ID Q0VAV5_MOUSE Unreviewed; 1268 AA. AC Q0VAV5; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 24-JAN-2024, entry version 124. DE SubName: Full=RAS protein activator like 2 {ECO:0000313|EMBL:AAI20903.1}; GN Name=Rasal2 {ECO:0000313|EMBL:AAI20903.1, GN ECO:0000313|MGI:MGI:2443881}; 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 {ECO:0000313|EMBL:AAI20903.1}; RN [1] {ECO:0000313|EMBL:AAI20903.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=PCR rescued clones {ECO:0000313|EMBL:AAI20903.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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). 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; BC120902; AAI20903.1; -; mRNA. DR RefSeq; NP_808312.3; NM_177644.5. DR AlphaFoldDB; Q0VAV5; -. DR IntAct; Q0VAV5; 1. DR MINT; Q0VAV5; -. DR DNASU; 226525; -. DR GeneID; 226525; -. DR AGR; MGI:2443881; -. DR CTD; 9462; -. DR MGI; MGI:2443881; Rasal2. DR OrthoDB; 22721at2759; -. DR BioGRID-ORCS; 226525; 3 hits in 77 CRISPR screens. DR ChiTaRS; Rasal2; mouse. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0060612; P:adipose tissue development; IMP:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:2000257; P:regulation of protein activation cascade; IMP:MGI. DR GO; GO:0002021; P:response to dietary excess; IMP:MGI. DR GO; GO:0009749; P:response to glucose; IMP:MGI. DR CDD; cd04013; C2_SynGAP_like; 1. DR CDD; cd05136; RasGAP_DAB2IP; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR021887; DAB2P_C. DR InterPro; IPR001849; PH_domain. 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:SF52; RAS GTPASE-ACTIVATING PROTEIN NGAP; 1. DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF12004; DAB2P_C; 1. DR Pfam; PF00616; RasGAP; 2. DR SMART; SM00239; C2; 1. DR SMART; SM00233; PH; 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; 2. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1. DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1. DR Genevisible; Q0VAV5; MM. PE 2: Evidence at transcript level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW GTPase activation {ECO:0000256|ARBA:ARBA00022468}. FT DOMAIN 57..287 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT DOMAIN 278..396 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 456..648 FT /note="Ras-GAP" FT /evidence="ECO:0000259|PROSITE:PS50018" FT REGION 92..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 179..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 757..799 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 878..1027 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1040..1084 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1245..1268 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1095..1181 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 143..167 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 201..215 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 757..779 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 902..916 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 930..963 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 964..983 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1040..1082 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1268 AA; 142714 MW; B770CB1F05C0CCC0 CRC64; MFTGLESDSP LPPEDLDAVV PVSGAVAGGM LDRILLESVC QQQSWVRVFD VKGPPTHRLS CGQSPYTETT SWERKYCILT DSQLVLLNKE KEMPVEGQDQ QTDSTKGRCL RRTVSVPSEG QFPEYPQEGT TKLEVPAERS PRRRSISGTS TSEKPNSMDT ANTSPFKVPG FFSKRLKGSI KRTKSQSKLD RNTSFRLPSL RNADDRSRGL PKLKESRSHG SLLSPCSAVE CLDLGRGEPV SVKPLHSSIL GQDFCFEVTY LSGSKCFSCS SASERDKWME NLRRTVQPNK DNCRRAENVL RLWIIEAKDL APKKKYFCEL CLDDTLFART TSKTKADNIF WGEHFEFYSL PPLHSITVHI YKDVEKKKKK DKNNYVGLVN IPTASVTGRQ FVEKWYPVST PTPNKGKTGG PSIRIKSRFQ TITILPMEQY KEFAEFITSN YTMLCSVLEP VISVRNKEEL ACALVHILQS TGRAKDFLTD LVMSEVDRCG EHDVLIFREN TIATKSIEEY LKLVGQQYLH DALGEFIKAL YESDENCEVD PSKCSSSELM DHQSNLKMCC ELAFCKIINS YCVFPRELKE VFASWKQQCL NRGKQDISER LISASLFLRF LCPAIMSPSL FNLMQEYPDD RTSRTLTLIA KVIQNLANFA KFGNKEEYMA FMNDFLEHEW GGMKRFLLEI SNPDTISNTP GFDGYIDLGR ELSVLHSLLW EVVSQLDKGE NSFLQATVAK LGPLPRVLAD ITKSLTNPTP IQQQLRRFAE HSSSPNVSGS LSSGLQRICE DPTDSDLHKL KSPSQDNTDS YFRGKTLLLV QQASSQSMTY SEKDEKENSL PNGRSISLMD LQDTHAAQAE HASVMLDVPM RLAGSQLSIT QVASIKQLRE TQSTPQSAPQ VRRPLHPALN QPGSLQPLSF QNPVYHLNNP VPAMPKASAD SSLENLSTAS SRSQSNSEDF KLSGPSNSSM EDFTKRSSHS EDFSRRHTVP DRHIPLALPR QNSTGQSQIR KLDHSGLGAR AKAPPSLPHS ASLRSTGSMS VASAALMAEP VQNGSRSRQQ SSSSRESPVP KVRAIQRQQT QQVQSPVDSA TMSPVERTAA WVLNNGQYEE DVEETEQNQD EAKHAEKYEQ EITKLKERLR VSSRRLEEYE RRLLVQEQQM QKLLLEYKAR LEDSEERLRR QQEEKDSQMK SIISRLMAVE EELKKDHAEM QAVIDAKQKI IDAQEKRIVS LDSANTRLMS ALTQVKERYS MQVRNGISPT NPTKLSITEN GEFKNSSC //