RAIN_MOUSE
ID RAIN_MOUSE Reviewed; 961 AA.
AC Q3U0S6; E9QLI7; Q6GQW4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ras-interacting protein 1;
DE Short=Rain;
GN Name=Rasip1;
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 [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-961.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=15031288; DOI=10.1074/jbc.m312867200;
RA Mitin N.Y., Ramocki M.B., Zullo A.J., Der C.J., Konieczny S.F.,
RA Taparowsky E.J.;
RT "Identification and characterization of Rain, a novel Ras-interacting
RT protein with a unique subcellular localization.";
RL J. Biol. Chem. 279:22353-22361(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-325, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19272373; DOI=10.1016/j.ydbio.2009.02.033;
RA Xu K., Chong D.C., Rankin S.A., Zorn A.M., Cleaver O.;
RT "Rasip1 is required for endothelial cell motility, angiogenesis and vessel
RT formation.";
RL Dev. Biol. 329:269-279(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-286; SER-320;
RP SER-322; SER-325 AND SER-413, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
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 [8]
RP FUNCTION, AND INTERACTION WITH MYH9 AND ARHGAP29.
RX PubMed=21396893; DOI=10.1016/j.devcel.2011.02.010;
RA Xu K., Sacharidou A., Fu S., Chong D.C., Skaug B., Chen Z.J., Davis G.E.,
RA Cleaver O.;
RT "Blood vessel tubulogenesis requires Rasip1 regulation of GTPase
RT signaling.";
RL Dev. Cell 20:526-539(2011).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-96, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Required for the proper formation of vascular structures that
CC develop via both vasculogenesis and angiogenesis. Acts as a critical
CC and vascular-specific regulator of GTPase signaling, cell architecture,
CC and adhesion, which is essential for endothelial cell morphogenesis and
CC blood vessel tubulogenesis. Regulates the activity of Rho GTPases in
CC part by recruiting ARHGAP29 and suppressing RhoA signaling and
CC dampening ROCK and MYH9 activities in endothelial cells. May act as
CC effector for Golgi-bound HRAS and other Ras-like proteins. May promote
CC HRAS-mediated transformation. Negative regulator of amino acid
CC starvation-induced autophagy (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19272373, ECO:0000269|PubMed:21396893}.
CC -!- SUBUNIT: Interacts with Ras family members that have been activated by
CC GTP binding. Interacts with HRAS, RAP1A, RAP2, RRAS, RAF1 and RRAS2 (By
CC similarity). Interacts with MYH9 and ARHGAP29. {ECO:0000250,
CC ECO:0000269|PubMed:21396893}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Golgi apparatus, Golgi stack {ECO:0000250}. Note=Associated with
CC perinuclear vesicles. Is recruited to Golgi stacks by activated HRAS
CC (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in kidney, heart, skeletal muscle, small
CC intestine and lung. {ECO:0000269|PubMed:15031288}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in the endothelium of the
CC developing blood vessels in embryos. {ECO:0000269|PubMed:19272373}.
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DR EMBL; AK156602; BAE33775.1; -; mRNA.
DR EMBL; AC149057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072584; AAH72584.1; -; mRNA.
DR CCDS; CCDS21256.1; -.
DR RefSeq; NP_082820.1; NM_028544.1.
DR AlphaFoldDB; Q3U0S6; -.
DR SMR; Q3U0S6; -.
DR BioGRID; 213746; 1.
DR STRING; 10090.ENSMUSP00000062429; -.
DR iPTMnet; Q3U0S6; -.
DR PhosphoSitePlus; Q3U0S6; -.
DR jPOST; Q3U0S6; -.
DR MaxQB; Q3U0S6; -.
DR PaxDb; Q3U0S6; -.
DR PRIDE; Q3U0S6; -.
DR ProteomicsDB; 253168; -.
DR Antibodypedia; 31787; 106 antibodies from 30 providers.
DR DNASU; 69903; -.
