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Database: UniProt
Entry: A0A3Q1D0Y7_AMPOC
LinkDB: A0A3Q1D0Y7_AMPOC
Original site: A0A3Q1D0Y7_AMPOC 
ID   A0A3Q1D0Y7_AMPOC        Unreviewed;      1089 AA.
AC   A0A3Q1D0Y7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=SLIT-ROBO Rho GTPase-activating protein 1-like {ECO:0000313|Ensembl:ENSAOCP00000031624.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000031624.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000031624.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1D0Y7; -.
DR   STRING; 80972.ENSAOCP00000031624; -.
DR   Ensembl; ENSAOCT00000033052.1; ENSAOCP00000031624.1; ENSAOCG00000023449.1.
DR   GeneTree; ENSGT00950000182824; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd04383; RhoGAP_srGAP; 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   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:UP000257160};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          19..319
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          478..676
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          725..784
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          701..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          978..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          357..384
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        801..815
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..842
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..914
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1040
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1089
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1089 AA;  122015 MW;  7EBB68BDFD114079 CRC64;
     MSNSNKSKKD KEILAEYESQ VKDVRTQLVE QQRCLEQQTE MRVQLLQDLQ DFFRKKAEIE
     TEYSRNLEKL AERFMAKTRS TKDHQQYKKD QNLLSPVNCW YLLLNQVRRE SKDHATLSDL
     YLNNVITRLT HISEDSARLL KRSKEIIFQL QEDLMKLLNE LYTVMKTYHM YHAETINAET
     KLREAERQEG RVKGVSGSGG GVEPVFGLRI EERHQRRNAA RKMEKMREKR KAKYSENKLK
     ALKARNEYLL TLEATNASVF KYYIHDLPDI IDCCDLGYHS SLSRSLRTYL SAELSLEASR
     RAGLEVLEGA VEGLDPARDR QRLLGLYPTA FCPPQRFSFQ AHMGDAVTQI ASQPQVQAEL
     TLRLTQLQTR LASLKIENEE VKKTWGATLT TLQDMTVLDD YDVSQSFTHS PSSESVKSSV
     SDGYLNKPSL AKRRANQQET ELFYFTKFRE YLEGSNLISK LQAKHDILKK ALAEGYKAEL
     LTTSRGRKNS HSKHQDSTKA IPLLVESCIR YINLHGLQHQ GIFRVSGSQV EVNDIKNSFE
     RGNDPLIDEE SNHDINSVAG VLKLYFRGLE NPLFPKDRFN DLISCIRIEN MYERAQCIRK
     ILLGVPRATL VVMRYLFAFL NHLSQYSDEN MMDAGNLAIV FGPTLLPTPD TLDQVACQAH
     VNEVIKTVIL NHDNIFPDTK ELPGPVYEKC MTGDQYCESP FSEPGALEEA EPDAGTETQT
     SDEEGEAVEA VARFDYVGRS GRELSFKKGA SLQLFQRASH DWWEGRHNGS IGLVPHQYIV
     VKDRADAMSD TLSQKADSDG GSSSTDDKRS RSELSSPTDI RPPDTYNSHR RKRTDGLFRR
     PLCRSNDNHG NGNVMERSSP PVTGHFSPRE LLLGRGQGLT PPLDSPERRR RSAAVTMTVS
     RHDSLRRPED TPIRRSSSGQ HGFNDNHRSR AIDPDTLAQD IEESVTVALG ELRQLERQGC
     RPAPDVVLDT LEQVKNGPVT ACSSESPSPH STPSTPGTPG TPGTPGTPGT PGTPSPLSPL
     SPISPLPGPP PGPPRPANPS PDALGSFKPV AAARIGAPLR PPALRPKPMV PPKSSTPPLP
     PPLDKSCTM
//
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