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Database: UniProt
Entry: RASA3_MOUSE
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Original site: RASA3_MOUSE 
ID   RASA3_MOUSE             Reviewed;         834 AA.
AC   Q60790; Q6PG24; Q925V1;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Ras GTPase-activating protein 3;
DE   AltName: Full=GAP1(IP4BP);
DE   AltName: Full=GapIII;
DE   AltName: Full=Ins P4-binding protein;
GN   Name=Rasa3;
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 [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=7500386; DOI=10.1002/jnr.490410615;
RA   Baba H., Fuss B., Urano J., Poullet P., Watson J.B., Tamanoi F.,
RA   Macklin W.B.;
RT   "GapIII, a new brain-enriched member of the GTPase-activating protein
RT   family.";
RL   J. Neurosci. Res. 41:846-858(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Iwashita S., Sezaki M.;
RT   "Murine R ras GAP cDNA construct.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and CD-1; TISSUE=Brain, and Neural stem cell;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-66, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809 AND SER-833, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, 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).
CC   -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind
CC       inositol tetrakisphosphate (IP4).
CC   -!- TISSUE SPECIFICITY: High levels in brain, lower in spleen and lung.
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DR   EMBL; U20238; AAA93008.1; -; mRNA.
DR   EMBL; AB052362; BAB55802.1; -; Genomic_DNA.
DR   EMBL; AK141511; BAE24707.1; -; mRNA.
DR   EMBL; CH466566; EDL22155.1; -; Genomic_DNA.
DR   EMBL; BC057300; AAH57300.2; -; mRNA.
DR   EMBL; BC068297; AAH68297.1; -; mRNA.
DR   CCDS; CCDS40234.1; -.
DR   RefSeq; NP_033051.2; NM_009025.2.
DR   AlphaFoldDB; Q60790; -.
DR   SMR; Q60790; -.
DR   STRING; 10090.ENSMUSP00000112998; -.
DR   GlyGen; Q60790; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q60790; -.
DR   PhosphoSitePlus; Q60790; -.
DR   EPD; Q60790; -.
DR   jPOST; Q60790; -.
DR   MaxQB; Q60790; -.
DR   PaxDb; 10090-ENSMUSP00000112998; -.
DR   ProteomicsDB; 253171; -.
DR   Pumba; Q60790; -.
DR   Antibodypedia; 26027; 310 antibodies from 32 providers.
DR   DNASU; 19414; -.
DR   Ensembl; ENSMUST00000117551.4; ENSMUSP00000112998.3; ENSMUSG00000031453.17.
DR   GeneID; 19414; -.
DR   KEGG; mmu:19414; -.
DR   UCSC; uc009kye.1; mouse.
DR   AGR; MGI:1197013; -.
DR   CTD; 22821; -.
DR   MGI; MGI:1197013; Rasa3.
DR   VEuPathDB; HostDB:ENSMUSG00000031453; -.
DR   eggNOG; KOG2059; Eukaryota.
DR   GeneTree; ENSGT00940000157953; -.
DR   HOGENOM; CLU_008096_1_1_1; -.
DR   InParanoid; Q60790; -.
DR   OMA; CKEEYMA; -.
DR   OrthoDB; 24454at2759; -.
DR   PhylomeDB; Q60790; -.
DR   TreeFam; TF105302; -.
DR   Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR   BioGRID-ORCS; 19414; 2 hits in 78 CRISPR screens.
DR   PRO; PR:Q60790; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q60790; Protein.
DR   Bgee; ENSMUSG00000031453; Expressed in gonadal fat pad and 266 other cell types or tissues.
DR   ExpressionAtlas; Q60790; baseline and differential.
DR   Genevisible; Q60790; MM.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR   GO; GO:0015278; F:calcium-release channel activity; ISO:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034605; P:cellular response to heat; ISO:MGI.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR   CDD; cd08401; C2A_RasA2_RasA3; 1.
DR   CDD; cd04010; C2B_RasA3; 1.
DR   CDD; cd13371; PH_GAP1_mammal-like; 1.
DR   CDD; cd05134; RasGAP_RASA3; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039360; Ras_GTPase.
DR   InterPro; IPR037774; RASA3_PH.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001562; Znf_Btk_motif.
DR   PANTHER; PTHR10194:SF53; RAS GTPASE-ACTIVATING PROTEIN 3; 1.
DR   PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR   Pfam; PF00779; BTK; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00616; RasGAP; 2.
DR   SMART; SM00107; BTK; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS51113; ZF_BTK; 1.
PE   1: Evidence at protein level;
KW   Acetylation; GTPase activation; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q14644"
FT   CHAIN           2..834
FT                   /note="Ras GTPase-activating protein 3"
FT                   /id="PRO_0000056643"
FT   DOMAIN          1..112
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          123..263
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          330..524
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT   DOMAIN          576..677
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   ZN_FING         679..715
FT                   /note="Btk-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT   BINDING         687
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT   BINDING         698
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT   BINDING         699
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT   BINDING         709
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14644"
FT   MOD_RES         66
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         110
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14644"
FT   MOD_RES         809
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         833
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   CONFLICT        139
FT                   /note="D -> H (in Ref. 1; AAA93008)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   834 AA;  95987 MW;  99FE01CAE4F1AE2F CRC64;
     MAVEEEGLRV FQSVRIKIGE AKNLPSYPGP NKMRDCYCTV NLDQEEVFRT KIVEKSLCPF
     YGEDFYCEIP RSFRHLSFYI FDRDVFRRDS IIGKVAIQKE DLQRYHNRDT WFQLQHVDAD
     SEVQGKVHLE LRLSEVITDT GVVCHKLAAR IFECQGLPIV NGQCDPYATV TLAGPFRSEA
     KKTKVKKKTN NPQFDEVFYF EVTRPCSYSK KSHFDFEEED VDKLEIRVDL WNASNLKFGD
     EFLGELRLPL KILRHSSSYE AWYFLQPRDN GNKSLKPDDL GSLRLNVVYT EDHVFSSEYY
     SPLRDLLLKS ADVEPVSASA AHILGEVCRD KQEAAIPLVR LLLHYGRVVP FISAIASAEV
     KRTQDPNTIF RGNSLTSKCI DETMKLAGMH YLHVTLKPTI EEICQSHKSC EIDPVKLKDG
     ENLENNMESL RQYVDRIFTV ITKSGVSCPT VMCDIFFSLR EAAAKRFQDD LDVRYTAVSS
     FIFLRFFAPA ILSPNLFQLT PHHTDPQTSR TLTLISKTIQ TLGSLSKSKS ASFKESYMAT
     FYEFFNEQKY ADAVKNFLDL ISSSGRRDPK SIEQPILLKE GFMIKRAQGR KRFGMKNFKK
     RWFRLTNHEF TYQKSKGDQP LCNIPIENIL AVERLEEESF RMKNMFQVIQ PERALYIQAN
     NCVEAKDWID ILTKVSQCNQ KRLTVFHPSA YLNGHWLCCR ASSDTAAGCT PCTGGLPANI
     QLDIDGDRET ERIYSLFNLY MGKLEKMQEA CGSKSVYDGP EQEEYSTFVI DDPQETYKTL
     KQVIAGVGTL EQEHAQYRRD KFKKTRYGSQ EHPIGDKSFQ NYIRQQSEIS THSI
//
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