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Database: UniProt
Entry: H2SVF2_TAKRU
LinkDB: H2SVF2_TAKRU
Original site: H2SVF2_TAKRU 
ID   H2SVF2_TAKRU            Unreviewed;      1064 AA.
AC   H2SVF2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=SLIT-ROBO Rho GTPase activating protein 1 {ECO:0000313|Ensembl:ENSTRUP00000016390.3};
GN   Name=SRGAP1 {ECO:0000313|Ensembl:ENSTRUP00000016390.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000016390.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000016390.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000016390.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; H2SVF2; -.
DR   STRING; 31033.ENSTRUP00000076243; -.
DR   Ensembl; ENSTRUT00000016462.3; ENSTRUP00000016390.3; ENSTRUG00000006667.3.
DR   GeneTree; ENSGT00950000182824; -.
DR   Proteomes; UP000005226; Chromosome 9.
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; 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:SF15; SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 1; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          22..312
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          462..652
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          701..760
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          768..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          965..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..791
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..879
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1018
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1054
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1064 AA;  121235 MW;  5176096D813DB90D CRC64;
     RGNPTHLKPH KEPLGVICLH ILPIRAQLVE QQKCLDQQTD MRVQLLQDLQ DFFRKKSEIE
     MEYSRNLEKL AERFMAKTRS TKDHQQYKDQ NLLSPVNCWY LLLNQVRRES KDHATLSDIY
     LNNVIMRFMQ ISEDSTRLLK KSKEIAFQLQ EDLMKVLNEL YTVMKTYHMY HSESISAESK
     LKEAEKQEEK QIGRGDQVFS IRMEDKYQRR SSVKKIEKMK EKRQAKYSEN KLKSIKARNE
     YLLTLEASNS SLFKYYIHDL SDLIDCCDLG YHASLNRALR TYLSAEYNLE TSRHEGLDII
     ENAVDSLDPR SDRQRFMEMY PTAFCPPAKF EFQSHMGDEV CQISLQPPVN GELILRFQQL
     QSRLATLKIE NEEIKKTSEA TLTTIQDMVT IEDYDVSECF HHSRSTESVR STVSETYLSK
     PSIAKRRANQ QETEQFYFMK FREYLEGSNL ISKLQAKHDF RGRRNSHTRH QDSGQAIPRV
     VESCIRYINL YGLQHQGIFR VSGSQLEVND IKNSFERGND PLTDDESNHD INSVAGVLKL
     YFRGLENPLF PKERFNDLLA CIRIENLYER ALYIRKILLT IPRSVLIVMR YLFAFLNHLS
     QYSDENMMDT YNLAICFGPT LMPTPESQDQ VSCQAHVNEI IKTIIIHHET IFPDTKELDG
     PVYEKCMAGG DYCESPFSEH GALEEVENEG GTETHTSEDE GEPIEAIAKF DYVGRSSREL
     SFKKGASLLL YQRASEDWWE GRHNGIDGLV PHQYIVVQDV DDNFSDTLSQ KADSEASSGH
     TGEDRCSGKD MAPPTDTRIS EAYITSRHKK RSDPPSRRPP ACPGEVHCMV HPSQHGHGGH
     GGTPELGSPV ISHFSPRDMR RTHNHVSTDS PERRRRTGHG SLNNISRHES LKKMESPPIR
     RSTSSGQYTG FTDVHRHHSG KALDPETIAQ DIEETMNTAL NELRELERQS SAKHAPDVVL
     DTLEQRQTSG GGSGGGPTPA SSGDSLSPIH GVMLRSTANT EPPIRRSISS TSDTMSTFKP
     VVAPRMGVQL KPPALRPKPL VVPKSSPAPQ PPAPQDAQDK SCTM
//
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