ID E9PXD2_MOUSE Unreviewed; 1543 AA.
AC E9PXD2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Rho GTPase-activating protein 7 {ECO:0000256|ARBA:ARBA00014465};
DE AltName: Full=Rho-type GTPase-activating protein 7 {ECO:0000256|ARBA:ARBA00030675};
DE AltName: Full=START domain-containing protein 12 {ECO:0000256|ARBA:ARBA00032733};
DE AltName: Full=StAR-related lipid transfer protein 12 {ECO:0000256|ARBA:ARBA00030542};
GN Name=Dlc1 {ECO:0000313|Ensembl:ENSMUSP00000132812.3,
GN ECO:0000313|MGI:MGI:1354949};
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|Ensembl:ENSMUSP00000132812.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000132812.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000132812.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] {ECO:0000313|Ensembl:ENSMUSP00000132812.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000132812.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
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DR RefSeq; NP_001181869.1; NM_001194940.2.
DR RefSeq; XP_006509229.1; XM_006509166.3.
DR SMR; E9PXD2; -.
DR jPOST; E9PXD2; -.
DR MaxQB; E9PXD2; -.
DR ProteomicsDB; 367680; -.
DR Antibodypedia; 22182; 270 antibodies from 36 providers.
DR Ensembl; ENSMUST00000163663.3; ENSMUSP00000132812.3; ENSMUSG00000031523.17.
DR GeneID; 50768; -.
DR UCSC; uc009llr.2; mouse.
DR AGR; MGI:1354949; -.
DR CTD; 10395; -.
DR MGI; MGI:1354949; Dlc1.
DR VEuPathDB; HostDB:ENSMUSG00000031523; -.
DR GeneTree; ENSGT00950000183061; -.
DR HOGENOM; CLU_004367_1_0_1; -.
DR OrthoDB; 2883046at2759; -.
DR PhylomeDB; E9PXD2; -.
DR BioGRID-ORCS; 50768; 0 hits in 79 CRISPR screens.
DR ChiTaRS; Dlc1; mouse.
DR Proteomes; UP000000589; Chromosome 8.
DR Bgee; ENSMUSG00000031523; Expressed in left lung lobe and 226 other cell types or tissues.
DR ExpressionAtlas; E9PXD2; baseline and differential.
DR Genevisible; E9PXD2; MM.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04375; RhoGAP_DLC1; 1.
DR CDD; cd09591; SAM_DLC1; 1.
DR Gene3D; 1.10.287.2070; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR12659:SF2; RHO GTPASE-ACTIVATING PROTEIN 7; 1.
DR PANTHER; PTHR12659; RHO-TYPE GTPASE ACTIVATING PROTEIN; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Proteomics identification {ECO:0007829|MaxQB:E9PXD2,
KW ECO:0007829|PeptideAtlas:E9PXD2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 1093..1299
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1329..1511
FT /note="START"
FT /evidence="ECO:0000259|PROSITE:PS50848"
FT REGION 390..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1543 AA; 172954 MW; B2CB5B2ECDC4F521 CRC64;
MSVAIRKRSW EEHVTQQTEQ PFISDEYDIA CHHGLASDSL EGRMEKDATL NVDHKEKCAS
LPDRCCGSET RDFPGRPMGH IAQEVDESDS QEGEERFLSL EASTETLVHI SDEDTDSDLN
LINDSQILTP QRHERDSQDS VKGAGSFMKT LSTMQSSQDS HNTWRMAGKA DMSPAEGSGE
RKDVEAINKS LGLCKNTSAD ETKDVPIGNT FQSLNTEDDV TPKTLLLDSS VLIEDVTPET
QLLDSAVITQ QCRKSDFPKD DQENNRHHVL EEDVLAAPYV DRGLPLLKAD CRSSLLQPPS
CPGGMSAEND LEKSGFSEYQ NKSTLGVSRE DGMQCLHLRG PVTTQETVDN QVRLRKRKET
REDRDRTRLD SMVLLIMKLD QLDQDIENAL STASSPSSTP TNLRRHVPDL ESGSESRTDS
MAVNQTQVNL SSESTDPSST PGSNSGTKPK AMAAPCVGEK EMAEIEAKEA CDWLRVTGFP
QYAQLYEDLL FPIDIALVKR EHDFLDRDAI EALCRRLNTL NKCAVMKLEI SPHRKRSEDS
DEDEPCAISG KWTFQRDSKR WSRLEEFDVF SPKQDPIPGS PDNSRLQSAT SHESMLTDLS
EHQEVASVRS LSSTSSSVPT HAAHSGDATT PRTNSVISVC SSGHFVGNDD SFSSLPSPKE
LSSFSFSMKG HHEKNTKSKT RSLLKRMESL KLKGSHHSKH KAPSKLGLII SAPILQEGMD
EAKLKQLNCV EISALNGNHI NVPMVRKRSV SNSTQTSSSS SQSETSSAVS TPSPVTRTRS
LSTCNKRVGM YLEGFDPFSQ STLNNVTEQN YKNRESYPED TVFYIPEDHK PGTFPKALSH
GSFCPSGNSS VNWRTGSFHG PGHLSLRREN SHDSPKELKR RNSSSSLSSR LSIYDNVPGS
ILYSSSGELA DLENEDIFPE LDDILYHVKG MQRIVNQWSE KFSDEGDSDS ALDSVSPCPS
SPKQIHLDVD HDRRTPSDLD STGNSLNEPE EPTDIPERRD SGVGASLTRC NRHRLRWHSF
QSSHRPSLNS VSLQINCQSV AQMNLLQKYS LLKLTALLEK YTPSNKHGFS WAVPKFMKRI
KVPDYKDRSV FGVPLTVNVQ RSGQPLPQSI QQAMRYLRNH CLDQVGLFRK SGVKSRIQAL
RQMNESAEDN VNYEGQSAYD VADMLKQYFR DLPEPLMTNK LSETFLQIYQ YVPKDQRLQA
IKAAIMLLPD ENREVLQTLL YFLSDVTAAV KENQMTPTNL AVCLAPSLFH LNTLKRENSS
PRVMQRKQSL GKPDQKDLNE NLAATQGLAH MIAECKKLFQ VPEEMSRCRN SYTEQELKPL
TLEALGHLNS DQPADYRHFL QDCVDGLFKE VKEKFKGWVS YPTSEQAELS YKKVSEGPPL
RLWRSTIEVP AAPEEILKRL LKEQHLWDVD LLDSKVIEIL DSQTEIYQYV QNSMAPHPAR
DYVVLRTWRT NLPRGACALL LTSVDHDRAP VAGVRVNVLL SRYLIEPCGS GKSKLTYMCR
ADLRGHMPEW YSKSFGHLCA AEVVKIRDSF SNQNTESKDT RSR
//
