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 03-AUG-2022, entry version 159.
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 iPTMnet; Q60790; -.
DR PhosphoSitePlus; Q60790; -.
DR EPD; Q60790; -.
DR jPOST; Q60790; -.
DR MaxQB; Q60790; -.
DR PaxDb; Q60790; -.
DR PRIDE; Q60790; -.
DR ProteomicsDB; 253171; -.
DR Antibodypedia; 26027; 294 antibodies from 32 providers.
DR DNASU; 19414; -.
DR Ensembl; ENSMUST00000117551; ENSMUSP00000112998; ENSMUSG00000031453.
DR GeneID; 19414; -.
DR KEGG; mmu:19414; -.
DR UCSC; uc009kye.1; mouse.
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; FDHSLNN; -.
DR OrthoDB; 145372at2759; -.
DR PhylomeDB; Q60790; -.
DR TreeFam; TF105302; -.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR BioGRID-ORCS; 19414; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q60790; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q60790; protein.
DR Bgee; ENSMUSG00000031453; Expressed in gonadal fat pad and 264 other tissues.
DR ExpressionAtlas; Q60790; baseline and differential.
DR Genevisible; Q60790; MM.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the 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 GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR CDD; cd13371; PH_GAP1_mammal-like; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
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; PTHR10194; 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; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
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
