ID RASL3_MOUSE Reviewed; 1041 AA. AC Q8C2K5; A3KMM0; Q8C2A5; Q8C9R4; Q8CDB4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 02-NOV-2016, entry version 121. DE RecName: Full=RAS protein activator like-3; GN Name=Rasal3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-187; SER-189; RP SER-190; SER-193; SER-239; SER-252; SER-256; SER-259; THR-262; SER-813 RP AND SER-816, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lung, 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 RT expression."; RL Cell 143:1174-1189(2010). RN [4] RP TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=25652366; DOI=10.1002/eji.201444977; RA Saito S., Kawamura T., Higuchi M., Kobayashi T., Yoshita-Takahashi M., RA Yamazaki M., Abe M., Sakimura K., Kanda Y., Kawamura H., Jiang S., RA Naito M., Yoshizaki T., Takahashi M., Fujii M.; RT "RASAL3, a novel hematopoietic RasGAP protein, regulates the number RT and functions of NKT cells."; RL Eur. J. Immunol. 45:1512-1523(2015). CC -!- FUNCTION: Functions as a Ras GTPase-activating protein. Plays an CC important role in the expansion and functions of natural killer T CC (NKT) cells in the liver by negatively regulating RAS activity and CC the down-stream ERK signaling pathway. CC {ECO:0000269|PubMed:25652366}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86YV0}. CC Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q86YV0}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8C2K5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8C2K5-2; Sequence=VSP_031931, VSP_031932; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Predominantly expressed in hematopoietic CC tissues. CC -!- DISRUPTION PHENOTYPE: No visible phenotype. The number of natural CC killer T (NKT) cells in the liver is selectively decreased (around CC 50%) in mutant mice (PubMed:25652366). CC {ECO:0000269|PubMed:25652366}. CC -!- SIMILARITY: Contains 1 C2 domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PH domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Ras-GAP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00167}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC30956.1; Type=Frameshift; Positions=11; 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; AK030797; BAC27141.1; -; mRNA. DR EMBL; AK041479; BAC30956.1; ALT_FRAME; mRNA. DR EMBL; AK088449; BAC40358.1; -; mRNA. DR EMBL; AK088987; BAC40689.1; -; mRNA. DR EMBL; BC132341; AAI32342.2; -; mRNA. DR CCDS; CCDS37556.1; -. [Q8C2K5-1] DR RefSeq; NP_848900.2; NM_178785.3. [Q8C2K5-1] DR RefSeq; XP_006524476.1; XM_006524413.3. [Q8C2K5-2] DR UniGene; Mm.122284; -. DR UniGene; Mm.416246; -. DR ProteinModelPortal; Q8C2K5; -. DR SMR; Q8C2K5; -. DR DIP; DIP-61657N; -. DR STRING; 10090.ENSMUSP00000064084; -. DR iPTMnet; Q8C2K5; -. DR PhosphoSitePlus; Q8C2K5; -. DR EPD; Q8C2K5; -. DR PaxDb; Q8C2K5; -. DR PRIDE; Q8C2K5; -. DR DNASU; 320484; -. DR Ensembl; ENSMUST00000063824; ENSMUSP00000064084; ENSMUSG00000052142. [Q8C2K5-1] DR Ensembl; ENSMUST00000137458; ENSMUSP00000123141; ENSMUSG00000052142. [Q8C2K5-2] DR GeneID; 320484; -. DR KEGG; mmu:320484; -. DR UCSC; uc008bwu.1; mouse. [Q8C2K5-2] DR UCSC; uc008bwv.1; mouse. [Q8C2K5-1] DR CTD; 64926; -. DR MGI; MGI:2444128; Rasal3. DR eggNOG; KOG3508; Eukaryota. DR eggNOG; ENOG410XPU1; LUCA. DR GeneTree; ENSGT00760000119092; -. DR HOGENOM; HOG000154074; -. DR InParanoid; Q8C2K5; -. DR KO; K17634; -. DR OMA; RRHFQPS; -. DR OrthoDB; EOG091G020W; -. DR TreeFam; TF105303; -. DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs. DR Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases. DR PRO; PR:Q8C2K5; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000052142; -. DR CleanEx; MM_A430107D22RIK; -. DR ExpressionAtlas; Q8C2K5; baseline and differential. DR Genevisible; Q8C2K5; MM. