ID F7DB04_ORNAN Unreviewed; 954 AA.
AC F7DB04;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=SH3 and PX domains 2A {ECO:0000313|Ensembl:ENSOANP00000002611.4};
GN Name=SH3PXD2A {ECO:0000313|Ensembl:ENSOANP00000002611.4};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000002611.4, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000002611.4}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000002611.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; F7DB04; -.
DR STRING; 9258.ENSOANP00000002611; -.
DR Ensembl; ENSOANT00000002612.4; ENSOANP00000002611.4; ENSOANG00000001630.5.
DR eggNOG; ENOG502QR1V; Eukaryota.
DR GeneTree; ENSGT00940000157732; -.
DR HOGENOM; CLU_013051_0_0_1; -.
DR InParanoid; F7DB04; -.
DR OMA; ASPEWAH; -.
DR TreeFam; TF329347; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000001630; Expressed in fibroblast and 7 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0002102; C:podosome; IEA:Ensembl.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:Ensembl.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0072675; P:osteoclast fusion; IEA:Ensembl.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:Ensembl.
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; 2.30.30.40; SH3 Domains; 5.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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:SF2; BUD EMERGENCE PROTEIN 1; 1.
DR PANTHER; PTHR15706; SH3 MULTIPLE DOMAIN; 1.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 5.
DR SUPFAM; SSF50044; SH3-domain; 5.
DR PROSITE; PS50002; SH3; 5.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 22..81
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 94..153
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 274..333
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 657..716
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 893..954
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 247..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 954 AA; 104319 MW; 872276132B9AD45A CRC64;
MSSWTESPKK DFTGADASSE PMILEQYVVV SNYEKQENSE LSLQAGEVVD VIEKNESGWW
FVSTSEEQGW VPATYLESQN GTRDDSDINT SKAGEEEKYV TIQPYTSQSK DEIGFEKGVT
VEVIQKNLEG WWYIRYLGKE GWAPASYLKK AKDDLPARKK NLTGPVEIIG NIMEISNLLN
KKTSGDKETQ ADNETADSHI TKKEISLPIL CNDSNGNAMT PDKPASKLAQ GSPAVARIAP
QRAQISSPNL RMRPPPRRES SLGFQLPKPP EPPSVEVEYY TIAEFQSCIS DGISFRGGQK
AEVIDKNSGG WWYVQIGEKE GWAPASYIDK RKKPNVNRRT STLTRPKVPP PAPPSKSKEA
EEGPAPGAPE SQDALPKPRY EEPEYDIPAF GGDSEAEGPE GPPEDAPAEQ RPSPAPRPSP
ASSLQRARFR VGESAEDVAL EEETIYENEG FRPYGEDRES SGDSDSQKST SLSLLRKNSP
TSSSPKPSLL KPQAEKPTQP GLGKTHSSSS FCSISTSAST PTPAPFSPKN REMKPRSASD
VGLRSGAKSS GKKETEPRAP LGSSARAKPS VRPKPFLSKG ESQSQEKMDI STLRRQLRPT
GQLKGGLTGS RSEESASPPP TARERPGESR RRGSADLIRP PARLGTSGRP GSERDQEGGD
AYVTCDSYQK VQDSEISFPA GVEVEVLEKQ DGGWWFVKIG EQEGWAPSHF LVLEENRPRE
TTPARETPTR EASLPPAPSG KDNEGRSNSL EKIEKRVQAL NTINQSKRTM PPIPSKPPGG
FSKTSVKMRN GVRQLAVRPQ SVFVSPPLPK DNTTARALRR NESLMAGDPL RAVRRNASFS
TARSPAGDTG GGSEERAGLE GPEPPVPASR REGIPVSAVR PKPIEKGQFI HNNLKDVYVS
IADYEGDEET AGFQEGVSME VLERNPNGWW YCQIMDGGKP FRGWVPSNYL EKKN
//
