ID A0A3B4BTI9_PYGNA Unreviewed; 1087 AA.
AC A0A3B4BTI9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=SH3 and PX domains 2A {ECO:0000313|Ensembl:ENSPNAP00000001839.1};
GN Name=SH3PXD2A {ECO:0000313|Ensembl:ENSPNAP00000001839.1};
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:ENSPNAP00000001839.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000001839.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the SH3PXD2 family.
CC {ECO:0000256|ARBA:ARBA00009628}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B4BTI9; -.
DR Ensembl; ENSPNAT00000011475.1; ENSPNAP00000001839.1; ENSPNAG00000008451.1.
DR GeneTree; ENSGT00940000157732; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IEA:InterPro.
DR CDD; cd06888; PX_FISH; 1.
DR CDD; cd12074; SH3_Tks5_1; 1.
DR CDD; cd12077; SH3_Tks5_2; 1.
DR CDD; cd12019; SH3_Tks5_4; 1.
DR CDD; cd12020; SH3_Tks5_5; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 5.
DR InterPro; IPR001655; P47PHOX.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR037961; SH3PXD2_PX.
DR InterPro; IPR035450; SH3PXD2A_SH3_1.
DR InterPro; IPR035452; SH3PXD2A_SH3_2.
DR InterPro; IPR035453; SH3PXD2A_SH3_4.
DR InterPro; IPR035454; SH3PXD2A_SH3_5.
DR PANTHER; PTHR15706:SF22; SH3 AND PX DOMAIN-CONTAINING PROTEIN 2A; 1.
DR PANTHER; PTHR15706; SH3 MULTIPLE DOMAIN; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 4.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00498; P47PHOX.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 5.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 5.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 5.
PE 3: Inferred from homology;
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..123
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 154..213
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 254..313
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 431..490
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 780..839
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1026..1087
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 403..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 120933 MW; 7CB9A9F241914912 CRC64;
MCAVQFEASI LTLCAFSSQV YLINVTYSDS TSHIIYRRYS KFFDLQMQIL DKFPIEGGQK
DPKKRIIPFL PGKILFRRSH VRDVAMKRLR FIDDYCRALV RLPPQISQSE EVLRFFETKP
DDINPPVEDS GAAGRWLTAC FFPSPAGLDS GEPMVLEQYV AVASYERQEN SEISLRAGET
VDVIEKSESG WWFVSTVEEQ GWVPATYLDA QTGTRDDLDL GTSRSGEVTK RRKAHLKRLD
RRWTLGGIVN RQQSREEKYV TLQPYTSQGK DEIGFEKGVT VEVIQKNLEG WWYIRYLGKE
GWAPASYLKK LKDDLSPRKK TLTGPVEIIG NIMEISNLLN KKAVSEKDVQ TDGEPTTPER
HISKSEISLP IPCNAEAEQA MTSSTAPGSP AIARVAPHRV EIGSPNLRQK PPPRRETNLG
FQLPKPPEPP TVEAEYYTIA EFQSCISDGI SFRGGQKADV IEKNSNGWWY VQIGDTEGWA
PCSYIDKRKK PNLSRRSSTL TRPKVPPPAP PVKKQDSEET PFASGCTSKA PESPSRPVYE
EPEYDIPAIG CDLDLDTTAA ERIAQATGKA SPLLLVKSSP FRNEDSLEHA TKEEAIYEND
GFRFSSDDFA CTRESSGGDS DSPRSRTLGR KPLGSSTGGG KSLRDTPDLY RSHSLNRPEK
NSPRSFSDES GRNPKREPVM RKDVEIQIGQ SPSTRPKPVV RPKPLLSKSE PQSPERMDIS
SLRRQLRPTG AIRHGVVRAA RGGEDSETAS VVSSEDSVSS RSNSDLSSIY SKGSRGDSDF
EGSLYRTMDA YERAQESELS FPAGVEVEVL EKQESGWWYV RWGVEEGWAP AFYLEPVRQH
SDVGVPESLD GHLAELSNAS KSNSLEKNEQ RVQALNNLNQ QNVRRLNNPS PPIPSKPPGG
FSKPSTQLNG SGVRMRNGIR QAAVRPQSVF VSPPQPVKDT NLYTGSLRRN ESLGASDHMR
SSGGVRRNSS FTAVRPQPVT DVRLRSGTTT AAPAGSSSPL IAHRNGIPVS TVKPKPIDKS
NLIHNNLREI YVSIADYRGD EETMGFPEGT SLEVLEKNPN GWWYCQVLDG LQGRKGWVPS
NYLERKK
//