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Database: UniProt
Entry: E9QN14_MOUSE
LinkDB: E9QN14_MOUSE
Original site: E9QN14_MOUSE 
ID   E9QN14_MOUSE            Unreviewed;      1075 AA.
AC   E9QN14;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   SubName: Full=SLIT-ROBO Rho GTPase activating protein 3 {ECO:0000313|Ensembl:ENSMUSP00000108794.3};
GN   Name=Srgap3 {ECO:0000313|Ensembl:ENSMUSP00000108794.3,
GN   ECO:0000313|MGI:MGI:2152938};
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:ENSMUSP00000108794.3, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:15345747}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000108794.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000108794.3,
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:ENSMUSP00000108794.3}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000108794.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   RefSeq; XP_006506208.1; XM_006506145.1.
DR   AlphaFoldDB; E9QN14; -.
DR   SMR; E9QN14; -.
DR   MaxQB; E9QN14; -.
DR   PeptideAtlas; E9QN14; -.
DR   ProteomicsDB; 348835; -.
DR   Antibodypedia; 25344; 150 antibodies from 20 providers.
DR   DNASU; 259302; -.
DR   Ensembl; ENSMUST00000113169.9; ENSMUSP00000108794.3; ENSMUSG00000030257.17.
DR   GeneID; 259302; -.
DR   UCSC; uc009dei.1; mouse.
DR   AGR; MGI:2152938; -.
DR   CTD; 9901; -.
DR   MGI; MGI:2152938; Srgap3.
DR   VEuPathDB; HostDB:ENSMUSG00000030257; -.
DR   GeneTree; ENSGT00950000182824; -.
DR   BioGRID-ORCS; 259302; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Srgap3; mouse.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000030257; Expressed in subiculum and 228 other cell types or tissues.
DR   ExpressionAtlas; E9QN14; baseline and differential.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07684; F-BAR_srGAP3; 1.
DR   CDD; cd04383; RhoGAP_srGAP; 1.
DR   CDD; cd11955; SH3_srGAP1-3; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035648; srGAP1/2/3_SH3.
DR   PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR14166:SF8; SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 3; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|EPD:E9QN14,
KW   ECO:0007829|MaxQB:E9QN14};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          19..314
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          482..670
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          720..779
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          785..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          359..386
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        785..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1075
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1075 AA;  121724 MW;  D36C31B18B28C76A CRC64;
     MSSQTKFKKD KEIIAEYEAQ IKEIRTQLVE QFKCLEQQSE SRLQLLQDLQ EFFRRKAEIE
     LEYSRSLEKL AERFSSKIRS SREHQFKKDQ YLLSPVNCWY LVLHQTRRES RDHATLNDIF
     MNNVIVRLSQ ISEDVIRLFK KSKEIGLQMH EELLKVTNEL YTVMKTYHMY HAESISAESK
     LKEAEKQEEK QFNKSGELSM NLLRHEDRPQ RRSSVKKIEK MKEKRQAKYS ENKLKCTKAR
     NDYLLNLAAT NAAISKYYIH DVSDLIDCCD LGFHASLART FRTYLSAEYN LETSRHEGLD
     VIENAVDNLD SRSDKHTVMD MCSQVFCPPL KFEFQPHMGD EVCQVSAQQP VQTELLMRYH
     QLQSRLATLK IENEEVRKTL DATMQTLQDM LTVEDFDVSD AFQHSRSTES IKSAASETYM
     SKINIAKRRA NQQETEMFYF TKFKEYVNGS NLITKLQAKH DLLKQTLGEG ERAECGTTRG
     RRNARTRNQD SGQAIPLVVE SCIRFINLYG LQQQGIFRVP GSQVEVNDIK NSFERGEDPL
     VDDQNERDIN SVAGVLKLYF RGLENPLFPK ERFQDLISTI KLENPADRVH PIQQILITLP
     RVVIVVMRYL FAFLNHLSQY SDENMMDPYN LAICFGPTLM HIPDGQDPVS CQAHVNEVIK
     TIIIHHEAIF PSPRELEGPV YEKCMAGGEE YCDSPHSEPG TIDEVDHDNG TEPHTSDEEV
     EQIEAIAKFD YVGRSPRELS FKKGASLLLY HRASEDWWEG RHNGVDGLIP HQYIVVQDMD
     DAFSDSLSQK ADSEASSGPL LDDKASSKND LQSPTEHISD YGFGGVMGRV RLRSDGAAIP
     RRRSGGDTHS PPRGLGPSID TPPRAAACPS SPHKIPLSRG RIESPEKRRM ATFGSAGSIN
     YPDKKALTEG LSMRSTCGST RHSSLGDHKS LEAEALAEDI EKTMSTALHE LRELERQNTV
     KQAPDVVLDT LEPLKNPPGP ISSEPASPLH TIVIRDPDAA MRRSSSSSTE MMTTFKPALS
     ARLAGAQLRP PPMRPVRPVV QHRSSSSSSS GVGSPAVTPT EKMFPNSSSD KSGTM
//
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