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Database: UniProt
Entry: A0A3B4C0E3_PYGNA
LinkDB: A0A3B4C0E3_PYGNA
Original site: A0A3B4C0E3_PYGNA 
ID   A0A3B4C0E3_PYGNA        Unreviewed;       845 AA.
AC   A0A3B4C0E3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Rho GTPase activating protein 17 {ECO:0000313|Ensembl:ENSPNAP00000004360.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000004360.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000004360.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_017561013.1; XM_017705524.1.
DR   AlphaFoldDB; A0A3B4C0E3; -.
DR   STRING; 42514.ENSPNAP00000004360; -.
DR   Ensembl; ENSPNAT00000007149.1; ENSPNAP00000004360.1; ENSPNAG00000001455.1.
DR   GeneID; 108431999; -.
DR   CTD; 550254; -.
DR   GeneTree; ENSGT00940000156201; -.
DR   OrthoDB; 7959at2759; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd04386; RhoGAP_nadrin; 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   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:SF3; RHO GTPASE-ACTIVATING PROTEIN 17; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
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, ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          14..249
FT                   /note="BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51021"
FT   DOMAIN          255..445
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          468..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          169..196
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        497..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..719
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..752
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..772
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..794
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  91687 MW;  002CE5C67D00E5DC CRC64;
     MKKQFNRMKQ LANQTVGRAE KTEVLSDDLL QIERRMELVR VISHNTHKRL VTCLQGHIGT
     DAEKRHKKLP LTALSQAMQD GGSQLGEESF IGKMMEVCGE AENKLASELM QHEVQIEKDI
     LDPLNQLAEI DIPNILKQRR QLAKLVLDYD SARARWLQAT KSIISGTNTQ ALTAKADSLK
     EEMDEAMNKM ELCKDQLSAD MYNFFSKEGD YACYYVMLLE AQADYHRKSL SVLESVLPTI
     QAQQDSWTEK PAFGTGLDEH LKRSGREIAL PIEACVMMLL ETGMKEEGLF RIAAGASKLK
     KLKAALDCST SQLEEFYSDP HAVAGALKSY LRELPEPLMT YQLYDEWIQA SNVPDPDKRL
     QALWLVCDQL PKNNKANFRY LVKFLAKLAQ ESELNKMTPS NIAIVLGPNL LWAKTEGSLA
     EMAAATSVHV VTIIEPIIQH ADWFFPEDVE FNVSGAFSMP APMINHVNHL TVPDHDSGTT
     ERKRPNSMVG PDGDMPKRDS SSNKLMDHNP RRGSTLTRKQ HASPAFQPPL PPVEAAGTAG
     GQPVAELLLQ QPTSAGTEAC QPSLALGMAA LVAAQQLLAQ HTEELSSKSR DSASTPPAQR
     NGSGGSAQLS VVPPVAGSSG LSPHTARRGT KKPAPAPPKP TNPPSGQLSG QSAPHASSGT
     PQSLSPSPRP LSSSSPNSLS PTQLAVQLTT TPRRHSSNQP PIQAPNHPPP EPPTQVTPPL
     QPKALGQTAG EPTEDPSPPS TPTPPHTPPP MVISPDNTST NAPSQFQSGS LPRSRPVPKP
     RNRPTVPPPP QPHSGGIDTN GICSTAYKMI DAGMPFKGLG RDLATEHQPV TQLKDADLDS
     ESTIL
//
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