ID A0A493TQD4_ANAPP Unreviewed; 1134 AA.
AC A0A493TQD4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=SH3 and PX domains 2A {ECO:0000313|Ensembl:ENSAPLP00000027805.1};
GN Name=SH3PXD2A {ECO:0000313|Ensembl:ENSAPLP00000027805.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000027805.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000027805.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000027805.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A493TQD4; -.
DR STRING; 8840.ENSAPLP00000027805; -.
DR Ensembl; ENSAPLT00000045338.1; ENSAPLP00000027805.1; ENSAPLG00000006691.2.
DR GeneTree; ENSGT00940000157732; -.
DR Proteomes; UP000016666; Chromosome 6.
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; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 5.
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; 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; 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; 3.
DR Pfam; PF07653; SH3_2; 2.
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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..172
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 195..254
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 295..354
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 476..535
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 843..902
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1073..1134
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 431..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 127224 MW; D32753D403A51B09 CRC64;
MKDESLILGA WQGQAQMSAL APSQLLCAAR NLPSLSWSEQ YRIVVYSLLC SWAEGFLQLL
CFANPLPSHT QAKKSSVPKQ PLCLPPKAFL LFPLQMQLLD KFPIEGGQKD PKQRIIPFLP
GKILFRRSHV RDVAVKRLKP IDEYCRALVR LPPHISQCDE VFRFFEARPE DLNPPKEDYG
SSKRKSGADA SSEPMILEQY VVVSNYEKQE NSEISLQAGE VVDVIEKNES GWWFVSTAEE
QGWVPATYLE SQNGTRDDSD INTSKTGEVS KRRKAHLRRL DRRWTLGGIV NRQQSREEKY
VTIQPYASQG KDEIGFEKGV TVEVIQKNLE GWWYIRYLGK EGWAPASYLK KAKDDLPSRK
KNLTGPVEII GNIMEISNLL NKKSSTDKET QAENETSESH ITKKEISLPI LCNDSNGNAM
MTPDKQASKL AQGSPAVARI APQRAQISSP NLRTRPPPRR ESSLGFQLPK PPEPPSVEVE
YYTIAEFQSC ISDGISFRGG QKAEVIEKNS GGWWYVQIGE KEGWAPASYI DKRKKPNLNR
RTSTLTRPKV PPPAPPSKPK DSEEGTTTGM VSSGDTQDSP HKLKYEEPEY DVPAFGFESE
CEVNESHEEG TPEKRLFQPL KPSPVSSLQK AKFKVGESSE DVAHEEETIY ENEGFRRYVE
DTLSNKESSG DSDSQKSSSL SLIRRNSPCS NSPKSSLVKP KIDKNIQPDL GKCHYSRNEE
TKPRSASDVG LRSMPRTGVK KEPAQSPSIR AKPIVRPKPF LNKADSQSQE KMDISTLRRQ
LRPTGQLRGG LKGSRSEESE SPPHTASENQ DDPVRRSSAD LITAPSRAIF CSSHPAKTEQ
ENDSRCFYVT TDSYQKVQDS EICFPAGVEV EVLEKQPSGW WYLKYGDMEG WAPSHYLALP
DNQRETTSAE TDASFARNRK NENKSNSLEK IEKRVQALNT INQSKRATPP IPSKPPGGFS
KTSGPVKMRN GVRQLAVRPQ SVFVSPPPKD NNLSCSLRRN ESLTSTDHLR NVRRNSSFSN
TRLQQGDAKG KQPERSGTDG SETTSNLPTQ RNGIPVSTVR PKPIEKSQFI HNNLKDIYVS
IADYEGDEET AGFQEGVCME VLERNPNGWW YCQIMNGVKP FKGWVPSNYL EKKN
//
