ID I3M7G8_ICTTR Unreviewed; 1063 AA.
AC I3M7G8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=SLIT-ROBO Rho GTPase activating protein 2 {ECO:0000313|Ensembl:ENSSTOP00000005559.3};
GN Name=Srgap2 {ECO:0000313|Ensembl:ENSSTOP00000005559.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000005559.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000005559.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR EMBL; AGTP01058204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01058205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01058206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01058207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01058208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01058209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01058210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3M7G8; -.
DR Ensembl; ENSSTOT00000006217.3; ENSSTOP00000005559.3; ENSSTOG00000006198.3.
DR GeneTree; ENSGT00950000182824; -.
DR HOGENOM; CLU_048287_0_0_1; -.
DR TreeFam; TF315892; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07682; F-BAR_srGAP2; 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:SF6; SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 2; 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 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 22..325
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 488..671
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 181..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..397
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 181..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 119880 MW; BAC76BB54A8A9F35 CRC64;
MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ DFFRKKAEIE
MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN LLLNQVKRES RDHTTLSDIY
LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ DDLMKVLNEL YSVMKTYHMY NADSISAQSK
LKEAEKQEEK QIGKSVKQED RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT
ENKLKAIKAR NEYLLALEAT NASVFKYYIH DLSDLIDQCC DLGYHASLNR ALRTFLSAEL
NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG DMASQLCAQQ
PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD IVTVEDFDVS DCFQYSNSME
SVKSTVSETF MSKPSIAKRR ANQQETEQFY FTKMKEYLEG RNLITKLQAK HDLLQKTLGE
SECGNSPWRL DSSQAIPLVV ESCIRFISRH GLQHEGIFRV SGSQVEVNDI KNAFERGEDP
LAGDQNDHDM DSIAGVLKLY FRGLEHPLFP KDIFHDLMAC VTMDNLQERA LHIRKVLLVL
PKTTLIIMRY LFAFLNHLSQ FSEENMMDPY NLAICFGPSL MSVPEGHDQV SCQAHVNELI
KTIIIQHENI FPNPKELEGP VYSRGGSMED YCDSPHGETT SAEDSTQDVT AEHHTSDDEC
EPIEAIAKFD YVGRTARELS FKKGASLLLY QRASDDWWEG RHNGIDGLIP HQYIVVQDTE
DGVVERSSPK SEIEVISEPP EEKVTARAGA SCPSGGHVAD IYLANINKQR KRPESGSIRK
TFRSDSHGLS SSLTDSSSPG VGASCRPSSQ PIMSQSLPKE GPDKCSISGH GSLNSISRHS
SLKNRLDSPQ IRKTATAGRS KSFNNHRPMD PEVIAQDIEA TMNSALNELR ELERQSSVKH
TPDVVLDTLE PLKTSPVVAP TSEPSSPLHT QLLKDPEPAF QRSASTAGDI ACAFRPVKSV
KMAAPVKPPA TRPKPTVFPK TNATSPGVNS SASPQSTDKS CTV
//