ID A0A093I8Q9_EURHL Unreviewed; 1048 AA.
AC A0A093I8Q9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 18-JUN-2025, entry version 46.
DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 1 {ECO:0000256|ARBA:ARBA00073473};
DE AltName: Full=Rho GTPase-activating protein 13 {ECO:0000256|ARBA:ARBA00083891};
DE Flags: Fragment;
GN ORFNames=N326_03076 {ECO:0000313|EMBL:KFV99059.1};
OS Eurypyga helias (Sunbittern) (Ardea helias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Phaethontimorphae;
OC Eurypygiformes; Eurypygidae; Eurypyga.
OX NCBI_TaxID=54383 {ECO:0000313|EMBL:KFV99059.1, ECO:0000313|Proteomes:UP000054232};
RN [1] {ECO:0000313|EMBL:KFV99059.1, ECO:0000313|Proteomes:UP000054232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N326 {ECO:0000313|EMBL:KFV99059.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase-activating protein for RhoA and Cdc42 small GTPases.
CC Together with CDC42 seems to be involved in the pathway mediating the
CC repulsive signaling of Robo and Slit proteins in neuronal migration.
CC SLIT2, probably through interaction with ROBO1, increases the
CC interaction of SRGAP1 with ROBO1 and inactivates CDC42.
CC {ECO:0000256|ARBA:ARBA00056458}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK557384; KFV99059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093I8Q9; -.
DR Proteomes; UP000054232; 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; cd07683; F-BAR_srGAP1; 1.
DR CDD; cd04383; RhoGAP_srGAP; 1.
DR CDD; cd11955; SH3_srGAP1-3; 1.
DR FunFam; 1.10.555.10:FF:000010; SLIT-ROBO Rho GTPase-activating protein 1 isoform 2; 1.
DR FunFam; 1.20.1270.60:FF:000006; SLIT-ROBO Rho GTPase-activating protein 1 isoform 2; 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; IPR037451; srGAP1_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:UP000054232};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..292
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 484..672
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 721..780
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 448..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 330..357
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 786..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1017
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV99059.1"
FT NON_TER 1048
FT /evidence="ECO:0000313|EMBL:KFV99059.1"
SQ SEQUENCE 1048 AA; 120376 MW; FC7D194D33C5B113 CRC64;
EIRAQLIEQQ KCLEQQTEMR VQLLQDLQDF FRKKSEIEME YSRNLEKLAE RFMAKTRSTK
DHQQYKKDQN LLSPVNCWYL LLNQVRRESK DHATLSDIYL NNVIMRFMQI SEDSTRMFKK
SKEIAFQLHE DLMKVLNELY TVMKTYHMYH AESISAESKL KEAEKQEEKQ IGRSGDPVFH
IRLEERHQRR SSVKKIEKMK EKRQAKYSEN KLKSIKARNE YLLTLEATNA SVFKYYIHDL
SDLIDCCDLG YHASLNRALR TYLSAEYNLE TSRHEGLDII ENAVDSLEPR SDKQRFMEMY
PTAFCPPMKF EFQSHMGDEV CQVTAQQPVQ AELMLRYQQL QSRLATLKIE NEEVKKTTEA
TLQTIQDMVT IEDYDVSECF QHSRSTESVK STVSETYLSK PSIAKRRANQ QETEQFYFMK
FREYLEGSNL ITKLQAKHDL LQRTLGEGHR AEYMTTRPPN LPPKPQKHRK PRPRSQYSAK
LFNGDLESFI KDSGQVIPLI VESCIRFINL YGLQHQGIFR VSGSQVEVND IKNSFERGEN
PLADDQSNHD INSVAGVLKL YFRGLENPVF PKERFNDLIS CIRIDNLYER ALHIRKLLLT
LPRSVLIVMR YLFAFLNHLS QYSDENMMDP YNLAICFGPT LMPVPDIQDQ VSCQAHVNEI
IKTIIIHHEA IFPDAKELDG PVYEKCMAGD DYCDSPYSEH GTLEEVDQDA STEPHTSEDE
CEPIEAIAKF DYVGRSAREL SFKKGASLLL YHRASEDWWE GRHNGIDGLV PHQYIVVQDM
DDTFSDTLSQ KADSEASSGP VTEDKSSSKD MNSPTDRHSD VYLGRQRKRS EPPPPLRRPG
RSSDGHCPVH PPHPLSNSAV ELGSPSLATH CSPRALLQNR NLNADSPERR RRPGHGSLTN
ISRHDSLKKI DSPPIRRSTS SGQYTGFNDH KPLDPESIAQ DIEETMNTAL NELRELERQS
SAKHAPDVVL DTLEQMKNTP TPATSTESLS PLHSVVLRSS EPQIRRSTSS SSDTMSTFKP
MVAPRMGVQL KPPALRPKPI VLPKTNPS
//
