RASL3_MOUSE
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-AUG-2022, entry version 156.
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};
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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 PRIDE; Q8C2K5; -.
DR ProteomicsDB; 300240; -. [Q8C2K5-1]
DR ProteomicsDB; 300241; -. [Q8C2K5-2]
DR Antibodypedia; 54246; 71 antibodies from 15 providers.
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 VEuPathDB; HostDB:ENSMUSG00000052142; -.
DR eggNOG; KOG3508; Eukaryota.
DR GeneTree; ENSGT00940000161423; -.
DR InParanoid; Q8C2K5; -.
DR OMA; WGRHKSP; -.
DR OrthoDB; 69536at2759; -.
DR TreeFam; TF105303; -.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR BioGRID-ORCS; 320484; 0 hits in 71 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 GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.506.10; -; 2.
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; PTHR10194; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 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
