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RGL1_MOUSE
ID   RGL1_MOUSE              Reviewed;         768 AA.
AC   Q60695; Q8VD09;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Ral guanine nucleotide dissociation stimulator-like 1;
DE            Short=RalGDS-like 1;
GN   Name=Rgl1; Synonyms=Rgl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7935463; DOI=10.1128/mcb.14.11.7483-7491.1994;
RA   Kikuchi A., Demo S.D., Ye Z.H., Chen Y.W., Williams L.T.;
RT   "ralGDS family members interact with the effector loop of ras p21.";
RL   Mol. Cell. Biol. 14:7483-7491(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   STRUCTURE BY NMR OF 632-734.
RX   PubMed=9891982; DOI=10.1016/s0014-5793(98)01596-8;
RA   Kigawa T., Endo M., Ito Y., Shirouzu M., Kikuchi A., Yokoyama S.;
RT   "Solution structure of the Ras-binding domain of RGL.";
RL   FEBS Lett. 441:413-418(1998).
CC   -!- FUNCTION: Probable guanine nucleotide exchange factor.
CC   -!- SUBUNIT: Interacts with Ras.
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DR   EMBL; U14103; AAA64950.1; -; mRNA.
DR   EMBL; AK144218; BAE25780.1; -; mRNA.
DR   EMBL; AK169109; BAE40891.1; -; mRNA.
DR   EMBL; AK169180; BAE40958.1; -; mRNA.
DR   EMBL; CH466520; EDL39452.1; -; Genomic_DNA.
DR   EMBL; BC017678; AAH17678.1; -; mRNA.
DR   CCDS; CCDS15365.1; -.
DR   PIR; A56234; A56234.
DR   RefSeq; NP_001333046.1; NM_001346117.1.
DR   RefSeq; NP_001333047.1; NM_001346118.1.
DR   RefSeq; NP_001333048.1; NM_001346119.1.
DR   RefSeq; NP_058542.2; NM_016846.4.
DR   PDB; 1EF5; NMR; -; A=632-734.
DR   PDBsum; 1EF5; -.
DR   AlphaFoldDB; Q60695; -.
DR   SMR; Q60695; -.
DR   STRING; 10090.ENSMUSP00000027760; -.
DR   iPTMnet; Q60695; -.
DR   PhosphoSitePlus; Q60695; -.
DR   MaxQB; Q60695; -.
DR   PaxDb; Q60695; -.
DR   PRIDE; Q60695; -.
DR   ProteomicsDB; 253257; -.
DR   Antibodypedia; 20603; 139 antibodies from 28 providers.
DR   DNASU; 19731; -.
DR   Ensembl; ENSMUST00000027760; ENSMUSP00000027760; ENSMUSG00000026482.
DR   GeneID; 19731; -.
DR   KEGG; mmu:19731; -.
DR   UCSC; uc007czh.1; mouse.
DR   CTD; 23179; -.
DR   MGI; MGI:107484; Rgl1.
DR   VEuPathDB; HostDB:ENSMUSG00000026482; -.
DR   eggNOG; KOG3629; Eukaryota.
DR   GeneTree; ENSGT00940000156012; -.
DR   HOGENOM; CLU_010252_0_1_1; -.
DR   InParanoid; Q60695; -.
DR   OMA; EQFNGLY; -.
DR   TreeFam; TF315204; -.
DR   Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR   BioGRID-ORCS; 19731; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Rgl1; mouse.
DR   EvolutionaryTrace; Q60695; -.
DR   PRO; PR:Q60695; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q60695; protein.
DR   Bgee; ENSMUSG00000026482; Expressed in right kidney and 220 other tissues.
DR   ExpressionAtlas; Q60695; baseline and differential.
DR   Genevisible; Q60695; MM.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   Gene3D; 1.10.840.10; -; 1.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008937; Ras-like_GEF.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR030748; RGL1.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23113; PTHR23113; 1.
DR   PANTHER; PTHR23113:SF199; PTHR23113:SF199; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..768
FT                   /note="Ral guanine nucleotide dissociation stimulator-like
FT                   1"
FT                   /id="PRO_0000068886"
FT   DOMAIN          65..196
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT   DOMAIN          232..501
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT   DOMAIN          648..735
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT   REGION          530..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        662
FT                   /note="N -> H (in Ref. 1; AAA64950)"
FT                   /evidence="ECO:0000305"
FT   STRAND          652..658
FT                   /evidence="ECO:0007829|PDB:1EF5"
FT   HELIX           676..682
FT                   /evidence="ECO:0007829|PDB:1EF5"
FT   TURN            683..687
FT                   /evidence="ECO:0007829|PDB:1EF5"
FT   STRAND          692..701
FT                   /evidence="ECO:0007829|PDB:1EF5"
FT   STRAND          703..705
FT                   /evidence="ECO:0007829|PDB:1EF5"
FT   STRAND          708..711
FT                   /evidence="ECO:0007829|PDB:1EF5"
FT   TURN            716..720
FT                   /evidence="ECO:0007829|PDB:1EF5"
FT   STRAND          726..732
FT                   /evidence="ECO:0007829|PDB:1EF5"
SQ   SEQUENCE   768 AA;  86324 MW;  F59853A281DD52F6 CRC64;
     MKLLWQAKMS SIQDWGEEVE EGAVYHVTLK RVQIQQAANK GARWLGVEGD QLPPGHTVSQ
     YETCKIRTIK AGTLEKLVEN LLTAFGDNDF TYISIFLSTY RGFASTKEVL ELLLDRYGNL
     TGPNCEDDGS QSSPESKAVI RNAIASILRA WLDQCAEDFR EPPHFPCLQK LLEYLKQMMP
     GSDPERRAQN LLEQFQKQDV DSDNGLLNTS SFSLEEEEEL ESGGSAEFTN FSEDLVAEQL
     TYMDAQLFKK VVPHHCLGCI WSQRDKKENK HLAPTIRATI SQFNTLTKCV VSTVLGSKEL
     KTQQRARVIE KWINIAHECR ILKNFSSLRA IVSALQSNSI YRLKKAWAAV PKDRMLMFEE
     LSDIFSDHNN HLTSRELLMK EGTSKFANLD SSVKENQKRT QRRLQLQKDM GVMQGTVPYL
     GTFLTDLTML DTALQDYIEG GLINFEKRRR EFEVIAQIKL LQSACNSYCM GPDQKFIQWF
     QRQQLLSEEE SYALSCEIEA AADANTTSPK PRKSMVKRLS LLFLGSDIIP GSTPTKEQPK
     SAASGSSGES MDSVSVSSCE SNHSEAEEGP VTPMDTPDEP QKKLSESSSS CSSIHSMDTN
     SSGMSSLINP LSSPPTCNNN PKIHKRSVSV TSITSTVLPP VYNQQNEDTC IIRISVEDNN
     GNMYKSIMLT SQDKTPAVIQ RAMSKHNLES DPAEEYELVQ VISEDKELVI PDSANVFYAM
     NSQVNFDFIL RKKNSVEEQV KLRSRTSLTL PRTAKRGCWS NRHSKITL
 
 
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