ID G3TDT4_LOXAF Unreviewed; 1013 AA.
AC G3TDT4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=SLIT-ROBO Rho GTPase activating protein 2 {ECO:0000313|Ensembl:ENSLAFP00000012362.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000012362.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000012362.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012362.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000012362.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012362.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; G3TDT4; -.
DR STRING; 9785.ENSLAFP00000012362; -.
DR Ensembl; ENSLAFT00000014763.3; ENSLAFP00000012362.3; ENSLAFG00000014764.3.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000182824; -.
DR InParanoid; G3TDT4; -.
DR OMA; SPLNCWN; -.
DR TreeFam; TF315892; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0060996; P:dendritic spine development; IEA:Ensembl.
DR GO; GO:1904861; P:excitatory synapse assembly; IEA:Ensembl.
DR GO; GO:0021816; P:extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration; IEA:Ensembl.
DR GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR GO; GO:1904862; P:inhibitory synapse assembly; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; 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-RELATED; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..239
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 432..620
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 669..728
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 95..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 277..311
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 95..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 113788 MW; 42D55AC3D0C38E67 CRC64;
RKDQNVLSPV NCWNLLLNQV KRESRDHTTL SDIYLNNIIP RFVQVSEDSG RLFKKSKEVG
QQLQDDLMKV LNELYSVMKT YHMYNADSIS AQSKLKEAEK QEEKQIGKSV KQEDRQTPRS
PDSSSNVRIE EKHVRRSSVK KIEKMKEKRQ AKYTENKLKA IKARNEYLLA LEATNASVFK
YYIHDLSDLI DQCCDLGYHA SLNRALRTFL SAELNLEQSK HEGLDAIENA VENLDATSDK
QRLMEMYNNV FCPPMKFEFQ PHMGDMASQL CAQQPVQSEL VQRCQQLQSR LSTLKIENEE
VKKTMEATLQ TIQDIVTVED FDVSDCFQYS NSMESVKSTV SETFMSKPSI AKRRANQQET
EQFYFTKMKE YLEGRNLITK LQAKHDLLQK TLGESQRTDC SLARIPLAYA KLNLRHVCGL
PSRQILHSIL TVYFSLAFQD SSQTIPLVVE SCIRFISRHG LQHEGIFRVS GSQVEVNDIK
NAFERGEDPL AGDQNDHDMD SIAGVLKLYF RGLEHPLFPK DIFHDLIACV TMDNLQERAT
HIRKVLLALP KTTLIIMRYL FAFLSHLSQF SEENMMDPYN LAICFGPSLM SVPEGHDQVS
CQAHVNELIK TIIIQHENIF PNPRELEGPV YSRGGSMEDY CDSPHGETTS AEDSAQDVTT
EHHMSDDECE PIEAIAKFDY VGRTARELSF KKGASLLLYQ RASDDWWEGR HNGIDGLIPH
QYIVVQDTED GVVERSSPKS EIEVISEPPE EKVTARAGAS CPSGGHIFFL IYKSMLIISL
KRPESGGIRK TFRSESHGLS SSLTDSSSPG LGASCRPSSQ PIMSQSLPKE APDKCSVSGH
GSLNSISRHS SLKNRLDSPQ IRKTVTAGRS KSFNNHRPMD PEVIAQDIEA TMNSALNELR
ELERQSNVKH TPDVVLDTLE PLKTSPVVAP TSEPSSPLHT QLLKDPEPSF QRSASTAGDI
ACTFRPVKSV KMAAPVKPPA TRPKPAVFPK TNATSPAVNS SASPQSSDKS CTV
//
