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Database: UniProt
Entry: A0A182PV99_9DIPT
LinkDB: A0A182PV99_9DIPT
Original site: A0A182PV99_9DIPT 
ID   A0A182PV99_9DIPT        Unreviewed;      1000 AA.
AC   A0A182PV99;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
OS   Anopheles epiroticus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI010886-PA, ECO:0000313|Proteomes:UP000075885};
RN   [1] {ECO:0000313|Proteomes:UP000075885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AEPI010886-PA}
RP   IDENTIFICATION.
RC   STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI010886-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A182PV99; -.
DR   STRING; 199890.A0A182PV99; -.
DR   EnsemblMetazoa; AEPI010886-RA; AEPI010886-PA; AEPI010886.
DR   VEuPathDB; VectorBase:AEPI010886; -.
DR   OrthoDB; 5476196at2759; -.
DR   Proteomes; UP000075885; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0002039; F:p53 binding; IEA:InterPro.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR047163; ASPP1/2.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR24131:SF10; ANKYRIN-REPEAT, SH3-DOMAIN, AND PROLINE-RICH-REGION CONTAINING PROTEIN, ISOFORM B; 1.
DR   PANTHER; PTHR24131; APOPTOSIS-STIMULATING OF P53 PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   REPEAT          829..861
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          862..887
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          928..991
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          206..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..730
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1000 AA;  110279 MW;  B254094958417AD2 CRC64;
     MAMRQQHQID TQHQMLAAKE QRLRFLKSQE TRNAVSIAEA ERLRRLRERV EAQESKLRRL
     RALRGQVDLQ KTYNVTLGND LDSIRALFSE KEKELTLAVA KVEALTRQLE ELRRDRRGVG
     NGANGISYNV NSNALNYNSS PVAKELEKLR LELAYRNQLS MQQNARLNMQ RETLQQRQIE
     LHSVDKRIIE LQSRINKKRI LNVQNYKFNG GNNSPASGHN NHSKTLQPNA NHPLHSRSSS
     THIIPTHSRT LSRGNIVAVE PFNHVPVKSS SSGDGLNLTL SPSSTGNIND KTLQMTSSTS
     DFMQQQHPQQ APSMIQNYQW DHDAASKMMG GEEAMLLAPE SDEKKLAVRQ QQQQQQYRSR
     FVESNDNVLE TETENGLETK DVQLNMVSND FEMKNNSNSP SSYDNANGMF DFYEKNTHDN
     DFESDSATSL DKGQSNGNNI GANSIGNSSQ DKHHQSIPSQ PKASYNFLQN IPLGNLVVPP
     RKPINSVAPT LAMKPSSTNA ANSGSVNELG AKITSVTRKV PVGIENTGTT NEADQTTAST
     SPNNNIRPAL PPKPNKSSGF GNVGAIVPTT SGNHNSNDEY GNETTVGLSA GGTSNENESS
     SAPFDMPDLS LPGSNNKQSA ANDKLPIKAK PLTIRKHPFL EQPKLKNFTS SFNPNQNAYT
     GMNKFSNASA TQQITNKRKE AAAVETANSE TNDATQYSNY EGESLNDKKH ASDNSEFHVG
     REHPIERLKK LKSGNTNSTD GNGNSEHEIT RRKRNFISMT PDGQGNASGN GIGSGNGVTM
     VGEGSKHKLS RRVSFDPLAL LLDASLEGEL ELVEKTAMQV TNPSAANDEG ITALHNAICA
     GHFEIVKFLV NFGCDVNAQD SDGWTPLHCA ASCNNLPMVK FLVESGACLF AATLSDHETP
     AEKCEEDEEG FDGCSEYLYS IQEKLGILNN GEVHAVFSYE SQQPDELSFF VNDKLTIIRK
     GDESEREWWW ARNSLGNEGY VPRNLLGLHP RLTPSYSDEN
//
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