCH KQCKDLVVFE CKKRAKNSTA
     PTEISTSVGP TSNLCSLGAK DLLHAPEEGP FTFPNGEAAE HSEESKDRTI MLMGVSSQKI
     SVRLKRTVAH MATQTEALSW PGSEGPSSHF VLSSPRKTAQ DTLYVLPSPT SPCPSPVLVR
     KRAFVKWENK ESFIKSKEEL RHLRLPTYQE LEQEINTLKA DNNALKIQLK YAQKKIETLQ
     LARNNHVLAQ MEQGDCS
//
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