ID A0A3M0JE46_HIRRU Unreviewed; 1103 AA.
AC A0A3M0JE46;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 3 {ECO:0000256|ARBA:ARBA00073505};
DE AltName: Full=Rho GTPase-activating protein 14 {ECO:0000256|ARBA:ARBA00083893};
DE AltName: Full=WAVE-associated Rac GTPase-activating protein {ECO:0000256|ARBA:ARBA00078662};
GN ORFNames=DUI87_24610 {ECO:0000313|EMBL:RMB99064.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Hirundinidae; Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB99064.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMB99064.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMB99064.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMB99064.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homodimer. Forms a heterooligomer with SRGAP1 and SRGAP2
CC through its F-BAR domain. Interacts with WASF1. Probably interacts with
CC ROBO1. Interacts with FASLG. {ECO:0000256|ARBA:ARBA00064269}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMB99064.1}.
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DR EMBL; QRBI01000151; RMB99064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0JE46; -.
DR STRING; 333673.A0A3M0JE46; -.
DR OrthoDB; 5981864at2759; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
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 FunFam; 1.10.555.10:FF:000013; SLIT-ROBO Rho GTPase activating protein 3; 1.
DR FunFam; 1.20.1270.60:FF:000020; SLIT-ROBO Rho GTPase activating protein 3; 1.
DR FunFam; 2.30.30.40:FF:000005; SLIT-ROBO Rho GTPase-activating protein 1 isoform 2; 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; IPR051627; SLIT-ROBO_RhoGAP.
DR InterPro; IPR035648; srGAP1/2/3_SH3.
DR InterPro; IPR049581; SrGAP3_F-BAR.
DR PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 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|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 58..350
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 542..747
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 797..856
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 506..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 395..422
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 784..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1078
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 124637 MW; 9931C3A531A26AD9 CRC64;
MSAQGKFKKD KEIIADYEAQ VKGVMDSGAV LVSSGRGYGQ SGAVLVSPGR GYGQWGCPEI
RTQLVEQFKC LEQQSESRLQ LLQDLQEFFR RKAEIELEYS RSLEKLAERF SSKIRSSREH
QFKKDQHLLS PVNCWYLVLT QTRRESRDHA TLNDIFMNNV IVRLSQISED VIRLFKKSKE
IGLQMHEELL KVTNELYTVM KTYHMYHAES ISAESKLKEA EKQEEKQFNK SGDISVNLLR
HEDRPQRRSS VKKIEKMKEK RQAKYSENKL KCTKARNDYL LNLAATNAAV SKYYIHDVSD
LIDCCDLGFH ASLARTFRTY LSAEYNLETS RHEGLDIIEN AVDNLDARSD KHTIMDMCNQ
VFCPPLKFEF QPHMGDEVCQ VSAQQPVQTE LLMRYHQLQS RLATLKIENE EVRKTLDATM
QTLQDMLTVE DFDVSDAFQH SRSTESVKSA ASETYMSKIN IAKRRANQQE TEMFYFTKFK
EYLNGSNLIT KLQAKHDLLK QTLGEGERAE CGTTRPPCLP PKPQKMRRPR PLSVYNHKLF
NGNMETFIKD SGQAIPLVVE SCIRYINLYG IAQQFQKSLL KHYSLPGLQQ QGIFRVPGSQ
VEVNDIKNSF ERGEDPLADD QNERDINSVA GVLKLYFRGL ENPLFPKERF QDLISTIKIE
NPAERVHQIQ QIIVTLPRAV IVVMRYLFAF LNHLSQYSDE NMMDPYNLAI CFGPTLMHIP
DGQDPVSCQA HVNEVIKTII IHHEGIFPSH RELEGPVYEK CMTGGEEYCD SPHSEPGTID
EVDHDNGTEP HTSDDEVEQI EAIAKFDYIG RSPRELSFKK GASLLLYHRA SEDWWEGRHN
GVDGLIPHQY IVVQDMDDAF SDSLSQKADS EASSGPLLDD KASSKNDIQS PTDHIMDYGF
GGVMGRGRIE SPEKRRMATF GSAGSINFPD RKALADSHPL RSTCGSTRHS SLGDQKSLEA
EALAEDIEKT MSTALNELRE LERQNTAKQA PDVVLDTLEP MKNPPMGAAN SEPASPLHTI
LIRDPDAAMR RSSSSTAEMM TTFKPALSAR LAGAQLRPPP MRPVRPVVQH RSSSSSSSGV
GSPAVTPTEK LFPSGSADKS GTM
//
