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Database: UniProt
Entry: A0A3Q1EWY9_9TELE
LinkDB: A0A3Q1EWY9_9TELE
Original site: A0A3Q1EWY9_9TELE 
ID   A0A3Q1EWY9_9TELE        Unreviewed;       796 AA.
AC   A0A3Q1EWY9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Rho GTPase-activating protein 44-like {ECO:0000313|Ensembl:ENSAPOP00000008649.1};
GN   Name=ARHGAP44 {ECO:0000313|Ensembl:ENSAPOP00000008649.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000008649.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000008649.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1EWY9; -.
DR   STRING; 80966.ENSAPOP00000008649; -.
DR   Ensembl; ENSAPOT00000002896.1; ENSAPOP00000008649.1; ENSAPOG00000010871.1.
DR   GeneTree; ENSGT00940000157296; -.
DR   InParanoid; A0A3Q1EWY9; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
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   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR047165; RHG17/44/SH3BP1-like.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1.
DR   PANTHER; PTHR14130:SF13; RHO GTPASE-ACTIVATING PROTEIN 44; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT   DOMAIN          14..248
FT                   /note="BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51021"
FT   DOMAIN          254..444
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          156..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..686
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..731
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   796 AA;  87084 MW;  F394FBE66D408379 CRC64;
     MKKQFNRMRQ LANQTVGRAE KTEVLSEDLL QVEKRLDLVK QVTHSTHKKL TACLQGQQGT
     DMEKRSKKLP LMILAQCMEE GAAVLGDDSL LGKMLKLCGE TEEKLAQELI QFEFQIERDV
     VEPLYVLAEV DIPNIQKQRK HLAKLVLDMD SARTRFQQSS KSSSHPSTLQ PGAKSESLRE
     EMEESANRME ICRDQLSADM YNFVAKEIDY ANYFQTLIET QAEYHRKSLE ILHSVLPQIK
     AHQEAWVEKP SFGKSLEEHL NISGREIAFP IEACVTMLLE CGMQEEGLFR VAPSASKLKK
     LKASLDCGVL DVQEYSSDPH AIAGALKSYL RELPEPLMTI ELYDEWIQAS NVQDMDKRLQ
     ALMAACEKLP TDNLNNFRYL IKFLAKLSEY QDANKMTPGN MAIVLGPNLL WTHTEPNMTE
     MMTTVSLQIV GIIEPIIQHA DWFFPGEIEF NLTGSYGSPI HTNHNSNYSS MPSPDMDQSD
     RKQQHDQSRR PLSVATDNMM LEFYKKDGIR KIQSMGVRVM DTSWVSRKGS STLARKASST
     PPGMQGPGSP ADTLIPEQPG ELATSPSATP PPGERICSLK SKELSPVIGH KAIQVAGPTV
     PPSSSPQSSS QSPHSTEHSP HTLRKGSKKL APVPPKVPYV PSGGMSDQST GQPSPVSLSP
     TPPSTPSPYG LACPPGQVPP SSPGQTPLGT PHSLSSPPSL TGTLTKSRPA PKPRQRPSLP
     PPQPPTAPPG FTGSAMAPVP QPLEQGLLDG LSPGESMSTG KHQPLATTPP PPPQVGLQRP
     SLRLAVALSN GDGGRV
//
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