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Database: UniProt
Entry: A0A3Q1H5L5_ANATE
LinkDB: A0A3Q1H5L5_ANATE
Original site: A0A3Q1H5L5_ANATE 
ID   A0A3Q1H5L5_ANATE        Unreviewed;       892 AA.
AC   A0A3Q1H5L5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Rho GTPase activating protein 4b {ECO:0000313|Ensembl:ENSATEP00000002774.2};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000002774.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000002774.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1H5L5; -.
DR   Ensembl; ENSATET00000002802.2; ENSATEP00000002774.2; ENSATEG00000001995.2.
DR   GeneTree; ENSGT00950000182824; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07656; F-BAR_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:SF16; RHO GTPASE-ACTIVATING PROTEIN 4; 1.
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   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
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:UP000265040};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          19..303
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          489..675
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          714..773
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          180..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          7..34
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        387..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   892 AA;  100449 MW;  C946F5BBA1E4732E CRC64;
     MTSHGKLRKE KGSLAEYESQ MKDLRTQLAD QIKILDSQVD VKQQQLSDLS EFLRRRGDIE
     AEYARALDKL TERFTHKTKK KEQWGQSVCQ VWSVLLTQTR LESREHAALG DTCCNTLTQR
     LVHSTEDTHR LHKRSKEVGT QMQDELLKVT NELQMALKTY NQYHTDCLIA EGKLKEAERL
     EERHTGKSSE LGPGQSGGQR RSSVKKMERL MEKRHGRVQE TQLKCTKARN DYLLNLAAAN
     AAMNKYYLQD VSTLIDCCDL GFHLSVERVM KCYLASRWRI QKTEETGLKQ LEAAVTSLDQ
     GGDRDGLLQQ HDAAFCLPFK FNYHPHEGDQ VCEVSAESQV RYELETRFQQ LQSRLAAVTL
     ETEEISKTLK ATLTALLDTI CDSDCNPSPD VPSTQSHEPP GGSTAPKLTL AKRRANQQET
     ETYYFTKVKE FLNSSSLASK LQAKHDLLQY AIQKAEAVDS DPSRVQCARS VRVRKSRPVS
     QFCHTLFNTD ILSYIQSSGQ QIPVVVESCI RFINLHGLHH EGIFRVPGSQ RDVNLLRDAF
     ERGEDPLSDS ECDLDSVAGV LKLYFRNLEP PLFPYDSYSQ LLECVQIEEE AEKAAQIKAI
     HSTFPRPLLV VMRYLFAFLN HVSQYSDENM MQPYNLAVCF GPSLLRGTDS DDAVARQPQV
     NDLVKTMILQ HDIIFPSQSE LPGPVYEKHM TLEQEYCEPI TEEGDGETEH LPSEDEWEAV
     AMFDYVARSP AELSFKQGDL ITLHSKASCD WWRGEVGGVK GLIPHKYISV LEGNARNTKS
     LSFCVRPDRM RVNSDSASLP GRQRGSEGSP SRKPPTSPAT RHLPEMINRQ MNSVFKELLS
     RQPPVQPATF ASPAAPSSSS SSSSSSSLPQ AAPSAKKVGF GLRGRALFRP VD
//
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