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 03-MAY-2023, entry version 159. DE RecName: Full=RAS protein activator like-3; GN Name=Rasal3; 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] (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., 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 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 project: RT 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 AND RP SER-816, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 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 and RT 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 (NKT) CC cells in the liver by negatively regulating RAS activity and the down- CC stream ERK signaling pathway. {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 -!- TISSUE SPECIFICITY: Predominantly expressed in hematopoietic tissues. CC -!- DISRUPTION PHENOTYPE: No visible phenotype. The number of natural CC killer T (NKT) cells in the liver is selectively decreased (around 50%) CC in mutant mice (PubMed:25652366). {ECO:0000269|PubMed:25652366}. 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; 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 CCDS; CCDS84292.1; -. [Q8C2K5-2] DR RefSeq; NP_001334272.1; NM_001347343.1. [Q8C2K5-2] DR RefSeq; NP_848900.2; NM_178785.3. [Q8C2K5-1] DR AlphaFoldDB; Q8C2K5; -. DR SMR; Q8C2K5; -. DR BioGRID; 236057; 1. DR DIP; DIP-61657N; -. DR IntAct; Q8C2K5; 3. DR STRING; 10090.ENSMUSP00000064084; -. DR iPTMnet; Q8C2K5; -. DR PhosphoSitePlus; Q8C2K5; -. DR EPD; Q8C2K5; -. DR jPOST; Q8C2K5; -. DR MaxQB; Q8C2K5; -. DR PaxDb; Q8C2K5; -. DR ProteomicsDB; 300240; -. [Q8C2K5-1] DR ProteomicsDB; 300241; -. [Q8C2K5-2] DR Antibodypedia; 54246; 72 antibodies from 16 providers. DR DNASU; 320484; -. DR Ensembl; ENSMUST00000063824.14; ENSMUSP00000064084.8; ENSMUSG00000052142.16. DR Ensembl; ENSMUST00000137458.2; ENSMUSP00000123141.2; ENSMUSG00000052142.16. [Q8C2K5-2] DR GeneID; 320484; -. DR KEGG; mmu:320484; -. DR UCSC; uc008bwu.1; mouse. [Q8C2K5-2] DR UCSC; uc008bwv.1; mouse. [Q8C2K5-1] DR AGR; MGI:2444128; -. DR CTD; 64926; -. DR MGI; MGI:2444128; Rasal3. DR VEuPathDB; HostDB:ENSMUSG00000052142; -. DR eggNOG; KOG3508; Eukaryota. DR GeneTree; ENSGT00940000161423; -. DR InParanoid; Q8C2K5; -. DR OMA; TWGSRSQ; -. DR OrthoDB; 22721at2759; -. DR TreeFam; TF105303; -. DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs. DR BioGRID-ORCS; 320484; 0 hits in 76 CRISPR screens. DR PRO; PR:Q8C2K5; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q8C2K5; protein. DR Bgee; ENSMUSG00000052142; Expressed in thymus and 71 other tissues. 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:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. 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:0043087; P:regulation of GTPase activity; IEA:InterPro. DR CDD; cd05136; RasGAP_DAB2IP; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR039360; Ras_GTPase. DR InterPro; IPR023152; RasGAP_CS. DR InterPro; IPR001936; RasGAP_dom. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1. DR PANTHER; PTHR10194:SF96; RAS PROTEIN ACTIVATOR LIKE-3; 1. DR Pfam; PF00616; RasGAP; 1. DR SMART; SM00323; RasGAP; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50004; C2; 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; Cytoplasm; GTPase activation; KW Phosphoprotein; Reference proteome. FT CHAIN 1..1041 FT /note="RAS protein activator like-3" FT /id="PRO_0000322567" FT DOMAIN 220..321 FT /note="PH" FT DOMAIN 312..430 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 484..676 FT /note="Ras-GAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167" FT REGION 1..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 234..256 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 790..910 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1016..1041 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 218..243 FT /evidence="ECO:0000255" FT COILED 931..1013 FT /evidence="ECO:0000255" FT COMPBIAS 10..48 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 806..820 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 41 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q86YV0" FT MOD_RES 74 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 187 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 189 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 193 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 239 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 256 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 262 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 813 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 816 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 1..22 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031931" FT VAR_SEQ 132 FT /note="E -> ERSKQAMVPGVKGQLSGVSSLLQLQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031932" FT CONFLICT 122 FT /note="L -> M (in Ref. 1; BAC27141)" FT /evidence="ECO:0000305" FT CONFLICT 494 FT /note="R -> H (in Ref. 1; BAC27141)" FT /evidence="ECO:0000305" FT CONFLICT 978 FT /note="G -> S (in Ref. 1; BAC40689)" FT /evidence="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 //