RASL1_MOUSE
ID RASL1_MOUSE Reviewed; 799 AA.
AC Q9Z268; Q99K69;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=RasGAP-activating-like protein 1 {ECO:0000305};
DE AltName: Full=RAS protein activator like 1 {ECO:0000312|MGI:MGI:1330842};
DE AltName: Full=Ras GTPase-activating-like protein {ECO:0000303|PubMed:9751798};
GN Name=Rasal1 {ECO:0000312|MGI:MGI:1330842};
GN Synonyms=Rasal {ECO:0000303|PubMed:9751798};
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].
RX PubMed=9751798; DOI=10.1016/s0378-1119(98)00394-1;
RA Allen M., Chu S., Brill S., Stotler C., Buckler A.;
RT "Restricted tissue expression pattern of a novel human rasGAP-related gene
RT and its murine ortholog.";
RL Gene 218:17-25(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Probable inhibitory regulator of the Ras-cyclic AMP pathway.
CC Plays a role in dendrite formation by melanocytes.
CC {ECO:0000250|UniProtKB:O95294}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
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DR EMBL; AF086714; AAD09007.1; -; mRNA.
DR EMBL; BC005418; AAH05418.1; -; mRNA.
DR EMBL; CH466529; EDL19757.1; -; Genomic_DNA.
DR CCDS; CCDS19623.1; -.
DR RefSeq; NP_038860.2; NM_013832.4.
DR RefSeq; XP_006530272.1; XM_006530209.3.
DR RefSeq; XP_006530273.1; XM_006530210.2.
DR AlphaFoldDB; Q9Z268; -.
DR SMR; Q9Z268; -.
DR BioGRID; 202598; 11.
DR IntAct; Q9Z268; 6.
DR STRING; 10090.ENSMUSP00000031606; -.
DR iPTMnet; Q9Z268; -.
DR PhosphoSitePlus; Q9Z268; -.
DR SwissPalm; Q9Z268; -.
DR EPD; Q9Z268; -.
DR MaxQB; Q9Z268; -.
DR PaxDb; Q9Z268; -.
DR PeptideAtlas; Q9Z268; -.
DR PRIDE; Q9Z268; -.
DR ProteomicsDB; 254988; -.
DR Antibodypedia; 31222; 239 antibodies from 32 providers.
DR DNASU; 19415; -.
DR Ensembl; ENSMUST00000031606; ENSMUSP00000031606; ENSMUSG00000029602.
DR Ensembl; ENSMUST00000156722; ENSMUSP00000123266; ENSMUSG00000029602.
DR GeneID; 19415; -.
DR KEGG; mmu:19415; -.
DR UCSC; uc008zhr.2; mouse.
DR CTD; 8437; -.
DR MGI; MGI:1330842; Rasal1.
DR VEuPathDB; HostDB:ENSMUSG00000029602; -.
DR eggNOG; KOG2059; Eukaryota.
DR GeneTree; ENSGT00940000158715; -.
DR HOGENOM; CLU_008096_0_0_1; -.
DR InParanoid; Q9Z268; -.
DR OMA; HQQDVKY; -.
DR OrthoDB; 145372at2759; -.
DR PhylomeDB; Q9Z268; -.
DR TreeFam; TF105302; -.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR BioGRID-ORCS; 19415; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9Z268; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z268; protein.
DR Bgee; ENSMUSG00000029602; Expressed in dentate gyrus of hippocampal formation granule cell and 68 other tissues.
DR ExpressionAtlas; Q9Z268; baseline and differential.
DR Genevisible; Q9Z268; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; 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:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR CDD; cd05135; RasGAP_RASAL; 1.
DR Gene3D; 1.10.506.10; -; 1.
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; IPR028555; RASAL1.
DR InterPro; IPR037776; RASAL_RasGAP.
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 PANTHER; PTHR10194:SF3; PTHR10194:SF3; 1.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 1.
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 Calcium; Differentiation; GTPase activation; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..799
FT /note="RasGAP-activating-like protein 1"
FT /id="PRO_0000056646"
FT DOMAIN 1..105
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 116..231
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 300..510
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 565..672
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 674..710
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 694
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 704
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT MOD_RES 400
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 660
FT /note="L -> F (in Ref. 1; AAD09007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 89395 MW; E42239D3B89D8069 CRC64;
MAKSGSLSIR VVEGRALPAK DVSGSSDPYC LVKVDDQVVA RTATIWRSLS PFWGEEYTVH
LPLDFHHLAF YVLDEDTVGH DDIIGKISLS KEAITADPRG IDSWINLSRV DPDAEVQGEV
CLDVKLLEDA RGRCLRCHVR QARDLAPRDI SGTSDPFARV FWGNHSLETS TIKKTRFPHW
DEVLELREAP GTTSPLRVEL WDWDMVGKND FLGMVEFTPQ TLQQKPPNGW FRLLPFPRAE
DSGGSLGALR LKVRLTEDRV LPSQYYQPLM ELLLESVQGP AEEDTTSPLA LLEELASGDC
RQDLATKLVK LFLGRGLAGP FLDYLTRREV ARTNDPNTLF RSNSLASKSM EQFMKLVGMR
YLHEVLRPVI SRVFEEKKYM ELDPCKMDLN RSRRISFKGT PTEEQVRETS LGLLTGYLGS
VVDAIVSSTG RCPLALRLAF KQLQRCVEKR FSGIEHQDVK YLAISGFLFL RFFAPAILTP
KLFDLRDQHA DPQTSRSLLL LAKAVQSIGN LGQQLGQGKE QWLAPLHPFL LQSISRVRDF
LDQLVDVDED EEAGGPACAL VQPSTIVREG FLLKRKEEPG GLATRFAFKK RYFRLSGRDL
SYSKTPEWQV HTSIPLSCIR AVEHVDEGAF QLPHVMQVVT QDGAGTSHTT YLQCKNVNDL
NQWLSALRKA SAPNPGKLVA CHPGAFRSGR WTCCLQAERS AAGCSRTHSA ITLGDWSDPL
DPDAEAQAVY RQLLLGRDQL RLKLLEDSSL DTEVDPGRDS SATDGPCAEV LAQQRAATTH
LLQVLEDLEQ AHEEFQKRG
