SPD2A_DANRE
ID SPD2A_DANRE Reviewed; 1119 AA.
AC Q1LYG0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=SH3 and PX domain-containing protein 2A;
GN Name=sh3pxd2a; ORFNames=si:dkey-82d4.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Adapter protein involved in invadopodia and podosome
CC formation and extracellular matrix degradation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC podosome {ECO:0000250}.
CC -!- DOMAIN: The PX domain is required for podosome localization because of
CC its ability to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) and
CC phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser
CC extent, phosphatidylinositol 4-phosphate (PtdIns(4)P),
CC phosphatidylinositol 5-phosphate (PtdIns(5)P), and phosphatidylinositol
CC 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3
CC domain (By similarity). {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SH3PXD2 family. {ECO:0000305}.
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 EMBL; BX005220; CAK11222.1; -; Genomic_DNA.
DR EMBL; CT737229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005171051.1; XM_005170994.3.
DR AlphaFoldDB; Q1LYG0; -.
DR SMR; Q1LYG0; -.
DR STRING; 7955.ENSDARP00000104186; -.
DR PaxDb; Q1LYG0; -.
DR GeneID; 562018; -.
DR CTD; 562018; -.
DR ZFIN; ZDB-GENE-060503-271; sh3pxd2aa.
DR eggNOG; KOG4773; Eukaryota.
DR InParanoid; Q1LYG0; -.
DR OrthoDB; 1183210at2759; -.
DR PhylomeDB; Q1LYG0; -.
DR TreeFam; TF329347; -.
DR Reactome; R-DRE-8941237; Invadopodia formation.
DR Reactome; R-DRE-9013148; CDC42 GTPase cycle.
DR ChiTaRS; sh3pxd2aa; zebrafish.
DR PRO; PR:Q1LYG0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IMP:ZFIN.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
DR CDD; cd06888; PX_FISH; 1.
DR CDD; cd12074; SH3_Tks5_1; 1.
DR CDD; cd12077; SH3_Tks5_2; 1.
DR CDD; cd12079; SH3_Tks5_3; 1.
DR CDD; cd12019; SH3_Tks5_4; 1.
DR CDD; cd12020; SH3_Tks5_5; 1.
DR Gene3D; 3.30.1520.10; -; 1.
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; IPR034917; SH3PXD2A.
DR InterPro; IPR035450; SH3PXD2A_SH3_1.
DR InterPro; IPR035452; SH3PXD2A_SH3_2.
DR InterPro; IPR035449; SH3PXD2A_SH3_3.
DR InterPro; IPR035453; SH3PXD2A_SH3_4.
DR InterPro; IPR035454; SH3PXD2A_SH3_5.
DR PANTHER; PTHR15706:SF22; PTHR15706:SF22; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 4.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 5.
DR SUPFAM; SSF50044; SSF50044; 5.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 5.
PE 3: Inferred from homology;
KW Cell junction; Cell projection; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1119
FT /note="SH3 and PX domain-containing protein 2A"
FT /id="PRO_0000278490"
FT DOMAIN 4..128
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 149..208
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 249..308
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 445..504
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 812..871
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1058..1119
FT /note="SH3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 388..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 124906 MW; 84BD40950C5FBB58 CRC64;
MQFRTVLDVK VVDVEKRRNP SKHYVYLINV TYSDSTSHII YRRYSKFFDL QMQILDKFPI
EGGQKDPKKR IIPFLPGKIL FRRSHVRDVA MKRLRFIDDY CRALVRLPPQ ISQSEEVLRF
FETKPDDINP PVEDYGSKRK SGLDSSEPMV LEQYVVVANY ERQENSEISL KAGETVDVIE
KSESGWWFVS TAEEQGWVPA TYLDSQSGTR DDLDLGTSRS GEVTKRRKAH LKRLDRRWTL
GGIVNRQQSR EEKYVSVQAY ASQGKDEIGF EKGVTVEVIQ KNLEGWWYIR YQGKEGWAPA
SYLKKLKDDL SPRKKTLTGP VEIIGNIMEI SNLLNKKAVS EKDIQTDGEA TTPERHISKS
EISLPMPYAP EAGVAPTVVT ALGMNSGSSA TLQENKSRAE PGSPAIARVA PHRVEIGSPN
LRQKPPPRRD ANLAFQLPKP PEAPTVEAEY YTIAEFQSSI SDGISFRGGQ KADVIEKNSG
GWWYVQIGDT EGWAPSSYID KRKKPNLSRR TSTLTRPKVP PPAPPVKKQD SEEGPSLGGS
ASKAPESPQR VYEEPEYDVP ALGFDSELDC NPPKPKTHNS PKPEPRKFEI KSNPAAAERI
AQAGKASPLL KVMTSPLRKR NSLENINKEE VIYENEGFRF SSDDFASGCD SHTPRSLTLG
RKPFGSSSGG GKPLRKVSPD LNRSHSLGRA ERHSSKLFSD ESARNPKREP VMRKDVEIRI
GQSPLARPKP VVRPKPLLTK SEPQSPERMD ISSIRRHLRP TGSLRQGAIR AMRGEDSETA
SVVSSEDSTS SRSTSDLSSV YSKGSRGGES DHESVLFRTT DAYERAQESE LSFPAGVEVE
VLEKQESGWW FVRWGSDEGW VPTFYLEPIK HTHNVGIQES RDSPLVDLGS TNKSNSLEKN
EQRVQALNNL NQQNLRSMSN PSPPIPSKPP GGFSKPTAML NGSSVRMRNG VRQAAVRPQS
VFVSPPQPLK ETNIHTGSLR RNESLGAGDH LRSTGGVRRN SSFTAVRPQP VTDVRVRAGT
TITAPAGSSS PLIAQRNGIP ISTVRPKPIE KMQLIHNNLR EVYVSIADYR GDEETMGFSE
GTSLEVLEKN PNGWWYCQVL DGLQGRKGWV PSNYLERKK
