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
//