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-2010, entry version 67. 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). CC -!- FUNCTION: May function as a Ras GTPase-activating protein (By CC similarity). 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 -!- SIMILARITY: Contains 1 C2 domain. CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SIMILARITY: Contains 1 Ras-GAP domain. CC -!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator. CC -!- SEQUENCE CAUTION: CC Sequence=BAC30956.1; Type=Frameshift; Positions=11; 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 IPI; IPI00624211; -. DR IPI; IPI00844774; -. DR RefSeq; NP_848900.2; -. DR UniGene; Mm.122284; -. DR ProteinModelPortal; Q8C2K5; -. DR SMR; Q8C2K5; 426-769. DR PhosphoSite; Q8C2K5; -. DR PRIDE; Q8C2K5; -. DR Ensembl; ENSMUST00000063824; ENSMUSP00000064084; ENSMUSG00000052142. DR GeneID; 320484; -. DR KEGG; mmu:320484; -. DR UCSC; uc008bwv.1; mouse. DR CTD; 320484; -. DR MGI; MGI:2444128; Rasal3. DR HOGENOM; HBG505952; -. DR InParanoid; Q8C2K5; -. DR OMA; LPSERYK; -. DR OrthoDB; EOG9M3CW3; -. DR NextBio; 396821; -. DR ArrayExpress; Q8C2K5; -. DR Bgee; Q8C2K5; -. DR CleanEx; MM_A430107D22RIK; -. DR Genevestigator; Q8C2K5; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0051056; P:regulation of small GTPase mediated signal ...; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB. DR InterPro; IPR011993; PH_type. DR InterPro; IPR001849; Pleckstrin_homology. DR InterPro; IPR001936; RasGAP. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF00616; RasGAP; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00323; RasGAP; 1. DR SUPFAM; SSF49562; C2_CaLB; 1. DR SUPFAM; SSF48350; Rho_GAP; 1. DR PROSITE; PS50004; C2; FALSE_NEG. DR PROSITE; PS50003; PH_DOMAIN; FALSE_NEG. DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1. DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Coiled coil; GTPase activation; Phosphoprotein. 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. FT COILED 218 243 Potential. FT COILED 931 1013 Potential. FT MOD_RES 41 41 Phosphoserine (By similarity). FT MOD_RES 74 74 Phosphoserine (By similarity). FT MOD_RES 187 187 Phosphoserine (By similarity). FT MOD_RES 190 190 Phosphoserine (By similarity). FT MOD_RES 259 259 Phosphoserine (By similarity). FT VAR_SEQ 1 22 Missing (in isoform 2). FT /FTId=VSP_031931. FT VAR_SEQ 132 132 E -> ERSKQAMVPGVKGQLSGVSSLLQLQ (in FT isoform 2). FT /FTId=VSP_031932. FT CONFLICT 122 122 L -> M (in Ref. 1; BAC27141). FT CONFLICT 494 494 R -> H (in Ref. 1; BAC27141). FT CONFLICT 978 978 G -> S (in Ref. 1; BAC40689). 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 //