DR Ensembl; ENSMUST00000057927; ENSMUSP00000062429; ENSMUSG00000044562.
DR GeneID; 69903; -.
DR KEGG; mmu:69903; -.
DR UCSC; uc009gwi.1; mouse.
DR CTD; 54922; -.
DR MGI; MGI:1917153; Rasip1.
DR VEuPathDB; HostDB:ENSMUSG00000044562; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000160072; -.
DR HOGENOM; CLU_010386_1_0_1; -.
DR InParanoid; Q3U0S6; -.
DR OMA; ERRFEIH; -.
DR OrthoDB; 447883at2759; -.
DR PhylomeDB; Q3U0S6; -.
DR TreeFam; TF315987; -.
DR BioGRID-ORCS; 69903; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Rasip1; mouse.
DR PRO; PR:Q3U0S6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3U0S6; protein.
DR Bgee; ENSMUSG00000044562; Expressed in cardiovascular system endothelium and 154 other tissues.
DR Genevisible; Q3U0S6; MM.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR GO; GO:1905709; P:negative regulation of membrane permeability; ISO:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0033625; P:positive regulation of integrin activation; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
DR CDD; cd15472; Myo5p-like_CBD_Rasip1; 1.
DR InterPro; IPR037983; CBD_Rasip1/Radil.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Cytoplasm; Golgi apparatus; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..961
FT /note="Ras-interacting protein 1"
FT /id="PRO_0000097164"
FT DOMAIN 141..253
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 594..895
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 121
FT /note="L -> M (in Ref. 1; BAE33775)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="M -> V (in Ref. 1; BAE33775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 961 AA; 103559 MW; 2E212A15513DB2FB CRC64;
MLSGERKEGG SPRFGKLHLP VGLWINSPRK QLAKLGRRWP SAASVKSSSS DTGSRSSEPL
PPPPPPPHVE LRRVGAVKAA GGASGSRAKR ISQLFRGSGA GGAGGPGTPG GAQRWASEKK
LPELAAGVAP EPPLPTRAAV PPGVLKIFAS GLASGANYKS VLATERSTAR ELVAEALERY
GLTGGRGAGD SGCVDAYALC DALGRPAVGV GGGEWRAEHL RVLADAERPL LVQDLWRARP
GWARRFELRG REEARRLEQE AFGAADADGT NAPSWRTQKN RSRAASGGAA LASPGPGSGS
GTPTGSGGKE RSENLSLRRS VSELSLQGRR RRQQERRQQA LSMAPGAADA QMVPTDPGDF
DQLTQCLIQA PSNRPYFLLL QGYQDAQDFV VYVMTREQHV FGRGGPSSSR GGSPAPYVDT
FLNAPDILPR HCTVRAGPEP PAMVRPSRGA PVTHNGCLLL REAELHPGDL LGLGEHFLFM
YKDPRSGGSG PARPSWLPAR PGAAPPGPGW AFSCRLCGRG LQERGEALAA YLDGREPVLR
FRPREEEALL GEIVRAAASG AGDLPPLGPA TLLALCVQHS ARELELGHLP RLLGRLARLI
KEAVWEKIKE IGDRQPENHP EGVPEVPLTP EAVSVELRPL ILWMANTTEL LSFVQEKVLE
MEKEADQEGL SSDPQLCNDL ELCDEALALL DEVIMCTFQQ SVYYLTKTLY STLPALLDSN
PFTAGAELPG PGAELEAMPP GLRPTLGVFQ AALELTSQCE LHPDLVSQTF GYLFFFSNAS
LLNSLMERGQ GRPFYQWSRA VQIRTNLDLV LDWLQGAGLG DIATEFFRKL SIAVNLLCVP
RTSLLKASWS SLRTDYPTLT PAQLHHLLSH YQLGPGRGPP PAWDPPPAER DAVDTGDIFE
SFSSHPPLIL PLGSSRLRLT GPVTDDALHR ELRRLRRLLW DLEQQELPAN HRHGPPVAST
P