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0098562; C:cytoplasmic side of membrane; ISO:MGI. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:UniProtKB. DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR Gene3D; 1.10.506.10; -; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR011993; PH_dom-like. DR InterPro; IPR023152; RasGAP_CS. DR InterPro; IPR001936; RasGAP_dom. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR Pfam; PF00616; RasGAP; 1. DR SMART; SM00323; RasGAP; 1. DR SUPFAM; SSF48350; SSF48350; 1. DR SUPFAM; SSF49562; SSF49562; 1. DR SUPFAM; SSF50729; SSF50729; 1. DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1. DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; KW GTPase activation; Phosphoprotein; Reference proteome. FT CHAIN 1 1041 RAS protein activator like-3. FT /FTId=PRO_0000322567. FT DOMAIN 220 321 PH. FT DOMAIN 334 410 C2. FT DOMAIN 484 676 Ras-GAP. {ECO:0000255|PROSITE- FT ProRule:PRU00167}. FT COILED 218 243 {ECO:0000255}. FT COILED 931 1013 {ECO:0000255}. FT MOD_RES 41 41 Phosphoserine. FT {ECO:0000250|UniProtKB:Q86YV0}. FT MOD_RES 74 74 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 187 187 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 189 189 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 190 190 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 193 193 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 239 239 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 252 252 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 256 256 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 259 259 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 262 262 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 813 813 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 816 816 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT VAR_SEQ 1 22 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_031931. FT VAR_SEQ 132 132 E -> ERSKQAMVPGVKGQLSGVSSLLQLQ (in FT isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_031932. FT CONFLICT 122 122 L -> M (in Ref. 1; BAC27141). FT {ECO:0000305}. FT CONFLICT 494 494 R -> H (in Ref. 1; BAC27141). FT {ECO:0000305}. FT CONFLICT 978 978 G -> S (in Ref. 1; BAC40689). FT {ECO:0000305}. SQ SEQUENCE 1041 AA; 114782 MW; DA58139782B1EEFF CRC64; MKPECGQTMF RTFWSRSRDS SAMDPPLQSE EDSQTQPSLP SPLTSYRWHT GGSGEKAAGG FRWGRFAGWG RALSHQEPMV NSQPAPRSLF RRVLSAPPKE SRSNRLRFSK TLWGRHKNVA PLEPKPNPKA PEPELELVAD PDLPVAQIPE PPTPDMPVWN IDGFTLLEGK LVMLGEEEGP RQIRVGSASS ENSMQAALGN LKDAVRTPGK TEPEAAGSNQ VHNVRKLLKR LKEKKRAKSE LGAYTPRDGP PSALGSRESL ATLSELDLGA ERDVRVWPLH PSLLGEPYCF QVTWAGGSLC FSCRSSAERD RWIEDLRRQF QPSQDNVERQ EMWLTVWVHE AKGLPRATVP GVRAELWLDG ALLARTAPRA GPGQLFWAER FHFEALPPAR RLSLRLRSAG PAGATVGRVV LELDEVSIPR APAAGLERWF PVLGAPAGAV LRARIRVRCL RVLPSERYKE LAEFLTFHYA RLCGALEPAL SAQAKEELAA AMVRVLRATG RAQALVTDLG TAELARCGGR EALLFRENTL ATKAIDEYMK LVAQEYLQDT LGQVVRCLCA STEDCEVDPS KCPTPELPKH QARLRDSCEE VFENIIHSYN CFPAELGSVF SSWREACKAR GSEALGPRLV CASLFLRLLC PAILAPSLFG LAPEHPAPGP ARTLTLIAKV IQNLANCAPF GEKEAYMAFM NSFLEDHGPA MQHFLDQVAT VDADTTPSGY QGSGDLALQL AVLHVQLCTI FAELDQKTQD SLEPLPTILR AIEEGRPVPV SVPMRLPRIS TQVQSSFFSG EKPGFLAPRD LPKHTPLISK SQSLRSFQGA GSWASRRPDE ERPQRRPRPV LRTQSVPARR PTHRRPSAGS KPRPKGSLRM GPAPCGRAWT RASASLPRKP SVPWQRQMDQ PGDRYQTTGT HRPVGKLAEI QCEVAIFREA QKALSLLVES LSTQVQALKE QQEHFRCQLQ DLYSRLGAGI SKLDSKGGLP SNGSHRLKSL EQRLTEMECS QDQLRDSLQS LQLLSKTPGS RSQPLPLKAP CVNGADLSMG T //